| Year |
Citation |
Score |
| 2020 |
Tower J, Pomatto LCD, Davies KJA. Sex differences in the response to oxidative and proteolytic stress. Redox Biology. 101488. PMID 32201219 DOI: 10.1016/J.Redox.2020.101488 |
0.366 |
|
| 2019 |
Pomatto LCD, Sun PY, Yu K, Gullapalli S, Bwiza CP, Sisliyan C, Wong S, Zhang H, Forman HJ, Oliver PL, Davies KE, Davies KJA. Limitations to adaptive homeostasis in an hyperoxia-induced model of accelerated ageing. Redox Biology. 24: 101194. PMID 31022673 DOI: 10.1016/J.Redox.2019.101194 |
0.321 |
|
| 2018 |
das Graças Fedoce A, Ferreira F, Bota RG, Bonet-Costa V, Sun PY, Davies KJA. The role of oxidative stress in anxiety disorder: cause or consequence? Free Radical Research. 1-11. PMID 29742940 DOI: 10.1080/10715762.2018.1475733 |
0.322 |
|
| 2018 |
Pomatto LCD, Wong S, Tower J, Davies KJA. Sex-specific adaptive homeostasis independs on increased proteolysis by the 20S Proteasome: Data-in-Brief. Data in Brief. 17: 653-661. PMID 29552615 DOI: 10.1016/J.Dib.2018.01.044 |
0.376 |
|
| 2018 |
Walker CL, Pomatto LCD, Tripathi DN, Davies KJA. Redox Regulation of Homeostasis and Proteostasis in Peroxisomes. Physiological Reviews. 98: 89-115. PMID 29167332 DOI: 10.1152/physrev.00033.2016 |
0.328 |
|
| 2018 |
Sisliyan C, Pomatto LC, Sun P, Zhang H, Hayek J, Forman H, Valacchi G, Davies K. Recruitment of Nrf2-dependent adaptive homeostatic redox responses in Rett syndrome Free Radical Biology and Medicine. 128: S134. DOI: 10.1016/J.Freeradbiomed.2018.10.355 |
0.455 |
|
| 2018 |
Yu K, Sun P, Davies K, Zhang H, Forman H. Oxygen concentration dependency of adaptive homeostatic responses Free Radical Biology and Medicine. 128: S129. DOI: 10.1016/J.Freeradbiomed.2018.10.320 |
0.424 |
|
| 2017 |
Lomeli N, Bota DA, Davies KJA. Diminished stress resistance and defective adaptive homeostasis in age-related diseases. Clinical Science (London, England : 1979). 131: 2573-2599. PMID 29070521 DOI: 10.1042/Cs20160982 |
0.362 |
|
| 2017 |
Pomatto LC, Wong S, Carney C, Shen B, Tower J, Davies KJ. The age- and sex-specific decline of the 20s proteasome and the Nrf2/CncC signal transduction pathway in adaption and resistance to oxidative stress in Drosophila melanogaster. Aging. PMID 28373600 DOI: 10.18632/aging.101218 |
0.385 |
|
| 2017 |
Sun PY, Yu K, Davies KJ. Age-dependent Decline in Adaptive Homeostasis and Nrf2 Mediated Proteasome Induction in Human Bronchial Epithelial Cells Exposed to Oxidative Stress Free Radical Biology and Medicine. 112: 57. DOI: 10.1016/j.freeradbiomed.2017.10.078 |
0.415 |
|
| 2017 |
Pomatto LC, Cline M, Woodward N, Morgan TE, Finch C, Forman HJ, Davies KJ. Oxidizing Nano Particles (Smog) Induce Protective Levels of Proteasome via the Nrf2 Signal Transduction Pathway in Young but Not Old Female Mice Free Radical Biology and Medicine. 112: 50. DOI: 10.1016/J.Freeradbiomed.2017.10.065 |
0.339 |
|
| 2017 |
Davies KJ. Importance of The Mitochondrial Lon Protease in Age- and Sex-Specific Adaptation to Oxidative Stress Free Radical Biology and Medicine. 108: S6. DOI: 10.1016/j.freeradbiomed.2017.04.049 |
0.493 |
|
| 2016 |
Pomatto LC, Carney C, Shen B, Wong S, Halaszynski K, Salomon MP, Davies KJ, Tower J. The Mitochondrial Lon Protease Is Required for Age-Specific and Sex-Specific Adaptation to Oxidative Stress. Current Biology : Cb. PMID 27916526 DOI: 10.1016/J.Cub.2016.10.044 |
0.35 |
|
| 2016 |
Reeg S, Jung T, Castro JP, Davies KJ, Henze A, Grune T. The Molecular Chaperone Hsp70 Promotes the Proteolytic Removal of Oxidatively Damaged Proteins by the Proteasome. Free Radical Biology & Medicine. PMID 27498116 DOI: 10.1016/j.freeradbiomed.2016.08.002 |
0.399 |
|
| 2016 |
Bota DA, Davies KJ. Mitochondrial Lon Protease in Human Disease and Aging: Including an etiologic classification of Lon-related diseases and disorders. Free Radical Biology & Medicine. PMID 27387767 DOI: 10.1016/J.Freeradbiomed.2016.06.031 |
0.429 |
|
| 2016 |
Raynes R, Juarez C, Pomatto LC, Sieburth D, Davies KJ. Aging and SKN-1-dependent Loss of 20S Proteasome Adaptation to Oxidative Stress in C. elegans. The Journals of Gerontology. Series a, Biological Sciences and Medical Sciences. PMID 27341854 DOI: 10.1093/Gerona/Glw093 |
0.392 |
|
| 2016 |
Raynes R, Pomatto LC, Davies KJ. Degradation of oxidized proteins by the proteasome: Distinguishing between the 20S, 26S, and immunoproteasome proteolytic pathways. Molecular Aspects of Medicine. PMID 27155164 DOI: 10.1016/J.Mam.2016.05.001 |
0.393 |
|
| 2016 |
Johnston-Carey HK, Pomatto LC, Davies KJ. The Immunoproteasome in oxidative stress, aging, and disease. Critical Reviews in Biochemistry and Molecular Biology. 1-14. PMID 27098648 DOI: 10.3109/10409238.2016.1172554 |
0.34 |
|
| 2016 |
Davies KJ. The Oxygen Paradox, oxidative stress, and ageing. Archives of Biochemistry and Biophysics. 595: 28-32. PMID 27095211 DOI: 10.1016/j.abb.2015.11.015 |
0.31 |
|
| 2016 |
Pomatto LC, Raynes R, Davies KJ. The peroxisomal Lon protease LonP2 in aging and disease: functions and comparisons with mitochondrial Lon protease LonP1. Biological Reviews of the Cambridge Philosophical Society. PMID 26852705 DOI: 10.1111/Brv.12253 |
0.499 |
|
| 2016 |
Bonet-Costa V, Davies KJ. Measuring 20S Proteasome and Immunoproteasome Activities in Oxidative Stress Free Radical Biology and Medicine. 100: S94. DOI: 10.1016/j.freeradbiomed.2016.10.235 |
0.34 |
|
| 2016 |
Pomatto LC, Carney C, Shen B, Tower J, Davies KJ. To Adapt or Not to Adapt: Sex-Specific and Age-Dependent Adaptation of the Mitochondrial Lon Protease in D. Melanogaster Free Radical Biology and Medicine. 100: S82-S83. DOI: 10.1016/J.Freeradbiomed.2016.10.205 |
0.422 |
|
| 2015 |
Emrani R, Rébillard A, Lefeuvre L, Gratas-Delamarche A, Davies KJ, Cillard J. The calcineurin antagonist RCAN1-4 is induced by exhaustive exercise in rat skeletal muscle. Free Radical Biology & Medicine. 87: 290-9. PMID 26122706 DOI: 10.1016/j.freeradbiomed.2015.06.023 |
0.307 |
|
| 2015 |
Zhang H, Davies KJ, Forman HJ. Oxidative stress response and Nrf2 signaling in aging. Free Radical Biology & Medicine. PMID 26066302 DOI: 10.1016/J.Freeradbiomed.2015.05.036 |
0.409 |
|
| 2015 |
Marton O, Koltai E, Takeda M, Koch LG, Britton SL, Davies KJ, Boldogh I, Radak Z. Mitochondrial biogenesis-associated factors underlie the magnitude of response to aerobic endurance training in rats. PflüGers Archiv : European Journal of Physiology. 467: 779-88. PMID 24943897 DOI: 10.1007/S00424-014-1554-7 |
0.353 |
|
| 2015 |
Davies KJ. Oxidative Stress and the Decline of Adaptive Homeostasis in Aging Free Radical Biology and Medicine. 86: S12. DOI: 10.1016/j.freeradbiomed.2015.07.053 |
0.394 |
|
| 2014 |
Raynes R, Juarez C, Pomatto LC, Sieburth D, Davies KJ. The Age-Related Decline of 20S Proteasome Adaptation to Oxidative Stress Is Dependent on SKN- 1 Signaling Free Radical Biology and Medicine. 76: S36. DOI: 10.1016/J.Freeradbiomed.2014.10.457 |
0.366 |
|
| 2013 |
Ngo JK, Pomatto LC, Davies KJ. Upregulation of the mitochondrial Lon Protease allows adaptation to acute oxidative stress but dysregulation is associated with chronic stress, disease, and aging. Redox Biology. 1: 258-64. PMID 24024159 DOI: 10.1016/J.Redox.2013.01.015 |
0.777 |
|
| 2013 |
Ermak G, Davies KJ. Chronic high levels of the RCAN1-1 protein may promote neurodegeneration and Alzheimer disease. Free Radical Biology & Medicine. 62: 47-51. PMID 23369757 DOI: 10.1016/j.freeradbiomed.2013.01.016 |
0.348 |
|
| 2013 |
Pickering AM, Staab TA, Tower J, Sieburth D, Davies KJ. A conserved role for the 20S proteasome and Nrf2 transcription factor in oxidative stress adaptation in mammals, Caenorhabditis elegans and Drosophila melanogaster. The Journal of Experimental Biology. 216: 543-53. PMID 23038734 DOI: 10.1242/Jeb.074757 |
0.374 |
|
| 2013 |
Davies KJ. Regulatory Mechanisms for Proteolytic Systems in Oxidative Stress Free Radical Biology and Medicine. 65: S5. DOI: 10.1016/j.freeradbiomed.2013.08.113 |
0.314 |
|
| 2012 |
Pickering AM, Davies KJ. Degradation of damaged proteins: the main function of the 20S proteasome. Progress in Molecular Biology and Translational Science. 109: 227-48. PMID 22727423 DOI: 10.1016/B978-0-12-397863-9.00006-7 |
0.413 |
|
| 2012 |
Koltai E, Hart N, Taylor AW, Goto S, Ngo JK, Davies KJ, Radak Z. Age-associated declines in mitochondrial biogenesis and protein quality control factors are minimized by exercise training. American Journal of Physiology. Regulatory, Integrative and Comparative Physiology. 303: R127-34. PMID 22573103 DOI: 10.1152/Ajpregu.00337.2011 |
0.725 |
|
| 2012 |
Pickering AM, Davies KJ. Differential roles of proteasome and immunoproteasome regulators Pa28αβ, Pa28γ and Pa200 in the degradation of oxidized proteins. Archives of Biochemistry and Biophysics. 523: 181-90. PMID 22564544 DOI: 10.1016/j.abb.2012.04.018 |
0.406 |
|
| 2012 |
Ermak G, Sojitra S, Yin F, Cadenas E, Cuervo AM, Davies KJ. Chronic expression of RCAN1-1L protein induces mitochondrial autophagy and metabolic shift from oxidative phosphorylation to glycolysis in neuronal cells. The Journal of Biological Chemistry. 287: 14088-98. PMID 22389495 DOI: 10.1074/Jbc.M111.305342 |
0.416 |
|
| 2012 |
Pickering AM, Linder RA, Zhang H, Forman HJ, Davies KJ. Nrf2-dependent induction of proteasome and Pa28αβ regulator are required for adaptation to oxidative stress. The Journal of Biological Chemistry. 287: 10021-31. PMID 22308036 DOI: 10.1074/Jbc.M111.277145 |
0.421 |
|
| 2011 |
Ngo JK, Pomatto LC, Bota DA, Koop AL, Davies KJ. Impairment of lon-induced protection against the accumulation of oxidized proteins in senescent wi-38 fibroblasts. The Journals of Gerontology. Series a, Biological Sciences and Medical Sciences. 66: 1178-85. PMID 21868393 DOI: 10.1093/Gerona/Glr145 |
0.774 |
|
| 2011 |
Grune T, Catalgol B, Licht A, Ermak G, Pickering AM, Ngo JK, Davies KJ. HSP70 mediates dissociation and reassociation of the 26S proteasome during adaptation to oxidative stress. Free Radical Biology & Medicine. 51: 1355-64. PMID 21767633 DOI: 10.1016/J.Freeradbiomed.2011.06.015 |
0.749 |
|
| 2011 |
Ermak G, Pritchard MA, Dronjak S, Niu B, Davies KJ. Do RCAN1 proteins link chronic stress with neurodegeneration? Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 25: 3306-11. PMID 21680892 DOI: 10.1096/fj.11-185728 |
0.315 |
|
| 2011 |
Kanika ND, Chang J, Tong Y, Tiplitsky S, Lin J, Yohannes E, Tar M, Chance M, Christ GJ, Melman A, Davies KD. Oxidative stress status accompanying diabetic bladder cystopathy results in the activation of protein degradation pathways. Bju International. 107: 1676-84. PMID 21518418 DOI: 10.1111/J.1464-410X.2010.09655.X |
0.326 |
|
| 2011 |
Grimm S, Hoehn A, Davies KJ, Grune T. Protein oxidative modifications in the ageing brain: Consequence for the onset of neurodegenerative disease Free Radical Research. 45: 73-88. PMID 20815785 DOI: 10.3109/10715762.2010.512040 |
0.412 |
|
| 2011 |
Lloret A, Badia MC, Giraldo E, Alonso D, Davies K, Viña J. Role of RCAN1, a gene involved in the adaptation to oxidative stress, in Alzheimer's pathology Alzheimers & Dementia. 7. DOI: 10.1016/J.Jalz.2011.05.1624 |
0.426 |
|
| 2010 |
Costa V, Giacomello M, Hudec R, Lopreiato R, Ermak G, Lim D, Malorni W, Davies KJ, Carafoli E, Scorrano L. Mitochondrial fission and cristae disruption increase the response of cell models of Huntington's disease to apoptotic stimuli. Embo Molecular Medicine. 2: 490-503. PMID 21069748 DOI: 10.1002/emmm.201000102 |
0.368 |
|
| 2010 |
Pickering AM, Koop AL, Teoh CY, Ermak G, Grune T, Davies KJ. The immunoproteasome, the 20S proteasome and the PA28αβ proteasome regulator are oxidative-stress-adaptive proteolytic complexes. The Biochemical Journal. 432: 585-94. PMID 20919990 DOI: 10.1042/BJ20100878 |
0.427 |
|
| 2010 |
Davies K, Kanika N, Tar M, Melman A. 885 EXPERIMENTAL PRIAPISM IS ASSOCIATED WITH INCREASED OXIDATIVE STRESS AND ACTIVATION OF PROTEIN DEGRADATION PATHWAYS IN CORPORAL TISSUE Journal of Urology. 183. DOI: 10.1016/J.JURO.2010.02.1641 |
0.363 |
|
| 2009 |
Ngo JK, Davies KJ. Mitochondrial Lon protease is a human stress protein. Free Radical Biology & Medicine. 46: 1042-8. PMID 19439239 DOI: 10.1016/J.Freeradbiomed.2008.12.024 |
0.78 |
|
| 2009 |
Radak Z, Atalay M, Jakus J, Boldogh I, Davies K, Goto S. Exercise improves import of 8-oxoguanine DNA glycosylase into the mitochondrial matrix of skeletal muscle and enhances the relative activity. Free Radical Biology & Medicine. 46: 238-43. PMID 18992806 DOI: 10.1016/J.Freeradbiomed.2008.10.022 |
0.43 |
|
| 2007 |
Ngo JK, Davies KJ. Importance of the lon protease in mitochondrial maintenance and the significance of declining lon in aging. Annals of the New York Academy of Sciences. 1119: 78-87. PMID 18056957 DOI: 10.1196/Annals.1404.015 |
0.77 |
|
| 2006 |
Davies KJ, Shringarpure R. Preferential degradation of oxidized proteins by the 20S proteasome may be inhibited in aging and in inflammatory neuromuscular diseases. Neurology. 66: S93-6. PMID 16432154 DOI: 10.1212/01.Wnl.0000192308.43151.63 |
0.389 |
|
| 2005 |
Grune T, Merker K, Jung T, Sitte N, Davies KJ. Protein oxidation and degradation during postmitotic senescence. Free Radical Biology & Medicine. 39: 1208-15. PMID 16214036 DOI: 10.1016/j.freeradbiomed.2005.06.009 |
0.381 |
|
| 2005 |
Bota DA, Ngo JK, Davies KJ. Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death. Free Radical Biology & Medicine. 38: 665-77. PMID 15683722 DOI: 10.1016/J.Freeradbiomed.2004.11.017 |
0.744 |
|
| 2004 |
Azzi A, Davies KJ, Kelly F. Free radical biology - terminology and critical thinking. Febs Letters. 558: 3-6. PMID 14982062 |
0.326 |
|
| 2004 |
Ermak G, Cheadle C, Becker KG, Harris CD, Davies KJA. DSCR1(Adapt78) modulates expression of SOD1 Faseb Journal. 18: 62-69. PMID 14718387 DOI: 10.1096/Fj.03-0451Com |
0.316 |
|
| 2003 |
Giulivi C, Traaseth NJ, Davies KJ. Tyrosine oxidation products: analysis and biological relevance. Amino Acids. 25: 227-32. PMID 14661086 DOI: 10.1007/S00726-003-0013-0 |
0.317 |
|
| 2003 |
Grune T, Davies KJ. The proteasomal system and HNE-modified proteins. Molecular Aspects of Medicine. 24: 195-204. PMID 12892997 DOI: 10.1016/S0098-2997(03)00014-1 |
0.329 |
|
| 2003 |
Wang Y, Davies KJ, Melendez JA, Crawford DR. Characterization of adapt33, a stress-inducible riboregulator. Gene Expression. 11: 85-94. PMID 12837039 |
0.312 |
|
| 2003 |
Grune T, Merker K, Sandig G, Davies KJ. Selective degradation of oxidatively modified protein substrates by the proteasome. Biochemical and Biophysical Research Communications. 305: 709-18. PMID 12763051 DOI: 10.1016/S0006-291X(03)00809-X |
0.374 |
|
| 2003 |
Demasi M, Davies KJ. Proteasome inhibitors induce intracellular protein aggregation and cell death by an oxygen-dependent mechanism. Febs Letters. 542: 89-94. PMID 12729904 DOI: 10.1016/S0014-5793(03)00353-3 |
0.301 |
|
| 2003 |
Shringarpure R, Grune T, Mehlhase J, Davies KJ. Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome. The Journal of Biological Chemistry. 278: 311-8. PMID 12401807 DOI: 10.1074/Jbc.M206279200 |
0.384 |
|
| 2002 |
Bota DA, Van Remmen H, Davies KJ. Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress. Febs Letters. 532: 103-6. PMID 12459471 DOI: 10.1016/S0014-5793(02)03638-4 |
0.463 |
|
| 2002 |
Grune T, Reinheckel T, North JA, Li R, Bescos PB, Shringarpure R, Davies KJ. Ezrin turnover and cell shape changes catalyzed by proteasome in oxidatively stressed cells. Faseb Journal : Official Publication of the Federation of American Societies For Experimental Biology. 16: 1602-10. PMID 12374783 DOI: 10.1096/Fj.02-0015Com |
0.41 |
|
| 2002 |
Bota DA, Davies KJ. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nature Cell Biology. 4: 674-80. PMID 12198491 DOI: 10.1038/Ncb836 |
0.486 |
|
| 2002 |
Crawford DR, Suzuki T, Sesay J, Davies KJ. Analysis of gene expression following oxidative stress. Methods in Molecular Biology (Clifton, N.J.). 196: 155-62. PMID 12152194 DOI: 10.1385/1-59259-274-0:155 |
0.312 |
|
| 2002 |
Ermak G, Harris CD, Davies KJA. The DSCR1 (Adapt78) isoform 1 protein calcipressin 1 inhibits calcineurin and protects against acute calcium-mediated stress damage, including transient oxidative stress Faseb Journal. 16: 814-824. PMID 12039863 DOI: 10.1096/Fj.01-0846Com |
0.367 |
|
| 2002 |
Shringarpure R, Davies KJ. Protein turnover by the proteasome in aging and disease. Free Radical Biology & Medicine. 32: 1084-9. PMID 12031893 DOI: 10.1016/S0891-5849(02)00824-9 |
0.394 |
|
| 2002 |
Ermak G, Davies KJ. Calcium and oxidative stress: from cell signaling to cell death. Molecular Immunology. 38: 713-21. PMID 11841831 DOI: 10.1016/S0161-5890(01)00108-0 |
0.301 |
|
| 2002 |
Grune T, Reinheckel T, Li R, North JA, Davies KJ. Proteasome-dependent turnover of protein disulfide isomerase in oxidatively stressed cells. Archives of Biochemistry and Biophysics. 397: 407-13. PMID 11795901 DOI: 10.1006/abbi.2001.2719 |
0.363 |
|
| 2001 |
Davies KJA, Harris CD, Ermak G. The essential role of calcium in induction of the DSCR1 (ADAPT78) gene Biofactors. 15: 91-93. PMID 12016333 DOI: 10.1002/Biof.5520150208 |
0.357 |
|
| 2001 |
Grune T, Shringarpure R, Sitte N, Davies K. Age-related changes in protein oxidation and proteolysis in mammalian cells. Journals of Gerontology Series a-Biological Sciences and Medical Sciences. 56. PMID 11682566 DOI: 10.1093/Gerona/56.11.B459 |
0.53 |
|
| 2001 |
Davies KJ. Oxidative stress, antioxidant defenses, and damage removal, repair, and replacement systems. Iubmb Life. 50: 279-89. PMID 11327322 DOI: 10.1080/713803728 |
0.354 |
|
| 2001 |
Davies KJ. An overview of oxidative stress. Iubmb Life. 50: 241-4. PMID 11327316 DOI: 10.1080/713803723 |
0.355 |
|
| 2001 |
Davies KJ. Degradation of oxidized proteins by the 20S proteasome. Biochimie. 83: 301-10. PMID 11295490 DOI: 10.1016/S0300-9084(01)01250-0 |
0.444 |
|
| 2001 |
Abramova NE, Davies KJ, Crawford DR. Polynucleotide degradation during early stage response to oxidative stress is specific to mitochondria. Free Radical Biology & Medicine. 28: 281-8. PMID 11281296 DOI: 10.1016/S0891-5849(99)00239-7 |
0.415 |
|
| 2000 |
Cadenas E, Davies KJ. Mitochondrial free radical generation, oxidative stress, and aging. Free Radical Biology & Medicine. 29: 222-30. PMID 11035250 DOI: 10.1016/S0891-5849(00)00317-8 |
0.451 |
|
| 2000 |
Reinheckel T, Grune T, Davies KJ. The measurement of protein degradation in response to oxidative stress. Methods in Molecular Biology (Clifton, N.J.). 99: 49-60. PMID 10909076 DOI: 10.1385/1-59259-054-3:49 |
0.373 |
|
| 2000 |
Davies KJ. The broad spectrum of responses to oxidants in proliferating cells: a new paradigm for oxidative stress. Iubmb Life. 48: 41-7. PMID 10791914 DOI: 10.1080/713803463 |
0.427 |
|
| 1999 |
Ullrich O, Reinheckel T, Sitte N, Hass R, Grune T, Davies KJ. Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones. Proceedings of the National Academy of Sciences of the United States of America. 96: 6223-8. PMID 10339569 DOI: 10.1073/PNAS.96.11.6223 |
0.359 |
|
| 1999 |
Crawford DR, Abramova NE, Davies KJ. Oxidative stress causes a general, calcium-dependent degradation of mitochondrial polynucleotides. Free Radical Biology & Medicine. 25: 1106-11. PMID 9870565 DOI: 10.1016/S0891-5849(98)00143-9 |
0.431 |
|
| 1998 |
Reinheckel T, Sitte N, Ullrich O, Kuckelkorn U, Davies KJ, Grune T. Comparative resistance of the 20S and 26S proteasome to oxidative stress. The Biochemical Journal. 637-42. PMID 9794805 DOI: 10.1042/BJ3350637 |
0.374 |
|
| 1998 |
Grune T, Blasig IE, Sitte N, Roloff B, Haseloff R, Davies KJ. Peroxynitrite increases the degradation of aconitase and other cellular proteins by proteasome. The Journal of Biological Chemistry. 273: 10857-62. PMID 9556559 DOI: 10.1074/JBC.273.18.10857 |
0.367 |
|
| 1997 |
Grune T, Davies KJ. Breakdown of oxidized proteins as a part of secondary antioxidant defenses in mammalian cells. Biofactors (Oxford, England). 6: 165-72. PMID 9259998 DOI: 10.1002/biof.5520060210 |
0.361 |
|
| 1997 |
Crawford DR, Wang Y, Schools GP, Kochheiser J, Davies KJ. Down-regulation of mammalian mitochondrial RNAs during oxidative stress. Free Radical Biology & Medicine. 22: 551-9. PMID 8981048 DOI: 10.1016/S0891-5849(96)00380-2 |
0.342 |
|
| 1997 |
Grune T, Reinheckel T, Davies KJA. Degradation of oxidized proteins in mammalian cells The Faseb Journal. 11: 526-534. DOI: 10.1096/fasebj.11.7.9212076 |
0.334 |
|
| 1996 |
Crawford DR, Leahy KP, Wang Y, Schools GP, Kochheiser JC, Davies KJ. Oxidative stress induces the levels of a MafG homolog in hamster HA-1 cells. Free Radical Biology & Medicine. 21: 521-5. PMID 8886803 DOI: 10.1016/0891-5849(96)00160-8 |
0.335 |
|
| 1996 |
Grune T, Reinheckel T, Davies KJ. Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome. The Journal of Biological Chemistry. 271: 15504-9. PMID 8663134 DOI: 10.1074/jbc.271.26.15504 |
0.329 |
|
| 1996 |
Davies KJ. Oxidative stress: the paradox of aerobic life. Biochemical Society Symposium. 61: 1-31. PMID 8660387 DOI: 10.1042/bss0610001 |
0.318 |
|
| 1996 |
Grune T, Reinheckel T, Davies K. PROTEOLYSIS MEDIATED BY OXIDATIVE STRESS IN MAMMALIAN CELLS Biochemical Society Transactions. 24: 630S-630S. DOI: 10.1042/bst024630sc |
0.379 |
|
| 1995 |
Grune T, Reinheckel T, Joshi M, Davies KJ. Proteolysis in cultured liver epithelial cells during oxidative stress. Role of the multicatalytic proteinase complex, proteasome. The Journal of Biological Chemistry. 270: 2344-51. PMID 7836468 DOI: 10.1074/jbc.270.5.2344 |
0.425 |
|
| 1995 |
Crawford DR, Davies KJ. Adaptive response and oxidative stress. Environmental Health Perspectives. 25-8. PMID 7705299 DOI: 10.1289/ehp.94102s1025 |
0.398 |
|
| 1991 |
Pacifici RE, Davies KJ. Protein, lipid and DNA repair systems in oxidative stress: the free-radical theory of aging revisited. Gerontology. 37: 166-80. PMID 2055497 DOI: 10.1159/000213257 |
0.379 |
|
| 1991 |
Salo DC, Donovan CM, Davies KJA. HSP70 and other possible heat shock or oxidative stress proteins are induced in skeletal muscle, heart, and liver during exercise Free Radical Biology and Medicine. 11: 239-246. PMID 1937141 DOI: 10.1016/0891-5849(91)90119-N |
0.352 |
|
| 1990 |
Davies KJ. Protein oxidation and proteolytic degradation. General aspects and relationship to cataract formation. Advances in Experimental Medicine and Biology. 264: 503-11. PMID 2244532 DOI: 10.1007/978-1-4684-5730-8_77 |
0.374 |
|
| 1990 |
Pacifici RE, Davies KJ. Protein degradation as an index of oxidative stress. Methods in Enzymology. 186: 485-502. PMID 2233315 DOI: 10.1016/0076-6879(90)86143-J |
0.389 |
|
| 1990 |
Salo DC, Donovan CM, Davies KJ. induction of HSP70 and other heat shock or oxidative stress proteins during exercise Free Radical Biology and Medicine. 9: 7. DOI: 10.1016/0891-5849(90)90192-L |
0.307 |
|
| 1989 |
Davies KJ, Lin SW. Oxidatively denatured proteins are degraded by an ATP-independent proteolytic pathway in Escherichia coli. Free Radical Biology & Medicine. 5: 225-36. PMID 3075950 DOI: 10.1016/0891-5849(88)90016-0 |
0.372 |
|
| 1989 |
Pacifici RE, Lin SW, Davies KJ. The measurement of protein degradation in response to oxidative stress. Basic Life Sciences. 49: 531-5. PMID 3074786 DOI: 10.1007/978-1-4684-5568-7_82 |
0.39 |
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| 1989 |
Marcillat O, Zhang Y, Davies KJ. Oxidative and non-oxidative mechanisms in the inactivation of cardiac mitochondrial electron transport chain components by doxorubicin. The Biochemical Journal. 259: 181-9. PMID 2719642 DOI: 10.1042/bj2590181 |
0.331 |
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| 1989 |
Salo DC, Lin SW, Pacifici RE, Davies KJ. Superoxide dismutase is preferentially degraded by a proteolytic system from red blood cells following oxidative modification by hydrogen peroxide. Free Radical Biology & Medicine. 5: 335-9. PMID 2476367 DOI: 10.1016/0891-5849(88)90105-0 |
0.301 |
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| 1988 |
Taylor A, Davies KJ. Protein oxidation and loss of protease activity may lead to cataract formation in the aged lens. Free Radical Biology & Medicine. 3: 371-7. PMID 3322949 DOI: 10.1016/0891-5849(87)90015-3 |
0.321 |
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| 1988 |
Marcillat O, Zhang Y, Lin SW, Davies KJ. Mitochondria contain a proteolytic system which can recognize and degrade oxidatively-denatured proteins. The Biochemical Journal. 254: 677-83. PMID 3196285 DOI: 10.1042/bj2540677 |
0.414 |
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| 1987 |
Davies KJ. Intracellular proteolytic systems may function as secondary antioxidant defenses: an hypothesis. Journal of Free Radicals in Biology & Medicine. 2: 155-73. PMID 3553299 DOI: 10.1016/S0748-5514(86)80066-6 |
0.317 |
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