ӰԺ

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Research at the ӰԺ EPR Center

The research conducted within the EPR Center includes both technological innovation and application of new techniques to biological problems. The main areas of research are free radicals, spin labeling, metal complexes, and metallo proteins.

How Are We Unique?

Technical Expertise

Technical Expertise

All of our faculty are trained in EPR spectroscopy and each utilizes EPR spectroscopy as a major component of their daily research.
Application of Techniques

Application of Techniques

Our faculty are closely involved in the application of the instrumental techniques being developed here at the EPR Center and in making EPR methodology available to the general research community. 
In-House Support

In-House Support

Our expert staff—comprising microwave, electrical, and software engineers, and a machinist—provide in-house support and maintenance for our instruments. 
Collaboration

Collaboration

We welcome collaborations with local users, and those across the country, and we have positioned ourselves to maintain our status as an EPR resource to the scientific community.

Grants

Ending after ~2000, with EPR Center faculty as Principal Investigator

all
S10OD036246_Accordion Pane

S10OD036246
05/01/2024–04/30/2025
PI: Candice S. Klug

A modern Bruker ELEXSYS-II E500 X-band CW (continuous wave) EPR (electron paramagnetic resonance) spectrometer system is requested to replace an outdated and frequently malfunctioning version in the National Biomedical EPR Center at ӰԺ. The enhanced sensitivity and reliability of the new instrument will significantly improve our ability to study critical biological phenomena including protein structure and functional dynamics, mechanisms of novel redox and cancer therapeutic agents, and aid in the design of safer and more effective drugs against a broad spectrum of diseases. This state-of-the-art instrument will ensure the continued success of our NIH-funded research programs while also facilitating new scientific collaborations.

Emergent Technology for Studying the Structure/Function Relationship of Enzymes Using Electron Paramagnetic Resonance

R01GM149568
06/06/2023–03/31/2028
PI: Jason W. Sidabras

Electron paramagnetic resonance (EPR) spectroscopy is a critically important technique in biomedical research with a unique ability to detect naturally occurring or engineered unpaired electrons in complex biological environments. I focus on the development of three technical and method developments that significantly improve X-band EPR sensitivity for three classes of samples: small to medium-sized (0.1–3 nl) protein single crystals, volume-limited frozen samples (85 nl), and microfluidic (500 nl) with microfluidic sample handling. The combination of these prototypes will be easy to use and widely available to the scientific community, enabling a wide range of new applications in biomedical EPR spectroscopy.

Development of High-Throughput, High-Sensitivity EPR Sample Handling Capabilities for Biomedical Research 
R01GM140385
01/01/2021–11/30/2024
MPI: Candice S. Klug, Michael T. Lerch

EPR spectroscopy is a critically important technique in biomedical research with a unique ability to detect naturally occurring or engineered unpaired electrons in complex biological environments. We will develop two innovative EPR spectrometer technologies with outstanding sample sensitivity that are easy to use and widely available to the scientific community. The resulting state-of-the-art prototypes will provide a transformative increase in throughput that will enable a wide range of new applications in biomedical EPR spectroscopy studies including structural biology, metalloprotein research, redox biology, rational drug design, and clinical diagnostics for a range of disease areas.

Regulation of β2-adrenergic Receptor Signaling by Post-Translational Modifications 

R01GM135581
09/20/2019–08/31/2024
PI: Michael T. Lerch

G-protein-coupled receptors are a large and diverse class of cell surface receptors responsible for regulating nearly every physiological process in the human body and are therefore important targets for drug development. In this project, we aim to elucidate the molecular basis for modulation of β2-adrenergic receptor signaling by two post-translational modifications (PTMs), glycosylation and palmitoylation, using a complementary combination of continuous-wave and pulsed electron paramagnetic resonance techniques and functional assays. By detailing the effects of these PTMs on the conformational landscape, the results from these studies will provide insight into the understudied yet critical role of these PTMs as regulators of receptor signaling, thereby increasing researchers' ability to rationally design drugs to achieve the desired therapeutic effect.

Chemoprevention of Lung Cancer by Targeting Lonidamine to Mitochondria

R01CA232433
04/15/2019–03/31/2024
MPI: Ming You, Balaraman Kalyanaraman, Laura Kresty

New and effective preventive agents for lung cancer are urgently needed. Selectively inhibiting cancer cell mitochondrial bioenergetics is a novel preventive strategy for lung cancer that has a great potential. By modifying lonidamine (LON), we created the mitochondria-targeted agent, Mito-LON, as a new, safe and potent preventive agent that robustly inhibits bioenergetics and induces autophagic cell death of cancer cells. We will systematically and thoroughly evaluate the chemopreventive potential of Mito-LON using both in vitro and in vivo models of lung cancer and determine its primary mechanism(s) of action.

Lpt Protein-Mediated Transport of LPS 

R01GM108817
09/01/2014–06/30/2024
PI: Candice S. Klug

Endotoxin, or lipopolysaccharide, from important disease-causing bacteria such as Escherichia coli, Salmonella typhimurium, and Pseudomonas aeruginosa induces severe septic shock in humans and can quickly lead to inflammatory disease and/or death. Endotoxin is required for the survival of these bacteria, thus the proteins and interactions involved in its transport within the bacterium are exciting potential new targets for novel antibiotics. The aim of this project is to use structural biology and microbiology assays to obtain a detailed understanding of how the endotoxin-transport proteins move endotoxin within the cell as a foundation for the future development of inventive antibiotics against pathogenic bacteria.

Type III Effector-Cofactor Dynamics Within the Cellular Environment

R01AI104922
05/23/2013–08/31/2022
MPI: Dara W. Frank, Jimmy B. Feix

Pseudomonas aeruginosa and a variety of bacterial genera deliver effectors directly into host cells via a specialized injection system. Effectors encode toxic enzymatic activities that cause cell death or dysfunction leading to pathology, tissue destruction and poor outcomes for infected individuals. The long-term goals of this research are to identify how a host encoded cofactor, ubiquitin, interacts with the P. aeruginosa effector, ExoU. Mapping this interface will provide information needed to design inhibitors that may be active against a variety of bacteria, most of which are highly resistant to antibiotics.


Chemoprevention of Lung Cancer with Mitochondria-Targeted Honokiol 

R01CA208648
03/01/2017–02/28/2022
MPI: Ming You & Balaraman Kalyanaraman

Chemoprevention of precancerous growths in the lung from progressing to cancer and inhibiting NSCLC's metastasis using novel, potent chemopreventive agents are important strategies to reduce NSCLC mortality. Honokiol (HNK), an active ingredient of the extract of Magnolia bark long popular in traditional Asian medicines, has cancer chemopreventive properties. Here we design a new mitochondria-targeted compound (called Mito- HNK) based on HNK’s structure to facilitate its delivery to mitochondria. We will evaluate the chemopreventive potential of Mito-HNK using both in vitro and in vivo models of lung adenocarcinoma and determine its mechanism of action. At the conclusion of these studies, we will have determined the efficacy of Mito-HNK for inhibiting lung adenocarcinoma progression and metastasis and its suitability for human clinical trials.

Upgrades to a Bruker Q-band E580 Pulse EPR Spectrometer 
S10OD025260
07/01/2019–06/30/2021
PI: Candice S. Klug

The research in this study, which used novel state-of-the-art enhancements to a biophysical spectroscopic technique to enable the study of protein structure and functional dynamics, will lead to a better understanding of the physiology of disease processes such as cardiovascular and pulmonary diseases; cystic fibrosis; diabetes; obesity; behavioral, neurological, and psychiatric disorders; Alzheimer's disease; and cancer. This research will also contribute to the development of novel antibiotics and cancer therapeutic agents, and to the design of safer and more effective drugs targeting a broad spectrum of diseases. Additional avenues of research are expected to be uncovered once the success of the initially proposed projects is evident, fostering further opportunities for new interdisciplinary science.

Small Volume Stopped-Flow EPR for Biomedical Applications
ӰԺ/Advancing a Healthier Wisconsin
12/01/2019–05/31/2021
PI: Candice S. Klug
Lipid Domains in Lens Membranes of a Single Eye: EPR Spin-Labeling Studies
R01EY015526
04/01/2004–05/31/2021
PI: W. Karol Subczynski

Cataracts are a major cause of blindness throughout the world. At present, surgery is the only effective treatment. The reason for the onset of cataracts is unknown, but a great deal of evidence suggests that the presence of high cholesterol and cholesterol bilayer domains in the eye lens helps to maintain transparency and prevent cataract formation. The goal of this study was to understand how fiber-cell plasma membranes in the lens, in particular their lipid bilayer portion, change during aging and cataract formation so that alternative strategies for preventing, slowing the progression, and curing cataracts can be devised and evaluated.

Molecular Mechanisms of Endogenous Modulators of Beta2-Adrenergic Receptor Signal Transduction
ӰԺ Research Affairs Committee
07/01/2018–06/30/2020
PI: Michael T. Lerch
Is ROS Formation Increased During Tumor Growth? Low-Temperature EPR and Bioluminescence Imaging Studies

ӰԺ Cancer Center Pilot Grant
02/01/2019–02/28/2020
PI: Balaraman Kalyanaraman

CYP2E1 Mediated Mitochondrial Injury and Cell Damage in Alcohol Liver Disease

R01AA022986
12/01/2014–11/30/2019
MPI: Narayan Avadhani, Balaraman Kalyanaraman

Alcohol consumption has been implicated in a multitude of human diseases including alcoholic liver disease (ALD), liver cancer, myocardial fibrosis/infarction, pancreatitis, and disorders of the immune, endocrine and reproductive systems and estimated to cost annually over 1.5 billion dollars in the U.S. in terms of lost productivity and cost of health management. This study will advance our understanding of ALD and critical molecular targets affected. A combination of subcellular targeting of antioxidants and enzyme inhibitors and use of humanized mouse models should provide novel insights into the mechanism of the disease and also lead to development of clinically important drugs for treating or reversing the alcohol liver damage.

Tetrahydrobiopterin in Fetal Hypoxic Brain Injury

R01NS081936
07/01/2016–06/30/2019
MPI: Sidhartha Tan, Jeannette Vasquez Vivar

There is a paucity of effective treatments for cerebral palsy and this proposal tested a promising strategy aimed at a preventive cure for this disease. The studies tested the ways at which a vitamin-like co-factor is involved in brain injury. Using surrogate markers of magnetic resonance imaging, this study examined what happens to brain cells in the early critical phase of injury, which seems to determine the eventual course of events leading to movement disorders of cerebral palsy.

Mechanism of Activation and Membrane Interactions of Pseudomonas Toxin ExoU 
R01GM114234
06/01/2015–04/30/2019
PI: Jimmy B. Feix

Pseudomonas aeruginosa is a Gram-negative opportunistic pathogen that is a leading cause of hospital-acquired infections, and is particularly problematic for patients who are immunosuppressed or require mechanical ventilation. P. aeruginosa persists chronically in cystic fibrosis patients, resulting in irreversible lung damage and mortality. The infectivity of P. aeruginosa is significantly enhanced by the Type III secreted toxin, ExoU. Our biochemical and biophysical studies of ExoU were designed to understand its molecular mechanism of activation, facilitating the development of novel inhibitors to reduce tissue damage or sepsis due to P. aeruginosa infection.

National Biomedical EPR Center

P41EB001980
03/01/1997–03/31/2019
PI: Candice S. Klug (transferred from James S. Hyde)

The mission of the National Biomedical EPR Center was to serve the community of EPR spectroscopists by development of advanced EPR instrumentation and new EPR methodologies.

National Biomedical ESR Center

P41RR001008
05/01/1976–02/28/2002
PI: James S. Hyde

The broad aim of the National Biomedical ESR Center was to create and maintain a comprehensive center with balance in all five categories of a research resource—technological research and development, collaborative research, service, training, and dissemination—with expertise in the three main application areas of ESR spectroscopy—free radicals, transition metals, and spin labels—with outstanding competence in ESR development.

Chemoprevention PPG–Chemoprevention of Oral Cancer Resubmission
ӰԺ Cancer Center Pilot Grant
06/01/2017–05/31/2018
PI: Balaraman Kalyanaraman
Development of Biomedical EPR Instrumentation

R01EB002052
07/01/1979–03/31/2016
PI: Candice S. Klug (transferred from James S. Hyde)

Molecular dynamics occur in all biological molecules across a wide range of motional frequencies, some of which are central to biological function. The nitroxide-radical spin-label method, based on EPR, is suitable for the study of molecular dynamics, including dynamics with characteristic motional periods of a millisecond to a microsecond that are biologically relevant. The study applied a new EPR spectrometer with many innovative features and that operates at the high microwave frequency of 94 GHz to characterize cholesterol-mediated lipid interactions in membranes as a function of cholesterol content and temperature.

Mitochondria-targeted Agents in Breast Cancer

R01CA152810
06/14/2010–04/30/2015
PI: Balaraman Kalyanaraman

The results obtained from this work likely mitigate the adverse side effects associated with breast cancer chemotherapy. This work also enables early detection of breast cancer in an animal model using a novel imaging technique.

Spin Labeling of MsbA

R01GM070642
05/01/2004–07/31/2014
PI: Candice S. Klug

Multidrug resistance is a serious problem in medicine, not only in the often futile treatment of infectious diseases, but also in the treatment of cancer patients. In addition, because of the close similarity of MsbA with other ABC transporters implicated in various common genetic disorders such as the cystic fibrosis transmembrane conductance regulator, any new functional information gained by studying the easily purified MsbA is beneficial to our understanding of structure-function relationships in this very important class of integral membrane proteins. The similarity of MsbA to so many proteins in its general class, and its prevalence in pathogenic bacteria, creates an opportunity for the detailed study of this transporter that will add to our fundamental knowledge of an entire class of potential novel drug targets.

Advanced Instrumentational Development Core: ӰԺ
U19AI091173
08/01/2010–07/31/2014
Project leader: James S. Hyde

This core provided input from what is generally agreed to be the leading EPR instrumental development site in the world, the National Biomedical EPR Center at the ӰԺ. The role of this core was to provide leadership in the development of specific aspects of the technology needed to accomplish the goals of the CMCR. These developments were carried out in collaboration with the projects and with the instrumental Core at Dartmouth, to facilitate the development of the best possible prototype instruments for EPR dosimetry.

Neuroprotection by Mitochondria-targeted Antioxidants

R01NS039958
02/01/2009–01/31/2014
MPI: Balaraman Kalyanaraman, Anumantha Kanthasamy

Role of Neuronal NOS & Superoxide in Neurodegeneration
R01NS039958
04/10/2000–03/31/2004
PI: Balaraman Kalyanaraman

Parkinson's disease (PD) is a debilitating neurodegenerative disease. Effective treatment to intervene the progression of neurodegenerative processes in PD remains unavailable. Using a cell culture and a mouse model of PD, we developed a "mitochondria-targeted" antioxidant-based neuroprotective strategy for treating PD. These studies, which brought together chemical and neuropharmacological expertise from two institutions (ӰԺ and Iowa State University), helped us develop efficacious mitochondria-targeted antioxidants for treatment of PD as well as understand the possible neuroprotective mechanisms of these novel class of agents.

Acquisition of Q-band Pulsed EPR Capability 

S10OD011937
04/01/2012–03/31/2013
PI: Candice S. Klug

This application was for an upgrade to Q-band for our current Bruker X-band E580 pulse spectrometer capable of running DEER (double electron-electron resonance), DQC (double quantum coherence), and ENDOR (electron nuclear double resonance) experiments at cryogenic temperatures. The primary use of both the current and upgraded instrument are to quantitate distance measurements between paramagnetic probes on or within biomedically relevant proteins. The major advantages of upgrading to Q-band (35 GHz) DEER from X-band (9 GHz) DEER are a >10-fold increase in sensitivity and overall higher quality distance data. The improvement in resolution, accuracy, identification, signal intensity and the collection of longer distances are of considerable benefit to an array of biological projects.

Spin-Labeled Peptide Antibiotics

R01GM068829
09/30/2004–08/31/2012
PI: Jimmy B. Feix

The prevalence of multi-drug resistant infections is one of the most serious problems in health care, both in the United States and worldwide, leading to increased treatment costs and a growing incidence of treatment failure. There is a critical need for the development of new antibiotics, and in particular for new classes of compounds that target non-traditional sites other than cell-wall synthesis and the bacterial ribosome. Antimicrobial peptides, which display remarkable efficacy against a broad spectrum of pathogens, including those resistant to conventional antibiotics, offer a novel approach to the treatment of drug-resistant infections. Developing a more complete understanding of the interactions of antimicrobial peptides with their target cells will enhance our ability to design and develop more effective peptide and peptidomimetic antibiotics.

Superoxide Generation from eNOS: The Role of Pterins

R01HL067244
12/16/2002–07/31/2012
PI: Jeannette Vasquez Vivar

The broad objectives of this study were designed to bridge the gap in knowledge and were based upon the hypothesis that altering basal tetrahydrobiopterin metabolism by lipid peroxidation products and reactive oxygen species has important consequences in normal nitric oxide/reactive oxygen species fluxes and endothelial physiology favoring phenotypical changes associated with atherogenesis.


Mechanism of Metabolism of S-Nitrosothiols

R01GM005792
12/10/2001–04/30/2012

R29GM055792
04/01/1997–11/30/2001
PI: Neil Hogg

The goal of this study was to disentangle the cellular effects of nitric oxide from the direct effects of S-nitrosothiols to more fully understand how these species affect cellular function. Importantly, these studies will point to a role of S-nitrosothiols formation not simply as "carriers" of nitric oxide bioactivity but as a distinct bifurcation in nitric oxide signaling pathways.

Nitric Oxide-Mediated Oxidation/Nitration in Membranes

R01HL063119
07/01/1999–03/31/2012
PI: Balaraman Kalyanaraman

Increased levels of nitrotyrosine and nitrated proteins have been detected in a variety of pulmonary and cardiovascular diseases, and in neurodegenerative and chronic inflammatory disorders. The overall objective of this study was to obtain new mechanistic insight into how the hydrophobic interior of biological membranes facilitates oxidation and nitration reactions of reactive nitrogen species, such as peroxynitrite or nitrogen dioxide radical. This goal of this comprehensive study of reactive nitrogen species reactions in simple well-defined model membrane system was to provide new mechanistic insight for understanding oxidative and nitrosative stress in pulmonary cardiovascular, neurodegenerative, and inflammatory diseases.

HFSS Modeling in Aqueous Biomedical EPR Instrumentation

R01EB001417
07/01/1979–03/31/2012
PI: James S. Hyde

This goals of this study were device-design driven. Two of the aims focused on development of novel sample resonators for EPR spectroscopy that provide substantially higher signal-to-noise ratios than those used. The third aim focused on development of a novel bimodal resonator for nuclear magnetic resonance signal enhancement by dynamic nuclear polarization.

EPR 2010

R13CA150298
04/0/2010–03/31/2011
PI: Balaraman Kalyanaraman

This is the first conference on in vivo spectroscopy, spin trapping, and spin labeling to be held in Puerto Rico. This interdisciplinary scientific conference brought together physicians, chemists, and biologist from the United States and around the globe, who are engaged in research activities involving magnetic resonance, structural and redox biology, radiation, cancer, and other rare diseases. The major purpose of this meeting is to discuss the applications of state-of-the-art EPR methodology in biomedical research with a view to enlightening the younger faculty, postdoctoral researchers, and graduate students on the broad scope of activities in magnetic resonance.

Site-Directed Spin Labeling of ArnT
R01AI058024
03/01/2004–02/28/2010
PI: Candice S. Klug

The goal of this proposal was to study the structure of the purified inner membrane protein ArnT by site-directed spin labeling EPR spectroscopy in order to provide the first structural information on this newly identified transferase. These studies were anticipated to provide insights into the local and global structure of ArnT, a previously uncharacterized integral membrane protein, which is of fundamental importance in furthering our understanding of the structure and functional dynamics of membrane proteins.

Is Cholesterol Crystalline Domain a Barrier to Oxygen Transport in the Eye Lens?

R03TW008052
02/01/2009–12/31/2009
PI: W. Karol Subczynski

Age-related cataracts are a major cause of blindness in developing countries. The reason for the onset of cataracts is unknown, but a great deal of evidence suggests that an increase in oxygen concentration in the lens interior can lead to the development of cataracts. The goal of the studies was to generate important fundamental information about the contribution of cholesterol to the process of oxygen transport within the eye lens, which should increase our understanding of the role cholesterol plays and, in turn, help contribute to the prevention of age-related nuclear cataracts.

Spin Labeling of MsbA
ӰԺ Research Affairs Committee
07/15/2008–07/14/2009
PI: Candice S. Klug
EPR 2007

R13EB007938
04/01/2007–03/31/2009
PI: Balaraman Kalyanaraman

EPR 2007 was a joint conference of the 12th In Vivo EPR Spectroscopy and Imaging meeting and the 9th International EPR Spin Trapping/Spin Labeling meeting. It was held April 29 through May 3, 2007, in Chicago, Illinois, at the the Hilton Suites Chicago/Magnificent Mile. The meeting was sponsored by the Department of Biophysics at the ӰԺ and the Department of Radiation and Cellular Oncology at the University of Chicago. The conference was an international workshop that brought together a community of scientists who apply the technique of electron paramagnetic resonance (EPR) to problems intimately related to human physiology and pathophysiology. The primary focus of the meeting was on the use of magnetic resonance technology to investigate the fundamental mechanisms related to technology and structural biology, oxidate cell signaling, and biomedicine. Sessions provided a balance between studies of biological systems and advances in methodology. This helped strengthen the program and promote the effectiveness of science in the United States and around the world. In addition to other invited institutions, all of the NIH-funded EPR centers participated: National EPR Center (ӰԺ, Milwaukee, WI), EPR Center for the Study of Viable Systems (Dartmouth College, Hanover, NH), and Center for EPR Imaging in In Vivo Physiology (University of Chicago, Chicago, IL). The EPR Group at the National Cancer Institute also participated in the conference. The meeting also aimed to attract a significant number of participants from other countries in Europe, Asia, Australia, Africa and South America. It was important for the United States to be well-represented at this meeting, so that our scientists were apprised of the latest technological developments from around the world and to establish future collaborations with potential postdoctoral researchers and with research groups.

Bicarbonate Enhances Peroxidation of SOD/ALS Mutants

R01NS040494
07/01/2000–01/31/2009
PI: Balaraman Kalyanaraman

The broad long-term objectives of this project are to understand the direct and indirect mechanisms by which human copper, zinc superoxide dismutase (hSOD1) mutants associated with familial and sporadic amyotrophic lateral sclerosis (ALS) disease cause selective toxicity to motor neurons. The goal of this study was to merge the oxidation and aggregation hypotheses in ALS SOD1-dependent toxicity using isolated hSOD1 proteins, and explore ceramide-induced oxidant signaling in G93A-transfected cells, and G93A mutant mice. Understanding the molecular basis of ALS SOD1 mutant toxicity will help improve overall strategies for developing effective drug therapy for ALS. The use of state-of-the-art analytical techniques coupled with syntheses of mitochondria-targeted spin probes and fluorescent probes should yield new insights on the molecular mechanism for increased toxicity of ALS SOD1 mutants in motor neuron cells.

eNOS and Radical Mechanism of Antitumor Anthracyclines

R01CA077822
01/01/1999–08/31/2008
PI: Balaraman Kalyanaraman

The long-term goal of this project was to unravel the free radical mechanisms by which doxorubicin (DOX), a cancer chemotherapeutic drug that is currently used in the clinic, induces cardiotoxicity in cancer patients.

Peroxide, NO and Iron Signaling in Endothelial Damage

R01HL073056
03/17/2003–02/29/2008
PI: Balaraman Kalyanaraman

The long-term goal of this proposal is to unravel the role of oxidant-induced iron signaling mechanism in endothelial cell apoptosis.

Additional Funds for the Acquisition of a Bruker E580 Pulse EPR Spectrometer
ӰԺ/Advancing a Healthier Wisconsin
12/01/2006–11/30/2007
PI: Candice S. Klug
Structural and Functional Characterization of the Bacterial Inner Membrane Enzyme Responsible for Lipid A Modification-Induced Polymyxin Resistance
ӰԺ Research Affairs Committee
07/15/2002–07/14/2003
PI: Candice S. Klug

Grants

Ending after ~2010, with EPR Center faculty as Co-Investigator or Collaborator

all
Neuroprotection by nNOS Inhibitors in Perinatal Hypoxia-Ischemia

R01NS114972
05/01/2020–02/28/2025
PI: Sidhartha Tan
Co-investigator: Jeannette Vasquez Vivar

There is a paucity of effective treatments for cerebral palsy and this proposal tests new promising drugs aimed at a preventive cure for this disease. These are new drugs aimed at inhibiting an enzyme present in brain called neuronal nitric oxide synthase. New information about how these drugs act, how they affect brain cells, and how effective they are in an animal model of cerebral palsy will be very valuable for future translation to clinical use in humans throughout the world.

Development of High-Throughput, High-Sensitivity EPR Sample Handling Capabilities for Biomedical Research

R01GM140385
01/01/2021–11/30/2024
MPI: Candice S. Klug, Michael T. Lerch (ӰԺ)
Co-investigators: Neil Hogg, Richard R. Mett, Jason W. Sidabras

EPR spectroscopy is a critically important technique in biomedical research with a unique ability to detect naturally occurring or engineered unpaired electrons in complex biological environments. We will develop two innovative EPR spectrometer technologies with outstanding sample sensitivity that are easy to use and widely available to the scientific community. The resulting state-of-the-art prototypes will provide a transformative increase in throughput that will enable a wide range of new applications in biomedical EPR spectroscopy studies including structural biology, metalloprotein research, redox biology, rational drug design, and clinical diagnostics for a range of disease areas.

Unravelling Cholesterol-Domain Organization and Function in the Plasma Membrane of the Eye Lens Fiber Cells Using Fluorescent Methods
IP-2019-04-1958
12/20/2019–12/19/2023
PI: Marija Raguz (University of Split, Croatia)
Collaborator: W. Karol Subczynski
Conformational and Functional Dynamics of Bacterial PASTA Kinase

R01GM135256
01/01/2020–11/30/2023
PI: Christopher J. Kristich (transferred from Candice S. Klug & Christopher J. Kristich [MPI])
Co-investigator: Candice S. Klug

Transmembrane kinases containing PASTA domains control critical processes in most Gram-positive pathogenic bacteria, including antibiotic resistance, toxin production, virulence, cell division, and bacterial viability. The research proposed here promises to reveal new insights into the mechanisms by which this family of kinases functions to coordinate biological adaptations to environmental stimuli. These insights will facilitate development of new treatments for infections caused by Gram-positive bacteria by defining new targets for innovative therapeutics with potentially unique modes of action.

Fis1 Regulation of Mitochondrial Fission
R01GM067180
01/01/2004–05/31/2023
PI: Blake R. Hill (ӰԺ)
Co-investigator: Jimmy B. Feix

Mitochondria are components of cells that perform many functions critical for life and are known for being the "power plant" of the cells. The mitochondria have their own life cycle with a mechanism to destroy damaged mitochondria that involves a splitting event that separates a healthy daughter mitochondrion from an unhealthy one that is subsequently removed by the cell. This study will illuminate mechanistic details of these processes and represents an important step towards the discovery of new therapeutic strategies for both rare and common human diseases, including cardiac and neurodegenerative diseases, cancer, diabetes, aging, and neonatal lethality syndrome.

Role of Beta-Arrestins in Chemokine Receptor Signaling
R01GM106727
02/11/2014–04/30/2023
PI: Adriano Marchese (ӰԺ)
Co-investigator: Candice S. Klug

The chemokine receptor CXCR4 is overexpressed in metastatic cancers and is associated with poor prognosis, yet the molecular and cellular mechanisms by which CXCR4 contributes to metastatic disease remain poorly understood. The objective of this proposal is to determine the signal transduction mechanisms by which CXCR4 promotes directed cell migration, a cancer-related process required for the spread of cancer to other tissues. Understanding these mechanisms may lead to the identification of new and innovative therapeutic targets to treat and prevent metastatic disease involving CXCR4 signaling.

Selective Uptake and Hydrolysis of Cholesteryl Ester by SR-BI 

R01HL058012
05/01/2015–03/31/2024
PI: Daisy Sahoo (ӰԺ) 
Co-investigator: Jimmy B. Feix

High plasma cholesterol levels are a major risk factor for heart disease, the leading cause of death worldwide. Our research is designed to understand how we can improve cholesterol removal from the body and lower plasma cholesterol levels. Our findings will help identify new strategies for treating heart disease and other related complications.


Lipid Domains in Lens Membranes of a Single Eye: EPR Spin-Labeling Studies

R01EY015526
04/01/2004–05/31/2021
PI: W. Karol Subczynski (ӰԺ)
Co-investigator: Jimmy B. Feix

Cataracts are a major cause of blindness throughout the world. At present, surgery is the only effective treatment. The reason for the onset of cataracts is unknown, but a great deal of evidence suggests that the presence of high cholesterol and cholesterol bilayer domains in the eye lens helps to maintain transparency and prevent cataract formation. The goal of this study was to understand how fiber-cell plasma membranes in the lens, in particular their lipid bilayer portion, change during aging and cataract formation so that alternative strategies for preventing, slowing the progression, and curing cataracts can be devised and evaluated.


Cholesterol Domains in Lipid Bilayers and Cholesterol Aggregates in Water—Structural, Temporal, and Mechanical Characteristics

2016/22/M/NZ1/00187
04/01/2017–03/31/2021
PI: Marta Pasenkiewicz-Gierula ( Jagiellonian University, Poland)
Co-investigator: W. Karol Subczynski

Research Training Program in Vision Science
T32EY014537
Research Training Program in Vision Science
9/1/2008–12/31/2018
PI: Joseph C. Besharse
Mentor: Candice S. Klug

The goal of the project was to train a new generation of vision science researchers at the predoctoral level that are highly competent in the newest technologies and at the same time mindful of the important role of interdisciplinary, collaborative and translational research in major scientific advances. Our challenge was to expose them to the major problems that need to be solved in vision research while providing in depth training in the technologies essential for research.

National Biomedical EPR Center

P41EB001980
National Biomedical EPR Center
03/01/1997–03/31/2019
PI: Candice S. Klug (transferred from James S. Hyde) (ӰԺ)
Co-Investigators & Collaborators: William E. Antholine, Brian Bennett, Jimmy Feix, Michael T. Lerch, Richard R. Mett, Jason W. Sidabras, Robert A. Strangeway, W. Karol Subczynski

The mission of the National Biomedical EPR Center was to serve the community of EPR spectroscopists by development of advanced EPR instrumentation and new EPR methodologies.


Structure of the GABA-A Receptor Binding Sites
R01NS034727
09/01/2009–08/31/2011 & 03/01/2013–02/28/2017
PI: Cynthia M. Czajkowski (University of Wisconsin-Madison)
Co-investigator: Candice S. Klug

Ligand-gated ion channels are proteins that reside in the membranes of all nerve cells. These proteins form channels through the membrane to allow neurons to signal one another at synapses, and thus regulate information flow throughout the brain. Defects in these channels lead to wide variety of neurological diseases and psychiatric conditions and they are the targets of a large number of clinically used drugs. We cannot hope to predict the actions of a drug, design safer and more effective drugs, develop better therapeutic strategies or predict the outcome of a disease-causing mutation without knowledge of how these channels work at a molecular level. The goal of this project was to advance our understanding of how these important channels work.

Arrestin Interactions with Non-Receptor Binding Partners
R01GM077561
4/10/2012–3/31/2016
PI: Vsevold Gurevich (Vanderbilt University)
Co-investigator: Candice S. Klug

This study focused on the elucidation of the structural basis of arrestin-dependent activation of the pro-apoptotic JNK family kinases and their activators MKK4/7 using biochemical and biophysical methods. The potential of arrestin mutants with dramatically reduced ability to activate JNKs, that were constructed based on this info, to protect cells against insults and prolong their survival was tested, and the ability of the mutants that activate JNKs more efficiently than wild type arrestins to facilitate cell death also was tested. Molecular tools that specifically increase or block pro-apoptotic signaling have therapeutic potential in disorders associated with excessive cell proliferation (e.g., cancer) or death (e.g., neurodegenerative diseases).

Development of Biomedical EPR Instrumentation

R01EB002052
07/01/1979–03/31/2016
PI: Candice S. Klug (transferred from James S. Hyde)
Co-investigators & Collaborators: Jimmy Feix, Richard R. Mett, Jason W. Sidabras, Robert A. Strangeway, W. Karol Subczynski

Molecular dynamics occur in all biological molecules across a wide range of motional frequencies, some of which are central to biological function. The nitroxide-radical spin-label method, based on EPR, is suitable for the study of molecular dynamics, including dynamics with characteristic motional periods of a millisecond to a microsecond that are biologically relevant. The study applied a new EPR spectrometer with many innovative features and that operates at the high microwave frequency of 94 GHz to characterize cholesterol-mediated lipid interactions in membranes as a function of cholesterol content and temperature.


Conformational Regulation of Arrestin-Mediated Signaling

R01GM081756
09/01/2008–06/30/2012
PI: Vsevold Gurevich (Vanderbilt University)
Co-investigator: Candice S. Klug

Arrestins are multi-functional adaptors that mobilize various signaling molecules to G protein-coupled receptors and microtubules with different functional consequences. The goal of this study was to elucidate the conformations of receptor-bound and microtubule-bound arrestins to understand how arrestin conformation affects its interactions with signaling proteins and the consequences of their binding. This information will set the stage for designing arrestin-based molecular tools for targeted manipulation of cellular signaling that can be used for experimental and therapeutic purposes.


iNOS Post-translational Regulation in Cardiac Rejection

R01HL078937
03/15/2006–02/28/2011
PI: Galen M. Pieper (ӰԺ)
Co-investigator: Jeannette Vasquez Vivar

The loss of cardiac muscle cells is a significant problem in human cardiac transplants that may contribute to poor heart function. Our studies aimed to identify a potential molecular problem intrinsic to cardiac cells that predisposes to cell death and injury. A better understanding of this molecular process may lead to better strategies to prevent injury cardiac cells in these patients.

Publications

Our faculty, collaborators, and visitors/users have published these molecular biophysics articles.
all
2024

Bluma MS, Schultz KM, Kristich CJ, Klug CS. . Protein Sci. 2023 Jul;32(7):e4697. doi: 10.1002/pro.4697. PMID: 37312631; PMCID: PMC10303680.

Schultz KM, Schneider JR, Fischer MA, Cina NP, Riegert MO, Frank DW, Klug CS. . Protein Sci. 2023 Aug;32(8):e4724. doi: 10.1002/pro.4724. PMID: 37417889; PMCID: PMC10360375.

VanZeeland NE, Schultz KM, Klug CS, Kristich CJ. . J Mol Biol. 2023 Sep 15;435(18):168216. doi: 10.1016/j.jmb.2023.168216. Epub 2023 Jul 28. PMID: 37517789; PMCID: PMC10528945.

Cina NP, Klug CS. . Appl Magn Reson. 2024 Mar;55(1-3):141-158. doi: 10.1007/s00723-023-01590-3. Epub 2023 Aug 7. PMID: 38645307; PMCID: PMC11025719. (Special Issue: Wayne Hubbell – on the Occasion of His 80th birthday)

2023

Flood AB, Sidabras JW, Swarts SG, Buehler PW, Schreiber W, Grinberg O, Swartz HM. . Radiat Prot Dosimetry. 2023 Sep 18;199(14):1539-1550. doi: 10.1093/rpd/ncad022. PMID: 37721065; PMCID: PMC10505939.

VanZeeland NE, Schultz KM, Klug CS, Kristich CJ. . J Mol Biol. 2023 Sep 15;435(18):168216. doi: 10.1016/j.jmb.2023.168216. Epub 2023 Jul 28. PMID: 37517789; PMCID: PMC10528945.

Subczynski WK, Pasenkiewicz-Gierula M, Widomska J. . Antioxidants (Basel). 2023 Sep 20;12(9):1783. doi: 10.3390/antiox12091783. PMID: 37760086; PMCID: PMC10525422.

Schultz KM, Schneider JR, Fischer MA, Cina NP, Riegert MO, Frank DW, Klug CS. . Protein Sci. 2023 Aug;32(8):e4724. doi: 10.1002/pro.4724. PMID: 37417889; PMCID: PMC10360375.

Widomska J, Subczynski WK, Welc-Stanowska R, Luchowski R. . Int J Mol Sci. 2023 Aug 18;24(16):12948. doi: 10.3390/ijms241612948. PMID: 37629129; PMCID: PMC10454802.

Bluma MS, Schultz KM, Kristich CJ, Klug CS. . Protein Sci. 2023 Jul;32(7):e4697. doi: 10.1002/pro.4697. PMID: 37312631; PMCID: PMC10303680.

Boban Z, Mardešić I, Jozić SP, Šumanovac J, Subczynski WK, Raguz M. . Membranes (Basel). 2023 Mar 18;13(3):352. doi: 10.3390/membranes13030352. PMID: 36984739; PMCID: PMC10059949.

Mardešić I, Boban Z, Subczynski WK, Raguz M. . Membranes (Basel). 2023 Mar 10;13(3):320. doi: 10.3390/membranes13030320. PMID: 36984707; PMCID: PMC10057498.

Mainali L, Raguz M, Subczynski WK. . Membranes (Basel). 2023 Feb 3;13(2):189. doi: 10.3390/membranes13020189. PMID: 36837692; PMCID: PMC9958954.

2022

Perry-Hauser NA, Hopkins JB, Zhuo Y, Zheng C, Perez I, Schultz KM, Vishnivetskiy SA, Kaya AI, Sharma P, Dalby KN, Chung KY, Klug CS, Gurevich VV, Iverson TM. . J Mol Biol. 2022 Apr 15;434(7):167465. doi: 10.1016/j.jmb.2022.167465. PMID: 35077767; PMCID: PMC8977243.

Hyde JS, Strangeway RA, Sidabras JW. . Appl Magn Reson. 2022 Jan;53(1):193-206. doi: 10.1007/s00723-021-01352-z. PMID: 35464635; PMCID: PMC9030583.

Teucher M, Sidabras JW, Schnegg A. . Phys Chem Chem Phys. 2022 May 25;24(20):12528-12540. doi: 10.1039/d1cp05508a. PMID: 35579184.

Subczynski WK, Raguz M, Widomska J. . Membranes (Basel). 2022 Jun 26;12(7):657. doi: 10.3390/membranes12070657. PMID: 35877860; PMCID: PMC9321980.

Mett RR, Hyde JS. . Appl Magn Reson. 2022 Sep;53(7-9):1265-1274. doi: 10.1007/s00723-021-01432-0. PMID: 35991538; PMCID: PMC9387911.

Subczynski WK, Widomska J. . Membranes (Basel). 2022 Sep 30;12(10):962. doi: 10.3390/membranes12100962. PMID: 36295720; PMCID: PMC9612125.

Subczynski WK, Widomska J, Raguz M, Pasenkiewicz-Gierula M. . Oxygen (Basel). 2022 Sep;2(3):295-316. doi: 10.3390/oxygen2030021. PMID: 36852103; PMCID: PMC9965258.

Schultz KM, Klug CS. . In: Sperandeo P, editor. Lipopolysaccharide Transport – Methods and Protocols, Methods in Molecular Biology. Springer Nature; 2022. Volume 2548; pp. 83-96.

Subczynski WK, Pasenkiewicz-Gierula M, Widomska J, Stein N. Role of cholesterol in maintaining the physical properties of the plasma membrane. In: Cholesterol: from Biophysics to the Clinics. Bukiya AN, Dopico AM, editors. Academic Press, 2022. Chapter 3, pp. 41-71.

2021

Stein N, Subczynski WK. . Exp Eye Res. 2021; 206:108536. doi: 10.1016/j.exer.2021.108536. PMID: 33716012. PMCID: PMC8139366

Campanella AJ, Nguyen MT, Zhang J, Ngendahimana T, Antholine WE, Eaton GR, Eaton SS, Glezakou VA, Zadrozny JM. . Dalton Trans. 2021;50(15):5342-5350. doi: 10.1039/d1dt00066g. PMID: 33881070.

Hyde JS, Strangeway RA, Sidabras JW. . Appl Magn Reson. 2022 Jan;53(1):193-206. doi: 10.1007/s00723-021-01352-z. PMID: 35464635; PMCID: PMC9030583.

Subczynski WK, Widomska J, Stein N, Swartz HM. . Appl Magn Reson. 2021 Oct;52(10):1237-1260. doi: 10.1007/s00723-021-01412-4. PMID: 36267674; PMCID: PMC9581439.

Markiewicz M, Szczelina R, Milanovic B, Subczynski WK, Pasenkiewicz-Gierula M. . Comput Struct Biotechnol J. 2021 Jul 26;19:4319-4335. doi: 10.1016/j.csbj.2021.07.022. PMID: 34429850; PMCID: PMC8361299.

Stein N, Subczynski WK.. Appl Magn Reson. 2021 Jan;52(1):61-80. doi: 10.1007/s00723-020-01237-7. PMID: 33776217; PMCID: PMC7992188.

Klug CS, Lerch MT, Feix JB. Applications of Nitroxide Spin Labels to Structural Biology. In: Ouari O, Gigmes D, editors. Nitroxides: Synthesis, Properties and Applications [Internet] London, UK: Royal Society of Chemistry; 2021. Chapter 10; p.392-419.

2020

Mainali L, Pasenkiewicz-Gierula M, Subczynski WK. . Curr Eye Res. 2020;45(2):162-172. doi:10.1080/02713683.2019.1662058 PMCID: PMC6980519

Del Alamo D, Tessmer MH, Stein RA, Feix JB, Mchaourab HS, Meiler J. . Biophys J. 2020 Jan 21;118(2):366-375. doi: 10.1016/j.bpj.2019.12.011. PMID: 31892409; PMCID: PMC6976798.

Cheng G, Pan J, Podsiadly R, Zielonka J, Garces AM, Dias Duarte Machado LG, Bennett B, McAllister D, Dwinell MB, You M, Kalyanaraman B. . Free Radic Biol Med. 2020 Feb 1;147:167-174. doi: 10.1016/j.freeradbiomed.2019.12.020. PMID: 31874251; PMCID: PMC6948008.

Boban Z, Puljas A, Kovač D, Subczynski WK, Raguz M. . Cell Biochem Biophys. 2020 Apr 21. doi: 10.1007/s12013-020-00910-9. PMCID: PMC7608754

Widomska J, SanGiovanni JP, Subczynski WK. . Nutrients. 2020;12(5):1333. Published 2020 May 7. doi:10.3390/nu12051333. PMCID: PMC7284714

Hilger D, Kumar KK, Hu H, Pedersen MF, O'Brien ES, Giehm L, Jennings C, Eskici G, Inoue A, Lerch M, Mathiesen JM, Skiniotis G, Kobilka BK. . Science. 2020;369(6503):eaba3373. doi:10.1126/science.aba3373

Zhuo Y, Gurevich VV, Vishnivetskiy SA, Klug CS, Marchese A. . J Biol Chem. 2020;jbc.RA120.015074. doi:10.1074/jbc.RA120.015074. PMCID: PMC7426584

Lerch MT, Matt RA, Masureel M, Elgeti M, Kumar KK, Hilger D, Foys B, Kobilka BK, Hubbell WL. . Proc Natl Acad Sci U S A. 2020 Nov 30:202013904. doi: 10.1073/pnas.2013904117. PMID: 33257561; PMCID: PMC7749303.

Tessmer MH, DeCero SA, Del Alamo D, Riegert MO, Meiler J, Frank DW, Feix JB. . Sci Rep. 2020 Nov 12;10(1):19700. doi: 10.1038/s41598-020-76023-3. PMID: 33184362; PMCID: PMC7665212.

Szala M, Grzelakowska A, Modrzejewska J, Siarkiewicz P, Slowinski D, Swierczynska M, Zielonka J, Podsiadly R. . Dyes and Pigments 2020 Dec;183:108693.

Chen Q, Zhuo Y, Sharma P, Perez I, Francis DJ, Chakravarthy S, Vishnivetskiy SA, Berndt S, Hanson SM, Zhan X, Brooks EK, Altenbach C, Hubbell WL, Klug CS, Iverson TM, Gurevich VV. . J Mol Biol. 2020 Dec 30:166790. doi: 10.1016/j.jmb.2020.166790. 

Subczynski WK, Pasenkiewicz-Gierula M. . Cell Biochem Biophys. 2020 Sep;78(3):241-247. doi: 10.1007/s12013-020-00925-2. PMID: 32602057; PMCID: PMC7403164.

2019

Mainali L, O'Brien WJ, Subczynski WK. . Exp Eye Res. 2019 January;178:72-81. PMCID: PMC6361697

Feix JB, Kohn S, Tessmer MH, Anderson DM, Frank DW. . Cell Biochem Biophys. 2019 March;77(1):79-87. PMCID: PMC6347562

Hyde JS, Sidabras JW, Mett RR. . Cell Biochem Biophys. 2019 March;77(1):3-14. PMCID: PMC6309773

Tikhonov AN, Subczynski WK. . Cell Biochem Biophys. 2019 March;77(1):47-59. PMCID: PMC6524781

Antholine WE, Vasquez-Vivar J, Quirk BJ, Whelan HT, Wu PK, Park JI, Myers CR. . Int J Mol Sci. 2019 March 6;20(5). PMCID: PMC6429069

Antholine WE. . Int J Mol Sci. 2019 May 14;20(10). PMCID: PMC6566446

Antholine WE, Myers CR. . Int J Mol Sci. 2019 June 22;20(12). PMCID: PMC6627071

Stein N, Mainali L, Hyde JS, Subczynski WK. . Appl Magn Reson. 2019 July;50(7):903-918. PMCID: PMC6594395

2018

Tessmer MH, Anderson DM, Pickrum AM, Riegert MO, Moretti R, Meiler J, Feix JB, Frank DW. . Proc Natl Acad Sci U S A. 2018 January;115(3):525-530. PMCID: PMC5776994

Schultz KM, Klug CS. . Protein Sci. 2018 February;27(2):381-389. PMCID: PMC5775163

Chitambar CR, Al-Gizawiy MM, Alhajala HS, Pechman KR, Wereley JP, Wujek R, Clark PA, Kuo JS, Antholine WE, Schmainda KM. . Mol Cancer Ther. 2018 June;17(6):1240-1250. PMCID: PMC5984712

Schultz KM, Fischer MA, Noey EL, Klug CS. . Protein Sci. 2018 August;27(8):1407-1417. PMCID: PMC6153404

Stadtmueller BM, Bridges MD, Dam KM, Lerch MT, Huey-Tubman KE, Hubbell WL, Bjorkman PJ. . Immunity. 2018 August 21;49(2):235-246.e4. PMCID: PMC6104740

Yang X, Bennett B, Holz RC. . Archives Biochem Biophys. 2018 November 1;657:1-7. PMCID: PMC6201762

Antholine WE, Zhang S, Gonzales J, Newman N. . Int J Mol Sci. 2018 November 9;19(11). PMCID: PMC6274703

2017

Tessmer MH, Anderson DM, Buchaklian A, Frank DW, Feix JB. . J Biol Chem. 2017 Jan 9. pii: jbc.M116.760074. PMCID: PMC5336173

Kalyanaraman B, Cheng G, Hardy M, Ouari O, Sikora A, Zielonka J, Dwinell MB. . Cell Biochem Biophys. 2017 Dec;75(3-4):311-317. PMCID: PMC5680142

Subczynski W.K., Widomska J., Mainali L. . Adv Exp Med Biol. 2017;977:27-34. PMCID: PMC5851008

Fischer AW, Anderson DM, Tessmer MH, Frank DW, Feix JB, Meiler J. . ACS Omega. 2017 Jun 30;2(6):2977-2984.  PMCID: PMC5494639

Hyde JS. . Appl. Magn. Reson. 2017 Dec; 48(11-12), 1103-1147. [Part of special issue dedicated to Hyde.] PMCID: PMC6022859

Sarna T, Kalyanaraman B, Berliner L. . Cell Biochem Biophys. 2017; 75(3): 257–258. PMCID: PMC5691121

Sidabras JW, Reijerse EJ, Lubitz W. . Appl. Magn. Reson. 2017.

Mainali L, Camenisch TG, Hyde JS, Subczynski WK. . Appl Magn Reson. 2017 Dec;48(11-12):1355-1373. PMCID: PMC5967259

Schultz KM, Klug CS. . Appl Magn Reson. 2017 Dec;48(11-12):1341-1353. PMCID: PMC5761346

Hyde JS, Mett RR. . Appl Magn Reson. 2017 Dec;48(11-12):1185-1204. PMCID: PMC5761080

Chen Q, Perry NA, Vishnivetskiy SA, Berndt S, Gilbert NC, Zhuo Y, Singh PK, Tholen J, Ohi MD, Gurevich EV, Brautigam CA, Klug CS, Gurevich VV, Iverson TM. . Nat Commun. 2017 Nov 10;8(1):1427. PMCID: PMC5681653

Herneisen AL, Sahu ID, McCarrick RM, Feix JB, Lorigan GA, Howard KP. . 2017 Nov 7;56(44):5955-5963. PMCID: PMC6112238

Schultz KM, Klug CS. . Protein Sci. 2018 Feb;27(2):381-389. PMCID: PMC5775163

Suliman M, Santosh V, Seegar TCM, Dalton AC, Schultz KM, Klug CS, Barton WA. . PLoS One. 2017 Aug 31;12(8):e0184271. PMCID: PMC5578623

Sidabras JW, Sarna T, Mett RR, Hyde JS. . J Magn Reson. 2017 Sep;282:129-135. PMCID: PMC5793860

Widomska J, Subczynski WK, Mainali L, Raguz M. . Cell Biochem Biophys. 2017 Dec;75(3-4):387-398. PMCID: PMC5691107

Strangeway RA, Hyde JS, Camenisch TG, Sidabras JW, Mett RR, Anderson JR, Ratke JJ, Subczynski WK. . 2017 Dec;75(3-4):259-273. PMCID: PMC5693649

Stein N, Gumataotao N, Hajnas N, Wu R, Lankathilaka KPW, Bornscheuer UT, Liu D, Fiedler AT, Holz RC, Bennett B. . Biochemistry. 2017 Jun 20;56(24):3068-3077. PMCID: PMC5821057

Schultz KM, Lundquist TJ, Klug CS. . Protein Sci. 2017 Aug;26(8):1517-1523. PMCID: PMC5521551

Subczynski WK, Pasenkiewicz-Gierula M, Widomska J, Mainali L, Raguz M. . Cell Biochem Biophys. 2017 Dec;75(3-4):369-385. Review. PMCID: PMC5521551

Langley M, Ghosh A, Charli A, Sarkar S, Ay M, Luo J, Zielonka J, Brenza T, Bennett B, Jin H, Ghaisas S, Schlichtmann B, Kim D, Anantharam V, Kanthasamy A, Narasimhan B, Kalyanaraman B, Kanthasamy AG. . Antioxid Redox Signal. 2017 Nov 10;27(14):1048-1066. PMCID: PMC5651937

Sidabras JW, Mett RR, Hyde JS. . J Magn Reson. 2017 Apr;277:45-51. PMCID: PMC5674976

Sidabras JW, Richie JE, Hyde JS. Axially uniform magnetic field-modulation excitation for electron paramagnetic resonance in rectangular and cylindrical cavities by slot cutting. J Magn Reson. 2017 Jan;274:115-124. PMCID: PMC5652332

Mainali L, Raguz M, O'Brien WJ, Subczynski WK. . Curr Eye Res. 2017 May;42(5):721-731. PMCID: PMC5409882

Subczynski WK, Mainali L, Raguz M, O'Brien WJ. . Exp Eye Res. 2017 Mar;156:79-86. PMCID: PMC5023447

Subczynski WK, Pasenkiewicz-Gierula M, Widomska J, Mainali L, Raguz M. . Cell Biochem Biophys. 2017 December;75(3-4):369-385. PMCID: PMC5645210

2016
Bennett B, Helbling D, Meng H, Jarzembowski J, Geurts AM, Friederich MW, Van Hove JL, Lawlor MW, Dimmock DP. (2016). . Free Radic Biol Med. 2016 Mar;92:141-51. PMCID: 5047058

Bennett B, Kowalski JM. (2015). . Methods Enzymol. 563:341-61. PMCID: PMC4772423

Hewage JS, Wanniarachchi S, Morin TJ, Liddle BJ, Banaszynski M, Lindeman SV, Bennett B, Gardinier JR. (2014). Inorganic chemistry53(19):10070-84. PMCID: PMC5047063

Mandal T, Shin S, Aluvila S, Chen H-C, Grieve C, Choe J-Y, Cheng EH, Hustedt EJ, Oh KJ. (2016). . Sci Rep. 6:30763. PMCID: PMC4973285.

Mainali L, Raguz M, O’Brien WJ, Subczynski WK. (2016). . Curr Eye Res. 1-11. PMCID: PMC5409882

Mett RR, Sidabras JW, Hyde JS. (2016). . Rev Sci Inst. Rev. Sci. Instrum. 87, 124704. PMCID: PMC5201604

Mett RR, Sidabras JW, Hyde JS. (2016). . Rev Sci Instrum. 87(8):084703. PMCID: PMC5010558

Johnson BJ, Antholine WE, Lindeman SV, Graham MJ, Mankad NP. (2016). . J Am Chem Soc. PMCID: PMC5378702 

Sidabras JW, Strangeway RA, Mett RR, Anderson JR, Mainali L, Hyde JS. (2016). . II Broadband Characterization. Rev Sci Instrum. 87(3):034704. PMCID: PMC4798996

Stein N, Love D, Judd ET, Elliott SJ, Bennett B, Pacheco AA. (2015). . Biochemistry. 54(24):3749-58. PMCID: PMC4743497

Subczynski W, Mainali L, Raguz M, O’Brien WJ. (2016). . Exp Eye Res. S0014-4835(6)30034-3. PMCID: PMC5023447

Widomska J, Zareba M, Subczynski WK. (2016). Foods. 5(1). pii: 7. PMCID: PMC4809277

Wen T, Wamer WG, Subczynski WK, Hou S, Wu X, Yin JJ. (2016). . Sci Rep. 6:24101. PMCID: PMC4829829

Zareba M, Widomaka J, Burka JM, Subczynski WK. (2016). . Free Rad Biol Med. 101:446-454. PMCID: PMC5154825

Zielonka J, Podsiadły R, Zielonka M, Hardy M, Kalyanaraman K. . Free Radic. Biol. Med. 2016, 99, 32-42. PMCID: PMC5107150
2015

Aitha M, Moritz L, Sahu ID, Sanyurah O, Roche Z, McCarrick R, Lorigan GA, Bennett B, Crowder MW. . J Biol Inorg Chem. 2015 Apr;20(3):585-94. doi: 10.1007/s00775-015-1244-8. PubMed PMID: 25827593; PubMed Central PMCID: PMC4733638.

Anderson DM, Feix JB, Frank DW. . PLoS Pathog. 2015 Jul 23;11(7):e1004944. doi: 10.1371/journal.ppat.1004944. Review. PubMed PMID: 26203905; PubMed Central PMCID: PMC4512716.

Anderson DM, Sato H, Dirck AT, Feix JB, Frank DW. . J Bacteriol. 2015 Feb;197(3):529-41. doi: 10.1128/JB.02402-14. PubMed PMID: 25404699; PubMed Central PMCID: PMC4285982.

Johnson BJ, Antholine WE, Lindeman SV, Mankad NP. . Chem Commun (Camb). 2015 Jul 28;51(59):11860-3. doi: 10.1039/c5cc04675k. PubMed PMID: 26111160; PubMed Central PMCID: PMC4731228.

Kim SS, Upshur MA, Saotome K, Sahu ID, McCarrick RM, Feix JB, Lorigan GA, Howard KP. . 2015 Dec 15;54(49):7157-67. doi: 10.1021/acs.biochem.5b01065. PubMed PMID: 26569023; PubMed Central PMCID: PMC4734095.

Kittell AW, Hyde JS. . J Magn Reson. 2015 Jun;255:68-76. doi: 10.1016/j.jmr.2015.03.014. PubMed PMID: 25917132; PubMed Central PMCID: PMC4441560.

Lane AC, Barnes CL, Antholine WE, Wang D, Fiedler AT, Walensky JR. . Inorg Chem. 2015 Sep 8;54(17):8509-17. doi: 10.1021/acs.inorgchem.5b01161. PubMed PMID: 26252561; PubMed Central PMCID: PMC4733884.

Mainali L, Raguz M, O'Brien WJ, Subczynski WK. . Eur Biophys J. 2015 Feb;44(1-2):91-102. doi: 10.1007/s00249-014-1004-7. PubMed PMID: 25502634; PubMed Central PMCID: PMC4323688.

Mainali L, Vasquez-Vivar J, Hyde JS, Subczynski WK. . Appl Magn Reson. 2015 Aug 1;46(8):885-895. PubMed PMID: 26441482; PubMed Central PMCID: PMC4591545.

Raguz M, Mainali L, O'Brien WJ, Subczynski WK. . Exp Eye Res. 2015 Mar;132:78-90. doi: 10.1016/j.exer.2015.01.018. PubMed PMID: 25617680; PubMed Central PMCID: PMC4352400.

Raguz M, Mainali L, O'Brien WJ, Subczynski WK. . Exp Eye Res. 2015 Nov;140:179-86. doi: 10.1016/j.exer.2015.09.006. PubMed PMID: 26384651; PubMed Central PMCID: PMC4624471.

Starus A, Nocek B, Bennett B, Larrabee JA, Shaw DL, Sae-Lee W, Russo MT, Gillner DM, Makowska-Grzyska M, Joachimiak A, Holz RC. . Biochemistry. 2015 Aug 11;54(31):4834-44. doi: 0.1021/acs.biochem.5b00475. PubMed PMID: 26186504; PubMed Central PMCID: PMC4671288.

Xu J, Eriksson SE, Cebula M, Sandalova T, Hedström E, Pader I, Cheng Q, Myers CR, Antholine WE, Nagy P, Hellman U, Selivanova G, Lindqvist Y, Arnér ES. . Cell Death Dis. 2015 Jan 22;6:e1616. doi: 10.1038/cddis.2014.574. PubMed PMID: 25611390; PubMed Central PMCID: PMC4669772.

Zielonka J, Sikora A, Adamus J, Kalyanaraman B. . Methods Mol Biol. 2015;1264:171-81. doi: 10.1007/978-1-4939-2257-4_16. PubMed PMID: 25631013; PubMed Central PMCID: PMC4451192.

2014

Cheng G, Zielonka J, McAllister D, Tsai S, Dwinell MB, Kalyanaraman B. . Br J Cancer. 2014 Jul 8;111(1):85-93. doi: 10.1038/bjc.2014.272. PMCID: PMC4090735

Diers AR, Broniowska KA, Chang CF, Hill RB, Hogg N. . Free Radic Biol Med. 2014 Apr;69:229-38. doi: 10.1016/j.freeradbiomed.2014.01.031. PMCID: PMC3982622

Dranka BP, Gifford A, McAllister D, Zielonka J, Joseph J, O'Hara CL, Stucky CL, Kanthasamy AG,Kalyanaraman B. . Neurosci Lett. 2014 Sep 25. pii: S0304-3940(14)00779-4. doi: 10.1016/j.neulet.2014.09.042. PMCID: PMC4253647

Hardy M, Poulhés F, Rizzato E, Rockenbauer A, Banaszak K, Karoui H, Lopez M, Zielonka J,Vasquez-Vivar J,Sethumadhavan S, Kalyanaraman B, Tordo P, Ouari O. . Chem Res Toxicol. 2014 Jul 21;27(7):1155-65. doi:  10.1021/tx500032e. PMCID: PMC5452977

He X, Swarts SG, Demidenko E, Flood AB, Grinberg O, Gui J, Mariani M, Marsh SD, Ruuge AE,Sidabras JW,  Tipikin D, Wilcox DE, Swartz HM. . Radiat Prot Dosimetry. 2014 Jun;159(1-4):172-81. doi: 10.1093/rpd/ncu129. PMCID: PMC4095917

Koto T, Michalski R, Zielonka J, Joseph J, Kalyanaraman B. . Free Radic Res. 2014 Apr;48(4):478-86. doi: 10.3109/10715762.2014.886774. PMCID: PMC4780754

Kumar A, Chen SH, Kadiiska MB, Hong JS, Zielonka J, Kalyanaraman B, Mason RP. . Free Radic Biol Med. 2014 Aug;73:51-9. doi: 10.1016/j.freeradbiomed.2014.04.014. PMCID: PMC4111989

Larson MC, Hillery CA, Hogg N. . Free Radic BiolMed. 2014 Aug;73:214-28. doi: 10.1016/j.freeradbiomed.2014.04.017. PMCID: PMC4465756

Michalski R, Michalowski B, Sikora A, Zielonka J, Kalyanaraman B. . Free Radic Biol Med. 2014 Feb;67:278-84. doi: 10.1016/j.freeradbiomed.2013.10.816. PMCID: PMC4275029

Michalski R, Zielonka J, Gapys E, Marcinek A, Joseph J, Kalyanaraman B. . J Biol Chem. 2014 Aug 8;289(32):22536-53. doi: 10.1074/jbc.M114.553727. PMCID: PMC4139259

Mouradian M, Kikawa KD, Dranka BP, Komas SM, Kalyanaraman B, Pardini RS. . Mol Carcinog. 2014 Apr 12. doi: 10.1002/mc.22151. 

Pan J, Zhang Q, Liu Q, Komas SM, Kalyanaraman B, Lubet RA, Wang Y, You M. . Cancer Prev Res (Phila). 2014 Sep 22. pii:canprevres.0091.2014. PMCID: PMC6010030

Raguz M, Mainali L, O'Brien WJ, Subczynski WK. . Exp Eye Res. 2014 Mar;120:138-51. doi: 10.1016/j.exer.2014.01.018. PMCID: PMC3963472

Shah G, Zielonka J, Chen F, Zhang G, Cao Y, Kalyanaraman B, See W. . J Urol. 2014 Jun 10. pii: S0022-5347(14)03738-0. doi: 10.1016/j.juro.2014.05.115. PMCID: PMC5798233

Sidabras JW, Varanasi SK, Mett RR, Swarts SG, Swartz HM, Hyde JS. . Rev Sci Instrum. 2014 Oct;85(10):104707. doi: 10.1063/1.4898179. PMCID: PMC401662

Widomska J, Subczynski WK. W J Clin Exp Ophthalmol. 2014 Feb 21;5(1):326. PMCID: PMC4038937

Yu L, Vásquez-Vivar J, Jiang R, Luo K, Derrick M, Tan S. . Free Radic Biol Med. 2014 Feb;67:426-36. doi: 10.1016/j.freeradbiomed.2013.11.026. PMCID: PMC3945116

Zhuo Y, Vishnivetskiy SA, Zhan X, Gurevich VV, Klug CS. . J Biol Chem. 2014 Jul 25;289(30):20991-1002. doi: 10.1074/jbc.M114.560680. PMCID: PMC4110305

Zielonka J, Cheng G, Zielonka M, Ganesh T, Sun A, Joseph J, Michalski R, O'Brien WJ, Lambeth JD, Kalyanaraman B. . J Biol Chem. 2014 Jun 6;289(23):16176-89. doi: 10.1074/jbc.M114.548693. PMCID: PMC4047388

2013

Anderson DM, Feix JB, Monroe AL, Peterson FC, Volkman BF, Haas AL, Frank DW. . J Biol Chem. 2013 Sep 13;288(37):26741-52. doi: 10.1074/jbc.M113.478529. PMCID: PMC3772220 

Hyde JS, Bennet B, Kittell AW, Kowalski JM, Sidabris JW. . J Magn Reson 236: 15-25, 2013. PMCID: PMC3919454 

Mainali L, Hyde JS, Subczynski WK. . J Magn Reson. 2013 Jan;226:35-44. doi: 10.1016/j.jmr.2012.11.001. PMCID: PMC3529815 

Mainali L, Raguz M, O'Brien WJ, Subczynski WK. . Biochim Biophys Acta. 2013 Jun;1828(6):1432-40. doi: 10.1016/j.bbamem.2013.02.006. PMCID: PMC4323688 

Mainali L, Raguz M, Subczynski WK. . J Phys Chem B. 2013 Aug 1;117(30):8994-9003. doi: 10.1021/jp402394m. PMCID: PMC3762674 

Rice AJ, Alvarez FJD, Schultz KM, Klug CS, Davidson AL, Pinkett HW. . J. Biol. Chem. 2013;288, 21228-21235. PMCID: PMC3774390 **JBC Paper of the Week

Schultz KM, Feix JB, Klug CS. . Protein Sci. 2013 Nov;22(11):1639-45. doi: 10.1002/pro.2369.  PMCID: PMC3831678

Valez V, Cassina A, Batinic-Haberle I, Kalyanaraman B, Ferrer-Sueta G, Radi R. . Arch Biochem Biophys. 2013 Jan 1;529(1):45-54. doi: 10.1016/j.abb.2012.10.012. PMCID: PMC3534903

2012

Bansal S, Srinivasan S, Anandasadagopan S, Chowdhury AR, Selvaraj V, Kalyanaraman B, Joseph J, Avadhani NG. . J Biol Chem. 2012 May 4;287(19):15284-97. PMCID: PMC3346148 

Broniowska KA, Hogg N. . Antioxid Redox Signal. 2012 Oct 1;17(7):969-80. PMCID: PMC3411335 

Broniowska KA, Keszler A, Basu S, Kim-Shapiro DB, Hogg N. . Biochem J. 2012 Feb 15;442(1):191-7. PMCID: PMC3943432

Cheng G, Zielonka J, Dranka BP, McAllister D, Mackinnon AC Jr, Joseph J, Kalyanaraman B. . Cancer Res. 2012 May 15;72(10):2634-44. PMCID: PMC3700358 

Cunniff B, Benson K, Stumpff J, Newick K, Held P, Taatjes D, Joseph J, Kalyanaraman B, Heintz NH. . J Cell Physiol. 2012 Sep 27. doi: 10.1002/jcp.24232. PMCID: PMC3928986 

Diers AR, Broniowska KA, Chang CF, Hogg N. . Biochem J. 2012 Jun 15;444(3):561- 71. PMCID: PMC4898201

Dranka BP, Zielonka J, Kanthasamy AG, Kalyanaraman B. . J Neurochem. 2012 Jun 18. doi: 10.1111/j.1471-4159.2012.07836.x. PMCID: PMC3423581 

Drobyshevsky A, Luo K, Derrick M, Yu L, Du H, Prasad PV, Vasquez-Vivar J, Batinic-Haberle I, Tan S. . J Neurosci. 2012 Apr 18;32(16):5500-9. PMCID: PMC3332550

Francis DJ, Hubbell WL, Klug CS. . Appl. Magn. Reson. 2012, Volume 43, Number 3, Pages 405-419. PMCID: PMC4240029

Gadicherla AK, Stowe DF, Antholine WE, Yang M, Camara AK. . Biochim Biophys Acta. 2012 Mar;1817(3):419-29. PMCID: PMC3269517 

Ghosh A, Kanthasamy A, Joseph J, Anantharam V, Srivastava P, Dranka BP, Kalyanaraman B, Kanthasamy AG. . J Neuroinflammation. 2012 Oct 23;9:241. doi: 10.1186/1742-2094-9-241. PMCID: PMC3488558

Kalyanaraman B, Darley-Usmar V, Davies KJ, Dennery PA, Forman HJ, Grisham MB, Mann GE, Moore K, Roberts LJ 2nd, Ischiropoulos H. . Free Radic Biol Med. 2012 Jan 1;52(1):1-6. PMCID: PMC3911769 

Kittell AW, Hustedt EJ, Hyde JS. . J Magn Reson. 2012 Aug;221:51-6. PMCID: PMC3957363

Liddle BJ, Wanniarachchi S, Hewage JS, Lindeman SV, Bennett B, Gardinier JR. . Inorg Chem. 2012 Dec 3;51(23):12720-8. doi: 10.1021/ic301437f. PMCID: PMC3601749

Mainali L, Raguz M, O'Brien WJ, Subczynski WK. . Exp Eye Res. 2012 Apr;97(1):117-29. PMCID: PMC3287047 

Mainali L, Raguz M, Subczynski WK. . Eur Biophys J. 2012 Feb;41(2):147-59. PMCID: PMC3270143 

Mao M, Sudhahar V, Ansenberger-Fricano K, Fernandes DC, Tanaka LY, Fukai T, Laurindo FR, Mason RP, Vasquez-Vivar J, Minshall RD, Stadler K, Bonini MG. . Free Radic Biol Med. 2012 Jan 15;52(2):427-35. EPMCID: PMC3432314

Merten JA, Schultz KM, Klug CS. . Protein Sci. 2012 Feb;21(2):211-8. doi: 10.1002/pro.2004. PMCID: PMC3324765 

Michalski R, Zielonka J, Hardy M, Joseph J, Kalyanaraman B. . Free Radic Biol Med. 2012 Oct 7. doi:pii: S0891- 5849(12)01143-4. 10.1016/j.freeradbiomed.2012.09.018. PMCID: PMC3711142 

Mukhopadhyay P, Horváth B, Zsengellėr Z, Bátkai S, Cao Z, Kechrid M, Holovac E, Erdėlyi K, Tanchian G, Liaudet L, Stillman IE, Joseph J, Kalyanaraman B, Pacher P. . Free Radic Biol Med. 2012 Sep 1;53(5):1123- 38. PMCID: PMC3432152 

Mukhopadhyay P, Horváth B, Zsengellér Z, Zielonka J, Tanchian G, Holovac E, Kechrid M, Patel V, Stillman IE, Parikh SM, Joseph J, Kalyanaraman B, Pacher P. . Free Radic Biol Med. 2012 Jan 15;52(2):497-506. PMCID: PMC3253235 

Petruk AA, Bartesaghi S, Trujillo M, Estrin DA, Murgida D, Kalyanaraman B, Marti MA, Radi R. . Arch Biochem Biophys. 2012 Sep 1;525(1):82-91. PMCID: PMC3414218 

Plesnar E, Subczynski WK, Pasenkiewicz-Gierula M. . Biochim Biophys Acta. 2012 Mar;1818(3):520-9. PMCID: PMC3273590 

Sethumadhavan S, Vasquez-Vivar J, Migrino RQ, Harmann L, Jacob HJ, Lazar J. . J Biol Chem. 2012 Jun 22;287(26):22174-82. PMCID: PMC3381178 

Soberanes S, Gonzalez A, Urich D, Chiarella SE, Radigan KA, Osornio-Vargas A, Joseph J, Kalyanaraman B, Ridge KM, Chandel NS, Mutlu GM, De Vizcaya-Ruiz A, Budinger GR. . Sci Rep. 2012;2:275. PMCID: PMC3281276 

Subczynski WK, Raguz M, Widomska J, Mainali L, Konovalov A. . J Membr Biol. 2012 Jan;245(1):51-68. PMCID: PMC3288876

Subczynski WK, Wisniewska-Becker A, Widomska J. ? Acta Biochim Pol. 2012;59(1):109-14. Epub 2012 Mar 17.

Swartz HM, Flood AB, Williams BB, Dong R, Swarts SG, He X, Grinberg O, Sidabras J, Demidenko E, Gui J, Gladstone DJ, Jarvis LA, Kmiec MM, Kobayashi K, Lesniewski PN, Marsh SD, Matthews TP, Nicolalde RJ, Pennington PM, Raynolds T, Salikhov I, Wilcox DE, Zaki BI. . Health Phys. 2012 Sep;103(3):255-67. doi: 10.1097/HP.0b013e3182588d92. PMCID: PMC3649772 

Tejero J, Basu S, Helms C, Hogg N, King SB, Kim-Shapiro DB, Gladwin MT. . J Biol Chem. 2012 May 25;287(22):18262-74. PMCID: PMC3365727 

Wang J, Alexanian A, Ying R, Kizhakekuttu TJ, Dharmashankar K, Vasquez-Vivar J, Gutterman DD, Widlansky ME. . Arterioscler Thromb Vasc Biol. 2012 Mar;32(3):712-20. PMCID: PMC3319449 

Wisniewska-Becker A, Nawrocki G, Duda M, Subczynski WK. . Acta Biochim Pol. 2012;59(1):119-24. PMCID: PMC4116753 

Yin JJ, Fu PP, Lutterodt H, Zhou YT, Antholine WE, Wamer W. . J Agric Food Chem. 2012 Mar 14;60(10):2554-61. PMCID: PMC3971523 

Zielonka J, Sikora A, Hardy M, Joseph J, Dranka BP, Kalyanaraman B. . Chem Res Toxicol. 2012 Sep 17;25(9):1793- 9. PMCID: PMC3501381 

Zielonka J, Zielonka M, Sikora A, Adamus J, Joseph J, Hardy M, Ouari O, Dranka BP, Kalyanaraman B. . J Biol Chem. 2012 Jan 27;287(5):2984-95. PMCID: PMC3270955 

Zsengellér ZK, Ellezian L, Brown D, Horváth B, Mukhopadhyay P, Kalyanaraman B, Parikh SM, Karumanchi SA, Stillman IE, Pacher P. . J Histochem Cytochem. 2012 Jul;60(7):521-9. PMCID: PMC3460350

2011

Ahmed MN, Codipilly C, Hogg N, Auten RL. . Exp. Lung Res. 2011 Feb;37:10-17. 

Anderson DM, Schmalzer KM, Sato H, Casey M, Terhune SS, Haas AL, Feix JB, Frank DW. . Mol Microbiol. 2011 Dec;82(6):1454-67. doi: 10.1111/j.1365-2958.2011.07904.x. PMCID: PMC3237844

Belik J, McIntyre BA, Enomoto M, Pan J, Grasemann H, Vasquez-Vivar J. . Free Radic Biol Med. 2011 Dec 15;51(12):2227-33. PMCID: PMC5050525

Bennett B, Hill BC. . FEBS Lett. 2011 Mar 23;585(6):861-4. PMCID: PMC3109496

Benson MA, Komas SM, Schmalzer KM, Casey MS, Frank DW, Feix JB. . Biophys J. 2011 Mar 2;100(5):1335-43. PMCID: PMC3043214

Chacko BK, Srivastava A, Johnson MS, Benavides GA, Chang MJ, Ye Y, Jhala N, Murphy MP, Kalyanaraman B, Darley-Usmar VM. . Hepatology. 2011 Jul;54(1):153-63. doi: 10.1002/hep.24377. PMCID: PMC3125473

Cheng G, Lopez M, Zielonka J, Hauser AD, Joseph J, McAllister D, Rowe JJ, Sugg SL, Williams CL, Kalyanaraman B. . Cancer Biol Ther. 2011 Oct 15;12(8):707-17. PMCID: PMC3218525

Ge ZD, Ionova IA, Vladic N, Pravdic D, Hirata N, Vásquez-Vivar J, Pratt PF Jr, Warltier DC, Pieper GM, Kersten JR.. Cardiovasc Res. 2011 Jul 15;91(2):340-9. PMCID: PMC3125073

Kalyanaraman B. . Biochem Soc Trans. 2011 Oct;39(5):1221-5. 

Kalyanaraman B, Darley-Usmar V, Davies KJ, Dennery PA, Forman HJ, Grisham MB, Mann GE, Moore K, Roberts LJ 2nd, Ischiropoulos H. Measuring reactive oxygen and nitrogen species with fluorescent probes: challenges and limitations. Free Radic Biol Med. 2011 Oct 2;52:1-6. PMCID: PMC3911769

Khan SA, Nanduri J, Yuan G, Kinsman B, Kumar GK, Joseph J, Kalyanaraman B, Prabhakar NR. . Antioxid. Redox Signal. 2011 Feb 15;14:533-542. PMCID: PMC3038125

Kittell AW, Camenisch TG, Ratke JJ, Sidabras JW, Hyde JS. . J Magn Reson. 2011 Aug;211(2):228-33. PMCID: PMC3148028

Kolesar JM, Sachidanandam K, Schelman WR, Eickhoff J, Holen KD, Traynor AM, Alberti DB, Thomas JP, Chitambar CR, Wilding G, Antholine WE. C. Exp Ther Med. 2011 Jan;2(1):119-123. PMID:21373381

Kowalski JM, Bennett B. Spin Hamiltonian Parameters for Cu(II)-Prion Peptide Complexes from L-Band Electron Paramagnetic Resonance Spectroscopy. J Am Chem Soc. 2011 Jan 25. [Epub ahead of print] 

Krishnapuram R, Dhurandhar EJ, Dubuisson O, Kirk-Ballard H, Bajpeyi S, Butte NF, Sothern MS, LarsenMeyer E, Chalew S, Bennett B, Gupta AK, Greenway FL, Johnson WD, Brashear M, Reinhart G, Rankinen T, Bouchard C, Cefalu WT, Ye J, Javier R, Zuberi A, Dhurandhar NV. . Am J Physiol Endocrinol Metab. 2011 May;300(5):E779-89. PMCID: PMC3093976

Kumar SN, Konorev EA, Aggarwal D, Kalyanaraman B. . J. Proteomics J Proteomics. 2011 May 1;74(5):683-97. PMCID: PMC3298037

Leskov IL, Whitsett J, Vasquez-Vivar J, Stokes KY. . Free Radic Biol Med. 2011 Dec 15;51(12):2300-8. PMCID: PMC3272703

Mainali L, Feix JB, Hyde JS, Subczynski WK. J Magn Reson. 2011 Oct;212(2):418-25. PMCID: PMC3214655

Mainali L, Raguz M, Camenisch TG, Hyde JS, Subczynski WK. . J Magn Reson. 2011 Sep;212(1):86-94. PMCID: PMC3163743

Mainali L, Raguz M, Subczynski WK. . Biophys J. 2011 Aug 17;101(4):837-46. PMCID: PMC3175055

Mett RR, Sidabras JW, Anderson JR, Hyde JS. . Rev Sci Instrum. 2011 Jul;82(7):074704. PMCID: PMC4798996

Murphy MP, Holmgren A, Larsson NG, Halliwell B, Chang CJ, Kalyanaraman B, Rhee SG, Thornalley PJ, Partridge L, Gems D, Nyström T, Belousov V, Schumacker PT, Winterbourn CC. . Cell. Metab. 2011 Apr 6;13:361-366. PMCID: PMC4445605

Myers JM, Antholine WE, Myers CR. . Toxicology. 2011 Mar 15;281(1-3):37-47. PMCID: PMC3039098

Myers JM, Antholine WE, Zielonka J, Myers CR. . Toxicol Lett. 2011 Mar 5;201(2):130-6.  PMCID: PMC21195754

Patel RP, Hogg N, Kim-Shapiro DB. . Cardiovasc. Res. 2011 Feb;89:507-515. PMCID: PMC3028972

Raguz M, Mainali L, Widomska J, Subczynski WK. . Biochim Biophys Acta. 2011 Apr;1808(4):1072-80. PMCID: PMC3062709

Raguz M, Mainali L, Widomska J, Subczynski WK. . Chem Phys Lipids. 2011 Aug 9.2011 Nov;164(8):819-29. PMCID: PMC3206151

Schultz KM, Merten JA, Klug CS. Characterization of the E506Q and H537A Dysfunctional Mutants in the E. coli ABC Transporter MsbA. Biochemistry. 2011 May 10;50(18):3599-608. PMCID: PMC3128438

Schultz KM, Merten JA, Klug CS. . 2011 Apr 5;50(13):2594-602. PMCID: PMC3110719

Sikora A, Zielonka J, Lopez M, Dybala-Defratyka A, Joseph J, Marcinek A, Kalyanaraman B. . Chem Res Toxicol. 2011 May 16;24(5):687-97. PMCID: PMC3743543

Subczynski WK, Mainali L, Camenisch TG, Froncisz W, Hyde JS. . J Magn Reson. 2011 Apr;209(2):142-8. PMCID: PMC3065517

Vishnivetskiy SA, Gimenez LE, Francis DJ, Hunson SM, Hubbell WL, Klug CS, Gurevich VV. . J Biol Chem. 2011 Jul 8;286(27):24288-99. PMCID: PMC3129209

Wanniarachchi S, Liddle BJ, Toussaint J, Lindeman SV, Bennett B, Gardinier JR. . Dalton Trans. 2011 Sep 21;40(35):8776-87. 

Yu L, Derrick M, Ji H, Silverman RB, Whitsett J, Vásquez-Vivar J, Tan S. . Dev Neurosci. 2011;33(3-4):312-9. PMCID: PMC3225251

Zhu BZ, Mao L, Fan RM, Zhu JG, Zhang YN, Wang J, Kalyanaraman B, Frei B. . Chem. Res. Toxicol. 2011 Jan 14;24:30-34.

2010

Bodemer GJ, Antholine WA, Basova LV, Saffarini D, Pacheco AA. . J Biol Inorg Chem. 2010 Jun;15(5):749-58. 

Chandran K, McCracken J, Peterson FC, Antholine WE, Volkman BF, Kalyanaraman B. . Biochemistry. 2010 Nov 1;49:10616-22.

Cheng Q, Antholine WE, Myers JM, Kalyanaraman B, Arnér ES, Myers CR. . J Biol Chem. 2010 Jul 9;285(28):21708-23. PMCID: PMC2898413

Choi DW, Bandow NL, McEllistrem MT, Semrau JD, Antholine WE, Hartsel SC, Gallagher W, Zea CJ, Pohl NL, Zahn JA, DiSpirito AA. . J Inorg Biochem. 2010 Dec;104(12):1240-7.

Farver O, Wherland S, Antholine WE, Gemmen GJ, Chen Y, Pecht I, Fee JA. Pulse radiolysis studies of temperature dependent electron transfers among redox centers in ba3-cytochrome c oxidase from Thermus thermophilus: Comparison of A- and B-type enzymes. Biochemistry. 2010 Oct 28. [Epub ahead of print] 

Ghosh A, Chandran K, Kalivendi SV, Joseph J, Antholine WE, Hillard CJ, Kanthasamy A, Kanthasamy A, Kalyanaraman B. l. Free Radic Biol Med. 2010 Dec 1;49(11):1674-84. PMCID: PMC4020411

Goetz BI, Shields HW, Basu S, Wang P, King SB, Hogg N, Gladwin MT, Kim-Shapiro DB.. Nitric Oxide. 2010 Feb 15;22(2):149-54. PMCID: PMC2819623

Hogg N. . Free Radic Biol Med. 2010 Jul 15;49(2):122-9. PMCID: PMC2916063

Hyde JS, Strangeway RA, Camenisch TG, Ratke JJ, Froncisz W. . J Magn Reson. 2010 Jul;205(1):93-101. PMCID: PMC2885579 

Keszler A, Zhang Y, Hogg N. Free Radic. Biol. Med. 2010 Jan 1;48:55-64. PMCID: PMC2829852

Limphong P, McKinney RM, Adams NE, Makaroff CA, Bennett B, Crowder MW. . J. Biol. Inorg. Chem. 2010 Feb;15:249-258. 

Myers CR, Antholine WE, Myers JM. . Free Radic Biol Med. 2010 Sep 27;49:1903-1915.

Subczynski WK, Raguz M, Widomska J. . Methods Mol. Biol. 2010;606:247-269.  PMCID: PMC4640678

Subczynski WK, Wisniewska A, Widomska J. . Arch Biochem Biophys. 2010 Dec 1;504(1):61-6. PMCID: PMC2957566

Vishnivetskiy SA, Francis D, Van Eps N, Kim M, Hanson SM, Klug CS, Hubbell WL, Gurevich VV. . J. Mol. Biol. 10 Jan;395:42-54. PMCID: PMC2787876

Zhu BZ, Mao L, Fan RM, Zhu JG, Zhang YN, Wang J, Kalyanaraman B, Frei B. . Chem Res Toxicol. 2010 Nov 3;24:30-34.

Zielonka J, Sikora A, Joseph J, Kalyanaraman B. . J Biol Chem. 2010 May 7;285(19):14210-6. PMCID: PMC2863194

Policies for Users & Collaborators

EPR Center users are requested to include the collaborating faculty member as an author on any publications that wholly or in part involve work carried out at the EPR Center. Any such publications should cite, if appropriate, the DEER instrumentation grants (NIH grants RR022422 and OD011937).