| Year |
Citation |
Score |
| 2021 |
Schipper S, Wu H, Furdui CM, Poole LB, Delahunty CM, Park R, Yates JR, Becker K, Przyborski JM. Identification of sulfenylation patterns in trophozoite stage Plasmodium falciparum using a non-dimedone based probe. Molecular and Biochemical Parasitology. 111362. PMID 33513391 DOI: 10.1016/j.molbiopara.2021.111362 |
0.312 |
|
| 2020 |
Poole LB, Furdui CM, King SB. Introduction to approaches and tools for the evaluation of protein cysteine oxidation. Essays in Biochemistry. PMID 32031597 DOI: 10.1042/Ebc20190050 |
0.414 |
|
| 2019 |
Randall LM, Rizza JD, Parsonage D, Santos J, Mehl RA, Lowther WT, Poole LB, Denicola A. Unraveling the effects of peroxiredoxin 2 nitration; role of C-terminal tyrosine 193. Free Radical Biology & Medicine. PMID 31323313 DOI: 10.1016/J.Freeradbiomed.2019.07.016 |
0.481 |
|
| 2019 |
Li Z, Forshaw TE, Holmila RJ, Vance SA, Wu H, Poole LB, Furdui CM, King SB. Triphenyl Phosphonium (TPP)-Derived Protein Sulfenic Acid Trapping Agents: Synthesis, Reactivity and Effect on Mitochondrial Function. Chemical Research in Toxicology. PMID 30784263 DOI: 10.1021/Acs.Chemrestox.8B00385 |
0.432 |
|
| 2019 |
Teixeira F, Tse E, Castro H, Makepeace KAT, Meinen BA, Borchers CH, Poole LB, Bardwell JC, Tomás AM, Southworth DR, Jakob U. Chaperone activation and client binding of a 2-cysteine peroxiredoxin. Nature Communications. 10: 659. PMID 30737390 DOI: 10.2210/Pdb6E0G/Pdb |
0.407 |
|
| 2019 |
Collins JA, Wood ST, Bolduc JA, Nurmalasari NPD, Chubinskaya S, Poole LB, Furdui CM, Nelson KJ, Loeser RF. Differential Peroxiredoxin Hyperoxidation Regulates MAP Kinase Signaling in Human Articular Chondrocytes. Free Radical Biology & Medicine. PMID 30639614 DOI: 10.1016/J.Freeradbiomed.2019.01.005 |
0.327 |
|
| 2018 |
Poole LB, Thorpe C. Redox Proteins. Protein Science : a Publication of the Protein Society. PMID 30461094 DOI: 10.1002/Pro.3555 |
0.378 |
|
| 2018 |
Vukelic S, Xu Q, Seidel-Rogol B, Faidley EA, Dikalova AE, Hilenski LL, Jorde U, Poole LB, Lassègue B, Zhang G, Griendling KK. NOX4 (NADPH Oxidase 4) and Poldip2 (Polymerase δ-Interacting Protein 2) Induce Filamentous Actin Oxidation and Promote Its Interaction With Vinculin During Integrin-Mediated Cell Adhesion. Arteriosclerosis, Thrombosis, and Vascular Biology. 38: 2423-2434. PMID 30354218 DOI: 10.1161/Atvbaha.118.311668 |
0.338 |
|
| 2018 |
Nelson KJ, Bolduc JA, Wu H, Collins JA, Burke EA, Reisz JA, Klomsiri C, Wood ST, Yammani RR, Poole LB, Furdui CM, Loeser RF. HO oxidation of cysteine residues in c-Jun N-terminal kinase 2 (JNK2) contributes to redox regulation in human articular chondrocytes. The Journal of Biological Chemistry. PMID 30190325 DOI: 10.1074/Jbc.Ra118.004613 |
0.422 |
|
| 2018 |
Al-Barakati HJ, McConnell EW, Hicks LM, Poole LB, Newman RH, Kc DB. SVM-SulfoSite: A support vector machine based predictor for sulfenylation sites. Scientific Reports. 8: 11288. PMID 30050050 DOI: 10.1038/S41598-018-29126-X |
0.4 |
|
| 2018 |
Bolduc JA, Nelson KJ, Haynes AC, Lee J, Reisz JA, Graff AH, Clodfelter JE, Parsonage D, Poole LB, Furdui CM, Lowther WT. Novel hyperoxidation resistance motifs in 2-Cys peroxiredoxins. The Journal of Biological Chemistry. PMID 29884768 DOI: 10.1074/Jbc.Ra117.001690 |
0.359 |
|
| 2018 |
Holmila RJ, Vance SA, Chen X, Wu H, Shukla K, Bharadwaj MS, Mims J, Wary Z, Marrs G, Singh R, Molina AJ, Poole LB, King SB, Furdui CM. Mitochondria-targeted Probes for Imaging Protein Sulfenylation. Scientific Reports. 8: 6635. PMID 29703899 DOI: 10.1038/S41598-018-24493-X |
0.35 |
|
| 2018 |
Portillo-Ledesma S, Randall LM, Parsonage D, Dalla Rizza J, Karplus PA, Poole LB, Denicola A, Ferrer-Sueta G. Differential Kinetics of Two-Cysteine Peroxiredoxin Disulfide Formation Reveal a Novel Model for Peroxide Sensing. Biochemistry. PMID 29553725 DOI: 10.1021/Acs.Biochem.8B00188 |
0.424 |
|
| 2018 |
Postiglione A, Keyes J, Patwardhan S, Hampton L, Delva-Wiley J, Jeong JS, Poole LB, Newman RH. Impact of Redox Modification on Global Kinase Substrate Selection Free Radical Biology and Medicine. 128: S6. DOI: 10.1016/J.Freeradbiomed.2018.10.381 |
0.406 |
|
| 2017 |
Long D, Wu H, Tsang AW, Poole LB, Yoza BK, Wang X, Vachharajani V, Furdui CM, McCall CE. The Oxidative State of Cysteine Thiol 144 Regulates the SIRT6 Glucose Homeostat. Scientific Reports. 7: 11005. PMID 28887543 DOI: 10.1038/S41598-017-11388-6 |
0.314 |
|
| 2017 |
Keyes JD, Parsonage D, Yammani RD, Rogers LAC, Kesty C, Furdui CM, Nelson KJ, Poole LB. Endogenous, Regulatory Cysteine Sulfenylation of ERK Kinases in Response to Proliferative Signals. Free Radical Biology & Medicine. PMID 28843779 DOI: 10.1016/J.Freeradbiomed.2017.08.018 |
0.32 |
|
| 2017 |
Chen X, Wu H, Park CM, Poole TH, Keceli G, Devarie Baez NO, Tsang AW, Lowther WT, Poole LB, King SB, Xian M, Furdui CM. Discovery of Heteroaromatic Sulfones As A New Class of Biologically Compatible Thiol-Selective Reagents. Acs Chemical Biology. PMID 28687042 DOI: 10.1021/Acschembio.7B00444 |
0.379 |
|
| 2017 |
Mauney C, Rogers L, Harris R, Daniel L, Devarie-Baez N, Wu H, Furdui C, Poole LB, Perrino F, Hollis T. The SAMHD1 dNTP triphosphohydrolase is controlled by a redox switch. Antioxidants & Redox Signaling. PMID 28398823 DOI: 10.1089/Ars.2016.6888 |
0.418 |
|
| 2017 |
Nelson KJ, Perkins A, Van Swearingen AE, Hartman S, Brereton AE, Parsonage D, Salsbury FR, Karplus PA, Poole LB. Experimentally Dissecting the Origins of Peroxiredoxin Catalysis. Antioxidants & Redox Signaling. PMID 28375740 DOI: 10.1089/Ars.2016.6922 |
0.416 |
|
| 2017 |
Harper AF, Leuthaeuser JB, Babbitt PC, Morris JH, Ferrin TE, Poole LB, Fetrow JS. An Atlas of Peroxiredoxins Created Using an Active Site Profile-Based Approach to Functionally Relevant Clustering of Proteins. Plos Computational Biology. 13: e1005284. PMID 28187133 DOI: 10.1371/Journal.Pcbi.1005284 |
0.322 |
|
| 2017 |
Keyes JD, Postiglione A, Patwardhan S, Smith-Pearson P, Parsonage D, Newman RH, Poole LB. Impact of Redox Modifications on ERK2 Substrate Phosphorylation Free Radical Biology and Medicine. 112: 193-194. DOI: 10.1016/J.Freeradbiomed.2017.10.305 |
0.384 |
|
| 2016 |
Perkins A, Parsonage D, Nelson KJ, Ogba OM, Cheong PH, Poole LB, Karplus PA. Peroxiredoxin Catalysis at Atomic Resolution. Structure (London, England : 1993). PMID 27594682 DOI: 10.1016/J.Str.2016.07.012 |
0.399 |
|
| 2016 |
Parsonage D, Sheng F, Hirata K, Debnath A, McKerrow JH, Reed SL, Abagyan R, Poole LB, Podust LM. X-ray structures of thioredoxin and thioredoxin reductase from Entamoeba histolytica and prevailing hypothesis of the mechanism of Auranofin action. Journal of Structural Biology. PMID 26876147 DOI: 10.1016/J.Jsb.2016.02.015 |
0.37 |
|
| 2016 |
Collins JA, Wood ST, Nelson KJ, Rowe MA, Carlson CS, Chubinskaya S, Poole LB, Furdui CM, Loeser RF. Oxidative Stress Promotes Peroxiredoxin Hyperoxidation and Attenuates Pro-survival Signalling in Aging Chondrocytes. The Journal of Biological Chemistry. PMID 26797130 DOI: 10.1074/Jbc.M115.693523 |
0.327 |
|
| 2016 |
Collins J, Wood S, Poole L, Furdui C, Loeser R. The level of reactive oxygen species differentially regulates peroxiredoxin oxidation and mitogen-activated protein kinase signaling in human chondrocytes Osteoarthritis and Cartilage. 24: S179-S180. DOI: 10.1016/J.Joca.2016.01.354 |
0.38 |
|
| 2016 |
Holmila R, Wu H, Chen X, Poole T, Park C, Poole LB, Xian M, Tsang AW, Bruce King S, Furdui CM. Selective Reagents for Analysis of Redox Effects in Biological Systems Free Radical Biology and Medicine. 100: S23. DOI: 10.1016/J.Freeradbiomed.2016.10.054 |
0.357 |
|
| 2015 |
Randall L, Manta B, Nelson KJ, Santos J, Poole LB, Denicola A. Structural changes upon peroxynitrite-mediated nitration of peroxiredoxin 2; nitrated Prx2 resembles its disulfide-oxidized form. Archives of Biochemistry and Biophysics. PMID 26612102 DOI: 10.1016/J.Abb.2015.11.032 |
0.445 |
|
| 2015 |
Buchko GW, Perkins A, Parsonage D, Poole LB, Karplus PA. Backbone chemical shift assignments for Xanthomonas campestris peroxiredoxin Q in the reduced and oxidized states: a dramatic change in backbone dynamics. Biomolecular Nmr Assignments. PMID 26438558 DOI: 10.1007/S12104-015-9637-8 |
0.359 |
|
| 2015 |
Wood ST, Long DL, Reisz JA, Yammani RR, Burke EA, Klomsiri C, Poole LB, Furdui CM, Loeser RF. Cysteine-Mediated Redox Regulation of Cell Signaling in Chondrocytes Stimulated with Fibronectin Fragments. Arthritis & Rheumatology (Hoboken, N.J.). PMID 26314228 DOI: 10.1002/Art.39326 |
0.39 |
|
| 2015 |
Perkins A, Nelson KJ, Parsonage D, Poole LB, Karplus PA. Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling. Trends in Biochemical Sciences. 40: 435-45. PMID 26067716 DOI: 10.1016/J.Tibs.2015.05.001 |
0.44 |
|
| 2015 |
Poole LB, Schöneich C. Introduction: What we do and do not know regarding redox processes of thiols in signaling pathways. Free Radical Biology & Medicine. 80: 145-7. PMID 25746478 DOI: 10.1016/J.Freeradbiomed.2015.02.005 |
0.417 |
|
| 2015 |
Parsonage D, Nelson KJ, Ferrer-Sueta G, Alley S, Karplus PA, Furdui CM, Poole LB. Dissecting peroxiredoxin catalysis: separating binding, peroxidation, and resolution for a bacterial AhpC. Biochemistry. 54: 1567-75. PMID 25633283 DOI: 10.1021/Bi501515W |
0.438 |
|
| 2015 |
Poole LB. The basics of thiols and cysteines in redox biology and chemistry. Free Radical Biology & Medicine. 80: 148-57. PMID 25433365 DOI: 10.1016/J.Freeradbiomed.2014.11.013 |
0.399 |
|
| 2015 |
Keceli G, Wu H, Devarie-Baez NO, Bruce King S, Poole LB, Furdui CM. Strategies to Investigate the Redox Biology of Sulfenic Acids in Cells Free Radical Biology and Medicine. 87: S16. DOI: 10.1016/J.Freeradbiomed.2015.10.046 |
0.314 |
|
| 2014 |
Perkins A, Poole LB, Karplus PA. Tuning of peroxiredoxin catalysis for various physiological roles. Biochemistry. 53: 7693-705. PMID 25403613 DOI: 10.1021/Bi5013222 |
0.413 |
|
| 2014 |
Poole TH, Reisz JA, Zhao W, Poole LB, Furdui CM, King SB. Strained cycloalkynes as new protein sulfenic acid traps. Journal of the American Chemical Society. 136: 6167-70. PMID 24724926 DOI: 10.1021/Ja500364R |
0.437 |
|
| 2014 |
Randall LM, Manta B, Hugo M, Gil M, Batthyà ny C, Trujillo M, Poole LB, Denicola A. Nitration transforms a sensitive peroxiredoxin 2 into a more active and robust peroxidase. The Journal of Biological Chemistry. 289: 15536-43. PMID 24719319 DOI: 10.1074/Jbc.M113.539213 |
0.463 |
|
| 2014 |
Klomsiri C, Rogers LC, Soito L, McCauley AK, King SB, Nelson KJ, Poole LB, Daniel LW. Endosomal H2O2 production leads to localized cysteine sulfenic acid formation on proteins during lysophosphatidic acid-mediated cell signaling. Free Radical Biology & Medicine. 71: 49-60. PMID 24657741 DOI: 10.1016/J.Freeradbiomed.2014.03.017 |
0.453 |
|
| 2014 |
Furdui CM, Poole LB. Chemical approaches to detect and analyze protein sulfenic acids. Mass Spectrometry Reviews. 33: 126-46. PMID 24105931 DOI: 10.1002/Mas.21384 |
0.414 |
|
| 2013 |
Perkins A, Nelson KJ, Williams JR, Parsonage D, Poole LB, Karplus PA. The sensitive balance between the fully folded and locally unfolded conformations of a model peroxiredoxin. Biochemistry. 52: 8708-21. PMID 24175952 DOI: 10.1021/Bi4011573 |
0.409 |
|
| 2013 |
Reisz JA, Bechtold E, King SB, Poole LB, Furdui CM. Thiol-blocking electrophiles interfere with labeling and detection of protein sulfenic acids. The Febs Journal. 280: 6150-61. PMID 24103186 DOI: 10.1111/Febs.12535 |
0.466 |
|
| 2013 |
Nelson KJ, Parsonage D, Karplus PA, Poole LB. Evaluating peroxiredoxin sensitivity toward inactivation by peroxide substrates. Methods in Enzymology. 527: 21-40. PMID 23830624 DOI: 10.1016/B978-0-12-405882-8.00002-7 |
0.373 |
|
| 2013 |
David Keyes J, Klomsiri C, Nelson K, Poole L. Modulation of Erk Activity by Reversible Cysteine Modification Free Radical Biology and Medicine. 65: S160. DOI: 10.1016/J.Freeradbiomed.2013.10.799 |
0.314 |
|
| 2013 |
Nelson KJ, Knutson ST, Parsonage D, Fetrow JS, Andrew Karplus P, Poole LB. Comparison of Peroxiredoxin Sensitivity towards Inactivation by Peroxide Substrates Free Radical Biology and Medicine. 65: S92. DOI: 10.1016/J.Freeradbiomed.2013.10.619 |
0.326 |
|
| 2012 |
Lang BS, Gorren AC, Oberdorfer G, Wenzl MV, Furdui CM, Poole LB, Mayer B, Gruber K. Vascular bioactivation of nitroglycerin by aldehyde dehydrogenase-2: reaction intermediates revealed by crystallography and mass spectrometry. The Journal of Biological Chemistry. 287: 38124-34. PMID 22988236 DOI: 10.1074/Jbc.M112.371716 |
0.417 |
|
| 2012 |
Perkins A, Gretes MC, Nelson KJ, Poole LB, Karplus PA. Mapping the active site helix-to-strand conversion of CxxxxC peroxiredoxin Q enzymes. Biochemistry. 51: 7638-50. PMID 22928725 DOI: 10.1021/Bi301017S |
0.414 |
|
| 2012 |
Salsbury FR, Poole LB, Fetrow JS. Electrostatics of cysteine residues in proteins: parameterization and validation of a simple model. Proteins. 80: 2583-91. PMID 22777874 DOI: 10.1002/Prot.24142 |
0.336 |
|
| 2012 |
Crump KE, Juneau DG, Poole LB, Haas KM, Grayson JM. The reversible formation of cysteine sulfenic acid promotes B-cell activation and proliferation. European Journal of Immunology. 42: 2152-64. PMID 22674013 DOI: 10.1002/Eji.201142289 |
0.396 |
|
| 2012 |
Cho SH, Parsonage D, Thurston C, Dutton RJ, Poole LB, Collet JF, Beckwith J. A new family of membrane electron transporters and its substrates, including a new cell envelope peroxiredoxin, reveal a broadened reductive capacity of the oxidative bacterial cell envelope. Mbio. 3. PMID 22493033 DOI: 10.1128/Mbio.00291-11 |
0.472 |
|
| 2012 |
Qian J, Wani R, Klomsiri C, Poole LB, Tsang AW, Furdui CM. A simple and effective strategy for labeling cysteine sulfenic acid in proteins by utilization of β-ketoesters as cleavable probes. Chemical Communications (Cambridge, England). 48: 4091-3. PMID 22430672 DOI: 10.1039/C2Cc17868K |
0.325 |
|
| 2012 |
Salsbury FR, Yuan Y, Knaggs MH, Poole LB, Fetrow JS. Structural and electrostatic asymmetry at the active site in typical and atypical peroxiredoxin dimers. The Journal of Physical Chemistry. B. 116: 6832-43. PMID 22401569 DOI: 10.1021/Jp212606K |
0.366 |
|
| 2012 |
Lang BS, Gorren AC, Oberdorfer G, Wenzl M, Furdui CM, Poole LB, Mayer B, Gruber K. Vascular bioactivation of nitroglycerin: reaction mechanism revealed by crystal structure of aldehyde dehydrogenase-2 Bmc Pharmacology and Toxicology. 13: A37. DOI: 10.1186/2050-6511-13-S1-A37 |
0.345 |
|
| 2012 |
Nelson KJ, Parsonage D, Van Swearingen AE, Yuan Y, Salsbury FR, Hall A, Andrew Karplus P, Poole LB. Specific Residues in Peroxiredoxins Promote Peroxide Reactivity Through Effects on Cysteine pKa, Transition State Stabilization and Oligomerization Free Radical Biology and Medicine. 53: S151. DOI: 10.1016/J.Freeradbiomed.2012.10.411 |
0.314 |
|
| 2012 |
Daniel LW, Klomsiri C, Rogers LC, Nelson KJ, Soito L, Bruce King S, Poole LB. Localized Hydrogen Peroxide-Dependent Cysteine Oxidation Is Required for Lysophosphatidic Acid Signaling in Ovarian and Prostate Cancer Cells Free Radical Biology and Medicine. 53: S33. DOI: 10.1016/J.Freeradbiomed.2012.10.083 |
0.33 |
|
| 2011 |
Reeves SA, Parsonage D, Nelson KJ, Poole LB. Kinetic and thermodynamic features reveal that Escherichia coli BCP is an unusually versatile peroxiredoxin. Biochemistry. 50: 8970-81. PMID 21910476 DOI: 10.1021/Bi200935D |
0.38 |
|
| 2011 |
Poole LB, Hall A, Nelson KJ. Overview of peroxiredoxins in oxidant defense and redox regulation. Current Protocols in Toxicology / Editorial Board, Mahin D. Maines (Editor-in-Chief) ... [Et Al.]. Unit7.9. PMID 21818754 DOI: 10.1002/0471140856.Tx0709S49 |
0.416 |
|
| 2011 |
Kaplan N, Urao N, Furuta E, Kim SJ, Razvi M, Nakamura Y, McKinney RD, Poole LB, Fukai T, Ushio-Fukai M. Localized cysteine sulfenic acid formation by vascular endothelial growth factor: role in endothelial cell migration and angiogenesis. Free Radical Research. 45: 1124-35. PMID 21740309 DOI: 10.3109/10715762.2011.602073 |
0.344 |
|
| 2011 |
Qian J, Klomsiri C, Wright MW, King SB, Tsang AW, Poole LB, Furdui CM. Simple synthesis of 1,3-cyclopentanedione derived probes for labeling sulfenic acid proteins. Chemical Communications (Cambridge, England). 47: 9203-5. PMID 21738918 DOI: 10.1039/C1Cc12127H |
0.349 |
|
| 2011 |
Wani R, Qian J, Yin L, Bechtold E, King SB, Poole LB, Paek E, Tsang AW, Furdui CM. Isoform-specific regulation of Akt by PDGF-induced reactive oxygen species. Proceedings of the National Academy of Sciences of the United States of America. 108: 10550-5. PMID 21670275 DOI: 10.1073/Pnas.1011665108 |
0.382 |
|
| 2011 |
Clarke TE, Romanov V, Chirgadze YN, Klomsiri C, Kisselman G, Wu-Brown J, Poole LB, Pai EF, Chirgadze NY. Crystal structure of alkyl hydroperoxidase D like protein PA0269 from Pseudomonas aeruginosa: homology of the AhpD-like structural family. Bmc Structural Biology. 11: 27. PMID 21615954 DOI: 10.1186/1472-6807-11-27 |
0.404 |
|
| 2011 |
Nirudodhi S, Parsonage D, Karplus PA, Poole LB, Maier CS. Conformational studies of the robust 2-Cys peroxiredoxin Salmonella typhimurium AhpC by solution phase hydrogen/deuterium (H/D) exchange monitored by electrospray ionization mass spectrometry. International Journal of Mass Spectrometry. 302: 93-100. PMID 21516234 DOI: 10.1016/J.Ijms.2010.08.018 |
0.402 |
|
| 2011 |
Nelson KJ, Knutson ST, Soito L, Klomsiri C, Poole LB, Fetrow JS. Analysis of the peroxiredoxin family: using active-site structure and sequence information for global classification and residue analysis. Proteins. 79: 947-64. PMID 21287625 DOI: 10.1002/Prot.22936 |
0.385 |
|
| 2011 |
Soito L, Williamson C, Knutson ST, Fetrow JS, Poole LB, Nelson KJ. PREX: PeroxiRedoxin classification indEX, a database of subfamily assignments across the diverse peroxiredoxin family. Nucleic Acids Research. 39: D332-7. PMID 21036863 DOI: 10.1093/Nar/Gkq1060 |
0.367 |
|
| 2011 |
Hall A, Nelson K, Poole LB, Karplus PA. Structure-based insights into the catalytic power and conformational dexterity of peroxiredoxins. Antioxidants & Redox Signaling. 15: 795-815. PMID 20969484 DOI: 10.1089/Ars.2010.3624 |
0.404 |
|
| 2011 |
Klomsiri C, Karplus PA, Poole LB. Cysteine-based redox switches in enzymes. Antioxidants & Redox Signaling. 14: 1065-77. PMID 20799881 DOI: 10.1089/Ars.2010.3376 |
0.403 |
|
| 2011 |
Olex AL, Westwood BM, Poole LB, Fetrow JS. Metabolic pathways are affected differently in Saccharomyces cerevisiae thiol peroxidase mutants during redox stress with hydrogen peroxide Genome Biology. 12: P16. DOI: 10.1186/Gb-2011-12-S1-P16 |
0.315 |
|
| 2011 |
Qian J, Klomsiri C, King SB, Poole LB, Tsang AW, Furdui CM. Simple Synthesis of Chemical Probes for Labeling Sulfenic Acid Proteins Free Radical Biology and Medicine. 51: S20. DOI: 10.1016/J.Freeradbiomed.2011.10.045 |
0.349 |
|
| 2010 |
Saunders JA, Rogers LC, Klomsiri C, Poole LB, Daniel LW. Reactive oxygen species mediate lysophosphatidic acid induced signaling in ovarian cancer cells. Free Radical Biology & Medicine. 49: 2058-67. PMID 20934509 DOI: 10.1016/J.Freeradbiomed.2010.10.663 |
0.325 |
|
| 2010 |
Hall A, Parsonage D, Poole LB, Karplus PA. Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization. Journal of Molecular Biology. 402: 194-209. PMID 20643143 DOI: 10.1016/J.Jmb.2010.07.022 |
0.422 |
|
| 2010 |
Parsonage D, Reeves SA, Karplus PA, Poole LB. Engineering of fluorescent reporters into redox domains to monitor electron transfers. Methods in Enzymology. 474: 1-21. PMID 20609901 DOI: 10.1016/S0076-6879(10)74001-5 |
0.38 |
|
| 2010 |
Nelson KJ, Klomsiri C, Codreanu SG, Soito L, Liebler DC, Rogers LC, Daniel LW, Poole LB. Use of dimedone-based chemical probes for sulfenic acid detection methods to visualize and identify labeled proteins. Methods in Enzymology. 473: 95-115. PMID 20513473 DOI: 10.1016/S0076-6879(10)73004-4 |
0.484 |
|
| 2010 |
Klomsiri C, Nelson KJ, Bechtold E, Soito L, Johnson LC, Lowther WT, Ryu SE, King SB, Furdui CM, Poole LB. Use of dimedone-based chemical probes for sulfenic acid detection evaluation of conditions affecting probe incorporation into redox-sensitive proteins. Methods in Enzymology. 473: 77-94. PMID 20513472 DOI: 10.1016/S0076-6879(10)73003-2 |
0.457 |
|
| 2010 |
Yuan Y, Knaggs M, Poole L, Fetrow J, Salsbury F. Conformational and oligomeric effects on the cysteine pK(a) of tryparedoxin peroxidase. Journal of Biomolecular Structure & Dynamics. 28: 51-70. PMID 20476795 DOI: 10.1080/07391102.2010.10507343 |
0.336 |
|
| 2010 |
Parsonage D, Desrosiers DC, Hazlett KR, Sun Y, Nelson KJ, Cox DL, Radolf JD, Poole LB. Broad specificity AhpC-like peroxiredoxin and its thioredoxin reductant in the sparse antioxidant defense system of Treponema pallidum. Proceedings of the National Academy of Sciences of the United States of America. 107: 6240-5. PMID 20304799 DOI: 10.1073/Pnas.0910057107 |
0.431 |
|
| 2010 |
Bechtold E, Reisz JA, Klomsiri C, Tsang AW, Wright MW, Poole LB, Furdui CM, King SB. Water-soluble triarylphosphines as biomarkers for protein S-nitrosation. Acs Chemical Biology. 5: 405-14. PMID 20146502 DOI: 10.1021/Cb900302U |
0.412 |
|
| 2009 |
Hall A, Sankaran B, Poole LB, Karplus PA. Structural changes common to catalysis in the Tpx peroxiredoxin subfamily. Journal of Molecular Biology. 393: 867-81. PMID 19699750 DOI: 10.1016/J.Jmb.2009.08.040 |
0.308 |
|
| 2009 |
Hall A, Karplus PA, Poole LB. Typical 2-Cys peroxiredoxins--structures, mechanisms and functions. The Febs Journal. 276: 2469-77. PMID 19476488 DOI: 10.1111/J.1742-4658.2009.06985.X |
0.427 |
|
| 2009 |
Hall A, Parsonage D, Horita D, Karplus PA, Poole LB, Barbar E. Redox-dependent dynamics of a dual thioredoxin fold protein: evolution of specialized folds. Biochemistry. 48: 5984-93. PMID 19459661 DOI: 10.1021/Bi900270W |
0.438 |
|
| 2008 |
Poole LB. Measurement of protein sulfenic acid content. Current Protocols in Toxicology / Editorial Board, Mahin D. Maines (Editor-in-Chief) ... [Et Al.]. Unit17.2. PMID 20963754 DOI: 10.1002/0471140856.Tx1702S38 |
0.46 |
|
| 2008 |
Hutson SM, Poole LB, Coles S, Conway ME. Redox regulation and trapping sulfenic acid in the peroxide-sensitive human mitochondrial branched chain aminotransferase. Methods in Molecular Biology (Clifton, N.J.). 476: 139-52. PMID 19157014 DOI: 10.1007/978-1-59745-129-1_10 |
0.446 |
|
| 2008 |
Nelson KJ, Parsonage D, Hall A, Karplus PA, Poole LB. Cysteine pK(a) values for the bacterial peroxiredoxin AhpC. Biochemistry. 47: 12860-8. PMID 18986167 DOI: 10.1021/Bi801718D |
0.397 |
|
| 2008 |
Smith-Pearson PS, Kooshki M, Spitz DR, Poole LB, Zhao W, Robbins ME. Decreasing peroxiredoxin II expression decreases glutathione, alters cell cycle distribution, and sensitizes glioma cells to ionizing radiation and H(2)O(2). Free Radical Biology & Medicine. 45: 1178-89. PMID 18718523 DOI: 10.1016/J.Freeradbiomed.2008.07.015 |
0.314 |
|
| 2008 |
Poole LB, Nelson KJ. Discovering mechanisms of signaling-mediated cysteine oxidation. Current Opinion in Chemical Biology. 12: 18-24. PMID 18282483 DOI: 10.1016/J.Cbpa.2008.01.021 |
0.438 |
|
| 2008 |
Salsbury FR, Knutson ST, Poole LB, Fetrow JS. Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid. Protein Science : a Publication of the Protein Society. 17: 299-312. PMID 18227433 DOI: 10.1110/Ps.073096508 |
0.438 |
|
| 2008 |
Yamamoto Y, Ritz D, Planson AG, Jönsson TJ, Faulkner MJ, Boyd D, Beckwith J, Poole LB. Mutant AhpC peroxiredoxins suppress thiol-disulfide redox deficiencies and acquire deglutathionylating activity. Molecular Cell. 29: 36-45. PMID 18206967 DOI: 10.1016/J.Molcel.2007.11.029 |
0.444 |
|
| 2008 |
Parsonage D, Karplus PA, Poole LB. Substrate specificity and redox potential of AhpC, a bacterial peroxiredoxin. Proceedings of the National Academy of Sciences of the United States of America. 105: 8209-14. PMID 18165315 DOI: 10.1073/Pnas.0708308105 |
0.415 |
|
| 2008 |
Nelson KJ, Day AE, Zeng BB, King SB, Poole LB. Isotope-coded, iodoacetamide-based reagent to determine individual cysteine pK(a) values by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Analytical Biochemistry. 375: 187-95. PMID 18162165 DOI: 10.1016/J.Ab.2007.12.004 |
0.395 |
|
| 2007 |
Poole LB. The catalytic mechanism of peroxiredoxins. Sub-Cellular Biochemistry. 44: 61-81. PMID 18084890 DOI: 10.1007/978-1-4020-6051-9_4 |
0.46 |
|
| 2007 |
Poole LB, Klomsiri C, Knaggs SA, Furdui CM, Nelson KJ, Thomas MJ, Fetrow JS, Daniel LW, King SB. Fluorescent and affinity-based tools to detect cysteine sulfenic acid formation in proteins. Bioconjugate Chemistry. 18: 2004-17. PMID 18030992 DOI: 10.1021/Bc700257A |
0.448 |
|
| 2007 |
Michalek RD, Nelson KJ, Holbrook BC, Yi JS, Stridiron D, Daniel LW, Fetrow JS, King SB, Poole LB, Grayson JM. The requirement of reversible cysteine sulfenic acid formation for T cell activation and function. Journal of Immunology (Baltimore, Md. : 1950). 179: 6456-67. PMID 17982034 DOI: 10.4049/Jimmunol.179.10.6456 |
0.334 |
|
| 2007 |
Jönsson TJ, Ellis HR, Poole LB. Cysteine reactivity and thiol-disulfide interchange pathways in AhpF and AhpC of the bacterial alkyl hydroperoxide reductase system. Biochemistry. 46: 5709-21. PMID 17441733 DOI: 10.1021/Bi7001218 |
0.731 |
|
| 2007 |
Erickson E, Furdui C, Tsang A, Fetrow J, Poole L, Loeser R. 174 JNK2 SULFENIC ACID FORMATION IN THE REDOX REGULATION OF α5β1 INTEGRIN SIGNALING Osteoarthritis and Cartilage. 15: C103-C104. DOI: 10.1016/S1063-4584(07)61807-X |
0.328 |
|
| 2006 |
Phalen TJ, Weirather K, Deming PB, Anathy V, Howe AK, van der Vliet A, Jönsson TJ, Poole LB, Heintz NH. Oxidation state governs structural transitions in peroxiredoxin II that correlate with cell cycle arrest and recovery. The Journal of Cell Biology. 175: 779-89. PMID 17145963 DOI: 10.1083/Jcb.200606005 |
0.345 |
|
| 2006 |
Panmanee W, Vattanaviboon P, Poole LB, Mongkolsuk S. Novel organic hydroperoxide-sensing and responding mechanisms for OhrR, a major bacterial sensor and regulator of organic hydroperoxide stress. Journal of Bacteriology. 188: 1389-95. PMID 16452421 DOI: 10.1128/Jb.188.4.1389-1395.2006 |
0.408 |
|
| 2006 |
Loeser R, Yammani R, Erickson E, King B, Poole L. A51 CHONDROCYTEMMP-13 EXPRESSION IN RESPONSE TO ALPHA5BETA1 INTEGRIN STIMULATION REQUIRES PROTEIN SULFENIC ACIDS AS SIGNALING INTERMEDIATES Osteoarthritis and Cartilage. 14: S42. DOI: 10.1016/S1063-4584(07)60504-4 |
0.312 |
|
| 2005 |
Poole LB, Zeng BB, Knaggs SA, Yakubu M, King SB. Synthesis of chemical probes to map sulfenic acid modifications on proteins. Bioconjugate Chemistry. 16: 1624-8. PMID 16287263 DOI: 10.1021/Bc050257S |
0.409 |
|
| 2005 |
Roberts BR, Wood ZA, Jönsson TJ, Poole LB, Karplus PA. Oxidized and synchrotron cleaved structures of the disulfide redox center in the N-terminal domain of Salmonella typhimurium AhpF Protein Science. 14: 2414-2420. PMID 16131664 DOI: 10.1110/Ps.051459705 |
0.458 |
|
| 2005 |
Parsonage D, Youngblood DS, Sarma GN, Wood ZA, Karplus PA, Poole LB. Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin Biochemistry. 44: 10583-10592. PMID 16060667 DOI: 10.1021/Bi050448I |
0.427 |
|
| 2005 |
Choi MH, Sajed D, Poole L, Hirata K, Herdman S, Torian BE, Reed SL. An unusual surface peroxiredoxin protects invasive Entamoeba histolytica from oxidant attack. Molecular and Biochemical Parasitology. 143: 80-9. PMID 15996766 DOI: 10.1016/J.Molbiopara.2005.04.014 |
0.375 |
|
| 2005 |
Poole LB. Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases. Archives of Biochemistry and Biophysics. 433: 240-54. PMID 15581580 DOI: 10.1016/J.Abb.2004.09.006 |
0.514 |
|
| 2004 |
Poole LB. Formation and functions of protein sulfenic acids. Current Protocols in Toxicology / Editorial Board, Mahin D. Maines (Editor-in-Chief) ... [Et Al.]. Unit17.1. PMID 20963761 DOI: 10.1002/0471140856.Tx1701S18 |
0.486 |
|
| 2004 |
Conway ME, Poole LB, Hutson SM. Roles for cysteine residues in the regulatory CXXC motif of human mitochondrial branched chain aminotransferase enzyme. Biochemistry. 43: 7356-64. PMID 15182179 DOI: 10.1021/Bi0498050 |
0.415 |
|
| 2004 |
Poole LB, Karplus PA, Claiborne A. Protein sulfenic acids in redox signaling. Annual Review of Pharmacology and Toxicology. 44: 325-47. PMID 14744249 DOI: 10.1146/Annurev.Pharmtox.44.101802.121735 |
0.488 |
|
| 2004 |
Poole LB. UNIT 17.2 Measurement of Protein Sulfenic Acid Content Current Protocols in Immunology. DOI: 10.1002/0471140856.Tx1702S18 |
0.454 |
|
| 2003 |
Wood ZA, Poole LB, Karplus PA. Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling Science. 300: 650-653. PMID 12714747 DOI: 10.1126/Science.1080405 |
0.384 |
|
| 2003 |
Conway ME, Yennawar N, Wallin R, Poole LB, Hutson SM. Human mitochondrial branched chain aminotransferase: structural basis for substrate specificity and role of redox active cysteines. Biochimica Et Biophysica Acta. 1647: 61-5. PMID 12686109 DOI: 10.1016/S1570-9639(03)00051-7 |
0.422 |
|
| 2003 |
Schröder E, Jönsson T, Poole L. The role of erythrocyte peroxiredoxin in detoxifying peroxides and in stimulating potassium efflux via the Gardos channels. Blood. 101: 2897; author reply 2. PMID 12642347 DOI: 10.1182/Blood-2002-12-3682 |
0.306 |
|
| 2003 |
Schröder E, Jönsson T, Poole L. Hydroxyapatite chromatography: altering the phosphate-dependent elution profile of protein as a function of pH. Analytical Biochemistry. 313: 176-8. PMID 12576076 DOI: 10.1016/S0003-2697(02)00567-5 |
0.311 |
|
| 2003 |
Wood ZA, Schröder E, Harris JR, Poole LB. Structure, mechanism and regulation of peroxiredoxins Trends in Biochemical Sciences. 28: 32-40. PMID 12517450 DOI: 10.1016/S0968-0004(02)00003-8 |
0.449 |
|
| 2003 |
Baker LM, Poole LB. Catalytic mechanism of thiol peroxidase from Escherichia coli. Sulfenic acid formation and overoxidation of essential CYS61. The Journal of Biological Chemistry. 278: 9203-11. PMID 12514184 DOI: 10.1074/Jbc.M209888200 |
0.43 |
|
| 2002 |
Conway ME, Yennawar N, Wallin R, Poole LB, Hutson SM. Identification of a peroxide-sensitive redox switch at the CXXC motif in the human mitochondrial branched chain aminotransferase. Biochemistry. 41: 9070-8. PMID 12119021 DOI: 10.1021/Bi020200I |
0.481 |
|
| 2002 |
Yamamoto Y, Poole LB, Hantgan RR, Kamio Y. An iron-binding protein, Dpr, from Streptococcus mutans prevents iron-dependent hydroxyl radical formation in vitro. Journal of Bacteriology. 184: 2931-9. PMID 12003933 DOI: 10.1128/Jb.184.11.2931-2939.2002 |
0.315 |
|
| 2002 |
Wood ZA, Poole LB, Hantgan RR, Karplus PA. Dimers to doughnuts: Redox-sensitive oligomerization of 2-cysteine peroxiredoxins Biochemistry. 41: 5493-5504. PMID 11969410 DOI: 10.1021/Bi012173M |
0.418 |
|
| 2002 |
Poole LB, Ellis HR. Identification of cysteine sulfenic acid in AhpC of alkyl hydroperoxide reductase. Methods in Enzymology. 348: 122-36. PMID 11885266 DOI: 10.1016/S0076-6879(02)48632-6 |
0.708 |
|
| 2002 |
Reynolds CM, Meyer J, Poole LB. An NADH-dependent bacterial thioredoxin reductase-like protein in conjunction with a glutaredoxin homologue form a unique peroxiredoxin (AhpC) reducing system in Clostridium pasteurianum. Biochemistry. 41: 1990-2001. PMID 11827546 DOI: 10.1021/Bi011802P |
0.672 |
|
| 2001 |
Ritz D, Lim J, Reynolds CM, Poole LB, Beckwith J. Conversion of a peroxiredoxin into a disulfide reductase by a triplet repeat expansion. Science (New York, N.Y.). 294: 158-60. PMID 11588261 DOI: 10.1126/Science.1063143 |
0.643 |
|
| 2001 |
Reynolds CM, Poole LB. Activity of one of two engineered heterodimers of AhpF, the NADH:peroxiredoxin oxidoreductase from Salmonella typhimurium, reveals intrasubunit electron transfer between domains. Biochemistry. 40: 3912-9. PMID 11300770 DOI: 10.1021/bi002766h |
0.613 |
|
| 2001 |
Wood ZA, Poole LB, Karplus PA. Structure of intact AhpF reveals a mirrored thioredoxin-like active site and implies large domain rotations during catalysis Biochemistry. 40: 3900-3911. PMID 11300769 DOI: 10.1021/Bi002765P |
0.463 |
|
| 2001 |
Baker LM, Raudonikiene A, Hoffman PS, Poole LB. Essential thioredoxin-dependent peroxiredoxin system from Helicobacter pylori: genetic and kinetic characterization. Journal of Bacteriology. 183: 1961-73. PMID 11222594 DOI: 10.1128/Jb.183.6.1961-1973.2001 |
0.378 |
|
| 2000 |
Poole LB, Michael Reynolds C, Wood ZA, Andrew Karplus P, Ellis HR, Li Calzi M. AhpF and other NADH:peroxiredoxin oxidoreductases, homologues of low M(r) thioredoxin reductase European Journal of Biochemistry. 267: 6126-6133. PMID 11012664 DOI: 10.1046/J.1432-1327.2000.01704.X |
0.738 |
|
| 2000 |
Reynolds CM, Poole LB. Attachment of the N-terminal domain of Salmonella typhimurium AhpF to Escherichia coli thioredoxin reductase confers AhpC reductase activity but does not affect thioredoxin reductase activity. Biochemistry. 39: 8859-69. PMID 10913298 DOI: 10.1021/bi000826d |
0.653 |
|
| 2000 |
Yamamoto Y, Higuchi M, Poole LB, Kamio Y. Identification of a new gene responsible for the oxygen tolerance in aerobic life of Streptococcus mutans Bioscience, Biotechnology and Biochemistry. 64: 1106-1109. PMID 10879495 DOI: 10.1271/Bbb.64.1106 |
0.34 |
|
| 2000 |
Yamamoto Y, Higuchi M, Poole LB, Kamio Y. Role of the dpr product in oxygen tolerance in Streptococcus mutans Journal of Bacteriology. 182: 3740-3747. PMID 10850989 DOI: 10.1128/Jb.182.13.3740-3747.2000 |
0.327 |
|
| 2000 |
Poole LB, Godzik A, Nayeem A, Schmitt JD. AhpF can be dissected into two functional units: tandem repeats of two thioredoxin-like folds in the N-terminus mediate electron transfer from the thioredoxin reductase-like C-terminus to AhpC. Biochemistry. 39: 6602-15. PMID 10828978 DOI: 10.1021/Bi000405W |
0.372 |
|
| 2000 |
Poole LB, Higuchi M, Shimada M, Li Calzi M, Kamio Y. Streptococcus mutans H2O2-forming NADH oxidase is an alkyl hydroperoxide reductase protein Free Radical Biology and Medicine. 28: 108-120. PMID 10656297 DOI: 10.1016/S0891-5849(99)00218-X |
0.476 |
|
| 1999 |
Higuchi M, Yamamoto Y, Poole LB, Shimada M, Sato Y, Takahashi N, Kamio Y. Functions of two types of NADH oxidases in energy metabolism and oxidative stress of Streptococcus mutans Journal of Bacteriology. 181: 5940-5947. PMID 10498705 DOI: 10.1128/Jb.181.19.5940-5947.1999 |
0.384 |
|
| 1998 |
Reynolds CM, Poole LB. Studies of an ahpf-thioredoxin reductase chimeric protein Faseb Journal. 12. |
0.646 |
|
| 1997 |
Ellis HR, Poole LB. Novel application of 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole to identify cysteine sulfenic acid in the AhpC component of alkyl hydroperoxide reductase Biochemistry. 36: 15013-15018. PMID 9398227 DOI: 10.1021/Bi972191X |
0.74 |
|
| 1997 |
Poole LB, Chae HZ, Flores BM, Reed SL, Rhee SG, Torian BE. Peroxidase activity of a TSA-like antioxidant protein from a pathogenic amoeba. Free Radical Biology & Medicine. 23: 955-9. PMID 9378375 DOI: 10.1016/S0891-5849(97)00066-X |
0.447 |
|
| 1997 |
Li Calzi M, Poole LB. Requirement for the two AhpF cystine disulfide centers in catalysis of peroxide reduction by alkyl hydroperoxide reductase Biochemistry. 36: 13357-13364. PMID 9341228 DOI: 10.1021/Bi9713660 |
0.451 |
|
| 1997 |
Ellis HR, Poole LB. Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium Biochemistry. 36: 13349-13356. PMID 9341227 DOI: 10.1021/Bi9713658 |
0.743 |
|
| 1997 |
Li Calzi M, Poole LB. Rapid reaction kinetic studies of ahpf and ahpc proteins of the alkyl hydroperoxide reductase ( AHPR) enzymatic system Faseb Journal. 11. |
0.389 |
|
| 1996 |
Poole LB. Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cystine disulfides involved in catalysis of peroxide reduction Biochemistry. 35: 65-75. PMID 8555199 DOI: 10.1021/Bi951888K |
0.505 |
|
| 1996 |
Poole LB, Ellis HR. Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 1. Purification and enzymatic activities of overexpressed AhpF and AhpC proteins Biochemistry. 35: 56-64. PMID 8555198 DOI: 10.1021/Bi951887S |
0.737 |
|
| 1995 |
Niimura Y, Poole LB, Massey V. Amphibacillus xylanus NADH oxidase and Salmonella typhimurium alkyl-hydroperoxide reductase flavoprotein components show extremely high scavenging activity for both alkyl hydroperoxide and hydrogen peroxide in the presence of S. typhimurium alkyl-hydroperoxide reductase 22-kDa protein component. The Journal of Biological Chemistry. 270: 25645-50. PMID 7592740 DOI: 10.1074/Jbc.270.43.25645 |
0.468 |
|
| 1995 |
Crane EJ, Parsonage D, Poole LB, Claiborne A. Analysis of the kinetic mechanism of enterococcal NADH peroxidase reveals catalytic roles for NADH complexes with both oxidized and two-electron- reduced enzyme forms Biochemistry. 34: 14114-14124. PMID 7578008 DOI: 10.1021/Bi00043A016 |
0.393 |
|
| 1994 |
Chae HZ, Robison K, Poole LB, Church G, Storz G, Rhee SG. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes Proceedings of the National Academy of Sciences of the United States of America. 91: 7017-7021. PMID 8041738 DOI: 10.1073/Pnas.91.15.7017 |
0.377 |
|
| 1993 |
Ashwell CM, Poole LB. Characterization of the N-terminal region within the alkyl hydroperoxide reductase AhpF protein Free Radical Biology and Medicine. 15: 506. DOI: 10.1016/0891-5849(93)90319-P |
0.361 |
|
| 1989 |
Poole LB, Claiborne A. The non-flavin redox center of the streptococcal NADH peroxidase. II. Evidence for a stabilized cysteine-sulfenic acid Journal of Biological Chemistry. 264: 12330-12338. PMID 2501303 |
0.334 |
|
| 1986 |
Poole LB, Claiborne A. Interactions of pyridine nucleotides with redox forms of the flavin-containing NADH peroxidase from Streptococcus faecalis Journal of Biological Chemistry. 261: 14525-14533. PMID 3095321 |
0.309 |
|
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