메뉴 건너뛰기




Volumn 427, Issue 7, 2015, Pages 1549-1563

Protein quality control under oxidative stress conditions

Author keywords

disulfide bond formation; molecular chaperone; N chlorination; oxidative stress; protein aggregation

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ALPHA 2 MACROGLOBULIN; CHAPERONE; CYSTEINE; ESCHERICHIA COLI PROTEIN; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 33; METHIONINE; OXIDIZING AGENT; POLYPHOSPHATE; REACTIVE CHLORINE SPECIE; REACTIVE OXYGEN METABOLITE; RIDA PROTEIN; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; CHLORINE DERIVATIVE; PROTEIN; PROTEIN AGGREGATE;

EID: 84924089568     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2015.02.014     Document Type: Review
Times cited : (136)

References (154)
  • 1
    • 84863738048 scopus 로고    scopus 로고
    • Mitochondrial oxidative phosphorylation
    • S. Dröse, and U. Brandt Mitochondrial oxidative phosphorylation Adv Exp Med Biol 2012 145 169
    • (2012) Adv Exp Med Biol , pp. 145-169
    • Dröse, S.1    Brandt, U.2
  • 2
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • J.D. Lambeth NOX enzymes and the biology of reactive oxygen Nat Rev Microbiol 4 2004 181 189
    • (2004) Nat Rev Microbiol , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 3
    • 47749151450 scopus 로고    scopus 로고
    • Biological roles for the NOX family NADPH oxidases
    • W.M. Nauseef Biological roles for the NOX family NADPH oxidases J Biol Chem 283 2008 16961 16965
    • (2008) J Biol Chem , vol.283 , pp. 16961-16965
    • Nauseef, W.M.1
  • 4
    • 77349092837 scopus 로고    scopus 로고
    • Peroxisome diversity and evolution
    • T. Gabaldón Peroxisome diversity and evolution Phil Trans R Soc B 365 2010 765 773
    • (2010) Phil Trans R Soc B , vol.365 , pp. 765-773
    • Gabaldón, T.1
  • 5
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • B. D'Autréaux, and M.B. Toledano ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis Nat Rev Mol Cell Biol 8 2007 813 824
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 813-824
    • D'Autréaux, B.1    Toledano, M.B.2
  • 6
    • 84857116578 scopus 로고    scopus 로고
    • Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling
    • P.D. Ray, B.-W. Huang, and Y. Tsuji Reactive oxygen species (ROS) homeostasis and redox regulation in cellular signaling Cell Signal 24 2012 981 990
    • (2012) Cell Signal , vol.24 , pp. 981-990
    • Ray, P.D.1    Huang, B.-W.2    Tsuji, Y.3
  • 7
    • 84924119180 scopus 로고    scopus 로고
    • Are free radicals involved in thiol-based redox signaling?
    • [in press]
    • C.C. Winterbourn Are free radicals involved in thiol-based redox signaling? Free Radic Biol Med 2015 10.1016/j.freeradbiomed.2014.08.017 [in press]
    • (2015) Free Radic Biol Med
    • Winterbourn, C.C.1
  • 9
    • 84879422944 scopus 로고    scopus 로고
    • The molecular mechanisms and physiological consequences of oxidative stress: Lessons from a model bacterium
    • J.A. Imlay The molecular mechanisms and physiological consequences of oxidative stress: lessons from a model bacterium Nat Rev Microbiol 11 2013 443 454
    • (2013) Nat Rev Microbiol , vol.11 , pp. 443-454
    • Imlay, J.A.1
  • 10
    • 84880277784 scopus 로고    scopus 로고
    • The biological chemistry of hydrogen peroxide
    • C.C. Winterbourn The biological chemistry of hydrogen peroxide Methods Enzymol 528 2013 3 25
    • (2013) Methods Enzymol , vol.528 , pp. 3-25
    • Winterbourn, C.C.1
  • 13
    • 84924183088 scopus 로고    scopus 로고
    • Reactions of myeloperoxidase-derived oxidants with biological substrates: Gaining chemical insight into human inflammatory diseases
    • B. Uttara, A. Singh, P. Zamboni, and R. Mahajan Reactions of myeloperoxidase-derived oxidants with biological substrates: gaining chemical insight into human inflammatory diseases Curr Med Chem 16 2009 4419 4444
    • (2009) Curr Med Chem , vol.16 , pp. 4419-4444
    • Uttara, B.1    Singh, A.2    Zamboni, P.3    Mahajan, R.4
  • 14
    • 62549102431 scopus 로고    scopus 로고
    • Reactive oxygen species: Destroyers or messengers?
    • G. Bartosz Reactive oxygen species: destroyers or messengers? Biochem Pharmacol 77 2009 1303 1315
    • (2009) Biochem Pharmacol , vol.77 , pp. 1303-1315
    • Bartosz, G.1
  • 15
    • 32444433202 scopus 로고    scopus 로고
    • Free radicals, metals and antioxidants in oxidative stress-induced cancer
    • M. Valko, C.J. Rhodes, J. Moncol, M. Izakovic, and M. Mazur Free radicals, metals and antioxidants in oxidative stress-induced cancer Chem Biol Interact 160 2006 1 40
    • (2006) Chem Biol Interact , vol.160 , pp. 1-40
    • Valko, M.1    Rhodes, C.J.2    Moncol, J.3    Izakovic, M.4    Mazur, M.5
  • 16
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • W. Dröge Free radicals in the physiological control of cell function Physiol Rev 82 2002 47 95
    • (2002) Physiol Rev , vol.82 , pp. 47-95
    • Dröge, W.1
  • 17
    • 84884528066 scopus 로고    scopus 로고
    • Bacterial responses to reactive chlorine species
    • M.J. Gray, W.Y. Wholey, and U. Jakob Bacterial responses to reactive chlorine species Annu Rev Microbiol 67 2013 141 160
    • (2013) Annu Rev Microbiol , vol.67 , pp. 141-160
    • Gray, M.J.1    Wholey, W.Y.2    Jakob, U.3
  • 18
    • 84886446627 scopus 로고    scopus 로고
    • Protein rescue from aggregates by powerful molecular chaperone machines
    • S.M. Doyle, O. Genest, and S. Wickner Protein rescue from aggregates by powerful molecular chaperone machines Nat Rev Mol Cell Biol 14 2013 617 629
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 617-629
    • Doyle, S.M.1    Genest, O.2    Wickner, S.3
  • 19
    • 84872476329 scopus 로고    scopus 로고
    • Redox reactions and microbial killing in the neutrophil phagosome
    • C.C. Winterbourn, and A.J. Kettle Redox reactions and microbial killing in the neutrophil phagosome Antioxid Redox Signal 18 2013 642 660
    • (2013) Antioxid Redox Signal , vol.18 , pp. 642-660
    • Winterbourn, C.C.1    Kettle, A.J.2
  • 20
    • 0033840437 scopus 로고    scopus 로고
    • Bactericidal activity of micromolar N-chlorotaurine: Evidence for its antimicrobial function in the human defense system
    • M. Nagl, M.W. Hess, K. Pfaller, P. Hengster, and W. Gottardi Bactericidal activity of micromolar N-chlorotaurine: evidence for its antimicrobial function in the human defense system Antimicrob Agents Chemother 44 2000 2507 2513
    • (2000) Antimicrob Agents Chemother , vol.44 , pp. 2507-2513
    • Nagl, M.1    Hess, M.W.2    Pfaller, K.3    Hengster, P.4    Gottardi, W.5
  • 21
    • 0030723030 scopus 로고    scopus 로고
    • Uses of inorganic hypochlorite (bleach) in health-care facilities
    • W.A. Rutala, and D.J. Weber Uses of inorganic hypochlorite (bleach) in health-care facilities Clin Microbiol Rev 10 1997 597 610
    • (1997) Clin Microbiol Rev , vol.10 , pp. 597-610
    • Rutala, W.A.1    Weber, D.J.2
  • 22
    • 0020052075 scopus 로고
    • Phagocyte-generated oxygen metabolites and cellular injury
    • S.J. Weiss, and A.F. LoBuglio Phagocyte-generated oxygen metabolites and cellular injury Lab Invest 47 1982 5 18
    • (1982) Lab Invest , vol.47 , pp. 5-18
    • Weiss, S.J.1    Lobuglio, A.F.2
  • 23
    • 0030220396 scopus 로고    scopus 로고
    • Hypochlorous acid interactions with thiols, nucleotides, DNA, and other biological substrates
    • W.A. Prütz Hypochlorous acid interactions with thiols, nucleotides, DNA, and other biological substrates Arch Biochem Biophys 332 1996 110 120
    • (1996) Arch Biochem Biophys , vol.332 , pp. 110-120
    • Prütz, W.A.1
  • 24
    • 84908456643 scopus 로고    scopus 로고
    • Protein chlorination in neutrophil phagosomes and correlation with bacterial killing
    • J.N. Green, A.J. Kettle, and C.C. Winterbourn Protein chlorination in neutrophil phagosomes and correlation with bacterial killing Free Radic Biol Med 77 2014 49 56
    • (2014) Free Radic Biol Med , vol.77 , pp. 49-56
    • Green, J.N.1    Kettle, A.J.2    Winterbourn, C.C.3
  • 25
    • 77954623743 scopus 로고    scopus 로고
    • Dual oxidase in mucosal immunity and host-microbe homeostasis
    • Y.S. Bae, M.K. Choi, and W.-J. Lee Dual oxidase in mucosal immunity and host-microbe homeostasis Trends Immunol 31 2010 278 287
    • (2010) Trends Immunol , vol.31 , pp. 278-287
    • Bae, Y.S.1    Choi, M.K.2    Lee, W.-J.3
  • 27
    • 27644498442 scopus 로고    scopus 로고
    • A direct role for dual oxidase in Drosophila gut immunity
    • E.M. Ha, C.T. Oh, Y.S. Bae, and W.J. Lee A direct role for dual oxidase in Drosophila gut immunity Science 310 2005 847 850
    • (2005) Science , vol.310 , pp. 847-850
    • Ha, E.M.1    Oh, C.T.2    Bae, Y.S.3    Lee, W.J.4
  • 28
    • 84900537629 scopus 로고    scopus 로고
    • Role of DUOX in gut inflammation: Lessons from Drosophila model of gut-microbiota interactions
    • S.-H. Kim, and W.-J. Lee Role of DUOX in gut inflammation: lessons from Drosophila model of gut-microbiota interactions Front Cell Infect Microbiol 3 2013 1 12
    • (2013) Front Cell Infect Microbiol , vol.3 , pp. 1-12
    • Kim, S.-H.1    Lee, W.-J.2
  • 29
    • 84886780246 scopus 로고    scopus 로고
    • Dual oxidases control release of hydrogen peroxide by the gastric epithelium to prevent Helicobacter felis infection and inflammation in mice
    • H. Grasberger, M. El Zaatari, D.T. Dang, and J.L. Merchant Dual oxidases control release of hydrogen peroxide by the gastric epithelium to prevent Helicobacter felis infection and inflammation in mice Gastroenterology 145 2013 1045 1054
    • (2013) Gastroenterology , vol.145 , pp. 1045-1054
    • Grasberger, H.1    El Zaatari, M.2    Dang, D.T.3    Merchant, J.L.4
  • 30
    • 79954997251 scopus 로고    scopus 로고
    • A specific and sensitive method for detection of hypochlorous acid for the imaging of microbe-induced HOCl production
    • X. Chen, K.-A. Lee, E.-M. Ha, K.M. Lee, Y.Y. Seo, and H.K. Choi A specific and sensitive method for detection of hypochlorous acid for the imaging of microbe-induced HOCl production Chem Commun 47 2011 4373 4375
    • (2011) Chem Commun , vol.47 , pp. 4373-4375
    • Chen, X.1    Lee, K.-A.2    Ha, E.-M.3    Lee, K.M.4    Seo, Y.Y.5    Choi, H.K.6
  • 31
    • 0033117503 scopus 로고    scopus 로고
    • Mechanisms of oxidative damage by myeloperoxidase in atherosclerosis and other inflammatory disorders
    • J.W. Heinecke Mechanisms of oxidative damage by myeloperoxidase in atherosclerosis and other inflammatory disorders J Lab Clin Med 133 1999 321 325
    • (1999) J Lab Clin Med , vol.133 , pp. 321-325
    • Heinecke, J.W.1
  • 32
    • 84876890840 scopus 로고    scopus 로고
    • Redox regulation of protein kinases
    • A. Corcoran, and T.G. Cotter Redox regulation of protein kinases FEBS J 280 2013 1944 1965
    • (2013) FEBS J , vol.280 , pp. 1944-1965
    • Corcoran, A.1    Cotter, T.G.2
  • 33
    • 84889585312 scopus 로고    scopus 로고
    • Protein oxidative modifications: Beneficial roles in disease and health
    • Z. Cai, and L.-J. Yan Protein oxidative modifications: beneficial roles in disease and health J Biochem Pharmacol Res 1 2013 15 26
    • (2013) J Biochem Pharmacol Res , vol.1 , pp. 15-26
    • Cai, Z.1    Yan, L.-J.2
  • 34
    • 0022272178 scopus 로고
    • Free-radical production and oxidative reactions of hemoglobin
    • C.C. Winterbourn Free-radical production and oxidative reactions of hemoglobin Environ Health Perspect 64 1985 321 330
    • (1985) Environ Health Perspect , vol.64 , pp. 321-330
    • Winterbourn, C.C.1
  • 35
    • 0032525801 scopus 로고    scopus 로고
    • Hypochlorite-induced damage to proteins: Formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation
    • C.L. Hawkins, and M.J. Davies Hypochlorite-induced damage to proteins: formation of nitrogen-centred radicals from lysine residues and their role in protein fragmentation Biochem J 332 1998 617 625
    • (1998) Biochem J , vol.332 , pp. 617-625
    • Hawkins, C.L.1    Davies, M.J.2
  • 36
    • 62549088648 scopus 로고    scopus 로고
    • Protein stability and resistance to oxidative stress are determinants of longevity in the longest-living rodent, the naked mole-rat
    • V.I. Perez, R. Buffenstein, V. Masamsetti, S. Leonard, A.B. Salmon, and J. Mele Protein stability and resistance to oxidative stress are determinants of longevity in the longest-living rodent, the naked mole-rat Proc Natl Acad Sci U S A 106 2009 3059 3064
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3059-3064
    • Perez, V.I.1    Buffenstein, R.2    Masamsetti, V.3    Leonard, S.4    Salmon, A.B.5    Mele, J.6
  • 37
    • 84887024669 scopus 로고    scopus 로고
    • Non-enzymatic post-translational protein modifications and proteostasis network deregulation in carcinogenesis
    • I.P. Trougakos, F. Sesti, E. Tsakiri, and V.G. Gorgoulis Non-enzymatic post-translational protein modifications and proteostasis network deregulation in carcinogenesis J Proteomics 92 2013 274 298
    • (2013) J Proteomics , vol.92 , pp. 274-298
    • Trougakos, I.P.1    Sesti, F.2    Tsakiri, E.3    Gorgoulis, V.G.4
  • 39
    • 0034781061 scopus 로고    scopus 로고
    • Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds
    • D.I. Pattison, and M.J. Davies Absolute rate constants for the reaction of hypochlorous acid with protein side chains and peptide bonds Chem Res Toxicol 14 2001 1453 1464
    • (2001) Chem Res Toxicol , vol.14 , pp. 1453-1464
    • Pattison, D.I.1    Davies, M.J.2
  • 41
    • 0037205455 scopus 로고    scopus 로고
    • Proteomics analysis of cellular response to oxidative stress: Evidence for in vivo overoxidation of peroxiredoxins at their active site
    • T. Rabilloud, M. Heller, F. Gasnier, S. Luche, C. Rey, and R. Aebersold Proteomics analysis of cellular response to oxidative stress: evidence for in vivo overoxidation of peroxiredoxins at their active site J Biol Chem 277 2002 19396 19401
    • (2002) J Biol Chem , vol.277 , pp. 19396-19401
    • Rabilloud, T.1    Heller, M.2    Gasnier, F.3    Luche, S.4    Rey, C.5    Aebersold, R.6
  • 43
    • 34547441421 scopus 로고    scopus 로고
    • Sulfiredoxin, the cysteine sulfinic acid reductase specific to 2-Cys peroxiredoxin: Its discovery, mechanism of action, and biological significance
    • S.G. Rhee, W. Jeong, T.-S. Chang, and H.A. Woo Sulfiredoxin, the cysteine sulfinic acid reductase specific to 2-Cys peroxiredoxin: its discovery, mechanism of action, and biological significance Kidney Int 72 2007 S3 S8
    • (2007) Kidney Int , vol.72 , pp. S3-S8
    • Rhee, S.G.1    Jeong, W.2    Chang, T.-S.3    Woo, H.A.4
  • 47
    • 34347264532 scopus 로고    scopus 로고
    • Thioredoxin glutathione reductase from Schistosoma mansoni: An essential parasite enzyme and a key drug target
    • A.N. Kuntz, E. Davioud-Charvet, A.A. Sayed, L.L. Califf, J. Dessolin, and E.S.J. Amer Thioredoxin glutathione reductase from Schistosoma mansoni: an essential parasite enzyme and a key drug target PLoS Med 4 2007 e206
    • (2007) PLoS Med , vol.4 , pp. e206
    • Kuntz, A.N.1    Davioud-Charvet, E.2    Sayed, A.A.3    Califf, L.L.4    Dessolin, J.5    Amer, E.S.J.6
  • 48
    • 84892366219 scopus 로고    scopus 로고
    • The thioredoxin antioxidant system
    • J. Lu, and A. Holmgren The thioredoxin antioxidant system Free Radic Biol Med 66 2014 75 87
    • (2014) Free Radic Biol Med , vol.66 , pp. 75-87
    • Lu, J.1    Holmgren, A.2
  • 49
    • 12844260763 scopus 로고    scopus 로고
    • Methionine oxidation by reactive oxygen species: Reaction mechanisms and relevance to Alzheimer's disease
    • C. Schöneich Methionine oxidation by reactive oxygen species: reaction mechanisms and relevance to Alzheimer's disease Biochim Biophys Acta (BBA) Proteins Proteomics 1703 2005 111 119
    • (2005) Biochim Biophys Acta (BBA) Proteins Proteomics , vol.1703 , pp. 111-119
    • Schöneich, C.1
  • 50
    • 84901803984 scopus 로고    scopus 로고
    • Reevaluation of the rate constants for the reaction of hypochlorous acid (HOCl) with cysteine, methionine, and peptide derivatives using a new competition kinetic approach
    • C. Storkey, M.J. Davies, and D.I. Pattison Reevaluation of the rate constants for the reaction of hypochlorous acid (HOCl) with cysteine, methionine, and peptide derivatives using a new competition kinetic approach Free Radic Biol Med 73 2014 60 66
    • (2014) Free Radic Biol Med , vol.73 , pp. 60-66
    • Storkey, C.1    Davies, M.J.2    Pattison, D.I.3
  • 51
    • 84913541407 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase: Chemistry, substrate binding, recycling process and oxidase activity
    • S. Boschi-Muller, and G. Branlant Methionine sulfoxide reductase: chemistry, substrate binding, recycling process and oxidase activity Bioorg Chem 57 2014 222 230
    • (2014) Bioorg Chem , vol.57 , pp. 222-230
    • Boschi-Muller, S.1    Branlant, G.2
  • 54
    • 84863797987 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases preferentially reduce unfolded oxidized proteins and protect cells from oxidative protein unfolding
    • L. Tarrago, A. Kaya, E. Weerapana, S.M. Marino, and V.N. Gladyshev Methionine sulfoxide reductases preferentially reduce unfolded oxidized proteins and protect cells from oxidative protein unfolding J Biol Chem 287 2012 24448 24459
    • (2012) J Biol Chem , vol.287 , pp. 24448-24459
    • Tarrago, L.1    Kaya, A.2    Weerapana, E.3    Marino, S.M.4    Gladyshev, V.N.5
  • 55
    • 71549124963 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase A (MsrA) restores α-crystallin chaperone activity lost upon methionine oxidation
    • L.A. Brennan, W. Lee, F.J. Giblin, L.L. David, and M. Kantorow Methionine sulfoxide reductase A (MsrA) restores α-crystallin chaperone activity lost upon methionine oxidation Biochim Biophys Acta (BBA) Gen Subj 1790 2009 1665 1672
    • (2009) Biochim Biophys Acta (BBA) Gen Subj , vol.1790 , pp. 1665-1672
    • Brennan, L.A.1    Lee, W.2    Giblin, F.J.3    David, L.L.4    Kantorow, M.5
  • 56
    • 84887520635 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase repair by Helicobacter pylori methionine sulfoxide reductase
    • S.L. Benoit, K. Bayyareddy, M. Mahawar, J.S. Sharp, and R.J. Maier Alkyl hydroperoxide reductase repair by Helicobacter pylori methionine sulfoxide reductase J Bacteriol 195 2013 5396 5401
    • (2013) J Bacteriol , vol.195 , pp. 5396-5401
    • Benoit, S.L.1    Bayyareddy, K.2    Mahawar, M.3    Sharp, J.S.4    Maier, R.J.5
  • 57
    • 2442456741 scopus 로고    scopus 로고
    • Potential role of methionine sulfoxide in the inactivation of the chaperone GroEL by hypochlorous acid (HOCl) and peroxynitrite (ONOO -)
    • H.K. Khor, M.T. Fisher, and C. Schoneich Potential role of methionine sulfoxide in the inactivation of the chaperone GroEL by hypochlorous acid (HOCl) and peroxynitrite (ONOO -) J Biol Chem 279 2004 19486 19493
    • (2004) J Biol Chem , vol.279 , pp. 19486-19493
    • Khor, H.K.1    Fisher, M.T.2    Schoneich, C.3
  • 58
    • 79956303754 scopus 로고    scopus 로고
    • Synergistic roles of Helicobacter pylori methionine sulfoxide reductase and GroEL in repairing oxidant-damaged catalase
    • M. Mahawar, V. Tran, J.S. Sharp, and R.J. Maier Synergistic roles of Helicobacter pylori methionine sulfoxide reductase and GroEL in repairing oxidant-damaged catalase J Biol Chem 286 2011 19159 19169
    • (2011) J Biol Chem , vol.286 , pp. 19159-19169
    • Mahawar, M.1    Tran, V.2    Sharp, J.S.3    Maier, R.J.4
  • 59
    • 84919626405 scopus 로고    scopus 로고
    • In Salmonella enterica, the Gcn5-related acetyltransferase MddA (formerly YncA) acetylates methionine sulfoximine and methionine sulfone, blocking their toxic effects
    • K.L. Hentchel, and J.C. Escalante-Semerena In Salmonella enterica, the Gcn5-related acetyltransferase MddA (formerly YncA) acetylates methionine sulfoximine and methionine sulfone, blocking their toxic effects J Bacteriol 197 2014 314 325
    • (2014) J Bacteriol , vol.197 , pp. 314-325
    • Hentchel, K.L.1    Escalante-Semerena, J.C.2
  • 60
    • 33750564770 scopus 로고    scopus 로고
    • Reactions of myeloperoxidase-derived oxidants with biological substrates: Gaining chemical insight into human inflammatory diseases
    • D. Pattison, and M. Davies Reactions of myeloperoxidase-derived oxidants with biological substrates: gaining chemical insight into human inflammatory diseases Curr Med Chem 13 2006 3271 3290
    • (2006) Curr Med Chem , vol.13 , pp. 3271-3290
    • Pattison, D.1    Davies, M.2
  • 63
    • 55449092300 scopus 로고    scopus 로고
    • Bleach activates a redox-regulated chaperone by oxidative protein unfolding
    • J. Winter, M. Ilbert, P.C.F. Graf, D. Özcelik, and U. Jakob Bleach activates a redox-regulated chaperone by oxidative protein unfolding Cell 135 2008 691 701
    • (2008) Cell , vol.135 , pp. 691-701
    • Winter, J.1    Ilbert, M.2    Graf, P.C.F.3    Özcelik, D.4    Jakob, U.5
  • 64
    • 0029827844 scopus 로고    scopus 로고
    • Hypochlorous acid activates the heat shock and soxRS systems of Escherichia coli
    • S. Dukan, S. Dadon, D.R. Smulski, and S. Belin Hypochlorous acid activates the heat shock and soxRS systems of Escherichia coli Appl Environ Microbiol 62 1996 4003 4008
    • (1996) Appl Environ Microbiol , vol.62 , pp. 4003-4008
    • Dukan, S.1    Dadon, S.2    Smulski, D.R.3    Belin, S.4
  • 65
    • 0025632973 scopus 로고
    • DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32
    • D. Straus, W. Walter, and C.A. Gross DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32 Genes Dev 4 1990 2202 2209
    • (1990) Genes Dev , vol.4 , pp. 2202-2209
    • Straus, D.1    Walter, W.2    Gross, C.A.3
  • 67
    • 84896718349 scopus 로고    scopus 로고
    • The role of thiol oxidative stress response in heat-induced protein aggregate formation during thermotolerance in Bacillus subtilis
    • S. Runde, N. Molière, A. Heinz, E. Maisonneuve, A. Janczikowski, and A.K.W. Elsholz The role of thiol oxidative stress response in heat-induced protein aggregate formation during thermotolerance in Bacillus subtilis Mol Microbiol 91 2014 1036 1052
    • (2014) Mol Microbiol , vol.91 , pp. 1036-1052
    • Runde, S.1    Molière, N.2    Heinz, A.3    Maisonneuve, E.4    Janczikowski, A.5    Elsholz, A.K.W.6
  • 68
    • 84880022114 scopus 로고    scopus 로고
    • Nonnative disulfide bond formation activates the σ32-dependent heat shock response in Escherichia coli
    • A. Müller, J.H. Hoffmann, H.E. Meyer, F. Narberhaus, U. Jakob, and L.I. Leichert Nonnative disulfide bond formation activates the σ32-dependent heat shock response in Escherichia coli J Bacteriol 195 2013 2807 2816
    • (2013) J Bacteriol , vol.195 , pp. 2807-2816
    • Müller, A.1    Hoffmann, J.H.2    Meyer, H.E.3    Narberhaus, F.4    Jakob, U.5    Leichert, L.I.6
  • 69
    • 79951896245 scopus 로고    scopus 로고
    • Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegans
    • C. Kumsta, M. Thamsen, and U. Jakob Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegans Antioxid Redox Signal 14 2011 1023 1037
    • (2011) Antioxid Redox Signal , vol.14 , pp. 1023-1037
    • Kumsta, C.1    Thamsen, M.2    Jakob, U.3
  • 70
    • 34548337296 scopus 로고    scopus 로고
    • Hydroxyl radical-mediated modification of proteins as probes for structural proteomics
    • G. Xu, and M.R. Chance Hydroxyl radical-mediated modification of proteins as probes for structural proteomics Chem Rev 107 2007 3514 3543
    • (2007) Chem Rev , vol.107 , pp. 3514-3543
    • Xu, G.1    Chance, M.R.2
  • 71
    • 79954414554 scopus 로고    scopus 로고
    • Modeling general proteostasis: Proteome balance in health and disease
    • D.M. Roth, and W.E. Balch Modeling general proteostasis: proteome balance in health and disease Curr Opin Cell Biol 23 2011 126 134
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 126-134
    • Roth, D.M.1    Balch, W.E.2
  • 72
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • B. Bukau, J. Weissman, and A. Horwich Molecular chaperones and protein quality control Cell 125 2006 443 451
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 73
    • 38549119467 scopus 로고    scopus 로고
    • Chaperones in control of protein disaggregation
    • K. Liberek, A. Lewandowska, and S. Ziętkiewicz Chaperones in control of protein disaggregation EMBO J 27 2008 328 335
    • (2008) EMBO J , vol.27 , pp. 328-335
    • Liberek, K.1    Lewandowska, A.2    Ziętkiewicz, S.3
  • 74
    • 84886412961 scopus 로고    scopus 로고
    • Chaperone machines for protein folding, unfolding and disaggregation
    • H. Saibil Chaperone machines for protein folding, unfolding and disaggregation Nat Rev Mol Cell Biol 14 2013 630 642
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 630-642
    • Saibil, H.1
  • 75
    • 13244279524 scopus 로고    scopus 로고
    • Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33
    • J. Winter, K. Linke, A. Jatzek, and U. Jakob Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33 Mol Cell 17 2005 381 392
    • (2005) Mol Cell , vol.17 , pp. 381-392
    • Winter, J.1    Linke, K.2    Jatzek, A.3    Jakob, U.4
  • 76
    • 0031946770 scopus 로고    scopus 로고
    • How chaperones fold proteins
    • M. Beissinger, and J. Buchner How chaperones fold proteins J Biol Chem 379 1998 245 259
    • (1998) J Biol Chem , vol.379 , pp. 245-259
    • Beissinger, M.1    Buchner, J.2
  • 77
    • 0842328576 scopus 로고    scopus 로고
    • Identification of a redox-regulated chaperone network
    • J.H. Hoffmann, K. Linke, P.C. Graf, H. Lilie, and U. Jakob Identification of a redox-regulated chaperone network EMBO J 23 2003 160 168
    • (2003) EMBO J , vol.23 , pp. 160-168
    • Hoffmann, J.H.1    Linke, K.2    Graf, P.C.3    Lilie, H.4    Jakob, U.5
  • 78
    • 84878851013 scopus 로고    scopus 로고
    • The proteasome and the degradation of oxidized proteins. Part i - Structure of proteasomes
    • T. Jung, and T. Grune The proteasome and the degradation of oxidized proteins. Part I - structure of proteasomes Redox Biol 1 2013 178 182
    • (2013) Redox Biol , vol.1 , pp. 178-182
    • Jung, T.1    Grune, T.2
  • 79
    • 84892182166 scopus 로고    scopus 로고
    • The proteasome and the degradation of oxidized proteins. Part II - Protein oxidation and proteasomal degradation
    • T. Jung, A. Höhn, and T. Grune The proteasome and the degradation of oxidized proteins. Part II - protein oxidation and proteasomal degradation Redox Biol 2 2014 99 104
    • (2014) Redox Biol , vol.2 , pp. 99-104
    • Jung, T.1    Höhn, A.2    Grune, T.3
  • 81
    • 0022348883 scopus 로고
    • Alterations in adenosine triphosphate and energy charge in cultured endothelial and P388D1 cells after oxidant injury
    • R.G. Spragg, D.B. Hinshaw, P.A. Hyslop, I.U. Schraufstätter, and C.G. Cochrane Alterations in adenosine triphosphate and energy charge in cultured endothelial and P388D1 cells after oxidant injury J Clin Invest 76 1985 1471 1476
    • (1985) J Clin Invest , vol.76 , pp. 1471-1476
    • Spragg, R.G.1    Hinshaw, D.B.2    Hyslop, P.A.3    Schraufstätter, I.U.4    Cochrane, C.G.5
  • 82
    • 64549097266 scopus 로고    scopus 로고
    • Thiol-based redox switches in eukaryotic proteins
    • N. Brandes, S. Schmitt, and U. Jakob Thiol-based redox switches in eukaryotic proteins Antioxid Redox Signal 11 2009 997 1014
    • (2009) Antioxid Redox Signal , vol.11 , pp. 997-1014
    • Brandes, N.1    Schmitt, S.2    Jakob, U.3
  • 83
    • 0036369545 scopus 로고    scopus 로고
    • S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase: Role of thiol oxidation and catalysis by glutaredoxin
    • I.A. Cotgreave, R. Gerdes, I. Schuppe-Koisstinen, and C. Lind S-glutathionylation of glyceraldehyde-3-phosphate dehydrogenase: role of thiol oxidation and catalysis by glutaredoxin Methods Enzymol 348 2002 175 182
    • (2002) Methods Enzymol , vol.348 , pp. 175-182
    • Cotgreave, I.A.1    Gerdes, R.2    Schuppe-Koisstinen, I.3    Lind, C.4
  • 84
    • 46149125288 scopus 로고    scopus 로고
    • Reactive oxygen species special feature: Quantifying changes in the thiol redox proteome upon oxidative stress in vivo
    • L.I. Leichert, F. Gehrke, H.V. Gudiseva, T. Blackwell, M. Ilbert, and A.K. Walker Reactive oxygen species special feature: quantifying changes in the thiol redox proteome upon oxidative stress in vivo Proc Natl Acad Sci U S A 105 2008 8197 8202
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 8197-8202
    • Leichert, L.I.1    Gehrke, F.2    Gudiseva, H.V.3    Blackwell, T.4    Ilbert, M.5    Walker, A.K.6
  • 86
    • 84937771130 scopus 로고    scopus 로고
    • Cross-talk between redox regulation and the ubiquitin-proteasome system in mammalian cell differentiation
    • [in press]
    • M. Demasi, V. Simões, and D. Bonatto Cross-talk between redox regulation and the ubiquitin-proteasome system in mammalian cell differentiation Biochim Biophys Acta (BBA) Gen Subj 2015 10.1016/j.bbagen.2014.10.031 [in press]
    • (2015) Biochim Biophys Acta (BBA) Gen Subj
    • Demasi, M.1    Simões, V.2    Bonatto, D.3
  • 87
    • 0027186528 scopus 로고
    • Characterization of twenty-six new heat shock genes of Escherichia coli
    • S.E. Chuang, and F.R. Blattner Characterization of twenty-six new heat shock genes of Escherichia coli J Bacteriol 175 1993 5242 5252
    • (1993) J Bacteriol , vol.175 , pp. 5242-5252
    • Chuang, S.E.1    Blattner, F.R.2
  • 88
    • 34249102506 scopus 로고    scopus 로고
    • Functional characterization of Hsp33 protein from Bacillus psychrosaccharolyticus: Additional function of HSP33 on resistance to solvent stress
    • H.-J. Kang, D.-H. Heo, S.-W. Choi, K.-N. Kim, J. Shim, and C.-W. Kim Functional characterization of Hsp33 protein from Bacillus psychrosaccharolyticus: additional function of HSP33 on resistance to solvent stress Biochem Biophys Res Commun 358 2007 743 750
    • (2007) Biochem Biophys Res Commun , vol.358 , pp. 743-750
    • Kang, H.-J.1    Heo, D.-H.2    Choi, S.-W.3    Kim, K.-N.4    Shim, J.5    Kim, C.-W.6
  • 89
    • 0033524938 scopus 로고    scopus 로고
    • Chaperone activity with a redox switch
    • U. Jakob, W. Muse, M. Eser, and J.C.A. Bardwell Chaperone activity with a redox switch Cell 96 1999 341 352
    • (1999) Cell , vol.96 , pp. 341-352
    • Jakob, U.1    Muse, W.2    Eser, M.3    Bardwell, J.C.A.4
  • 92
    • 84899128105 scopus 로고    scopus 로고
    • Bile salts act as effective protein-unfolding agents and instigators of disulfide stress in vivo
    • C.M. Cremers, D. Knoefler, V. Vitvitsky, R. Banerjee, and U. Jakob Bile salts act as effective protein-unfolding agents and instigators of disulfide stress in vivo Proc Natl Acad Sci U S A 111 2014 1610 1619
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 1610-1619
    • Cremers, C.M.1    Knoefler, D.2    Vitvitsky, V.3    Banerjee, R.4    Jakob, U.5
  • 94
    • 84857371785 scopus 로고    scopus 로고
    • Hsp33 confers bleach resistance by protecting elongation factor Tu against oxidative degradation in Vibrio cholerae
    • W.Y. Wholey, and U. Jakob Hsp33 confers bleach resistance by protecting elongation factor Tu against oxidative degradation in Vibrio cholerae Mol Microbiol 83 2012 981 991
    • (2012) Mol Microbiol , vol.83 , pp. 981-991
    • Wholey, W.Y.1    Jakob, U.2
  • 96
    • 0034623949 scopus 로고    scopus 로고
    • Redox switch of Hsp33 has a novel zinc-binding motif
    • U. Jakob, M. Eser, and J.C.A. Bardwell Redox switch of Hsp33 has a novel zinc-binding motif J Biol Chem 275 2000 38302 38310
    • (2000) J Biol Chem , vol.275 , pp. 38302-38310
    • Jakob, U.1    Eser, M.2    Bardwell, J.C.A.3
  • 98
    • 84884197445 scopus 로고    scopus 로고
    • Oxidant sensing by reversible disulfide bond formation
    • C.M. Cremers, and U. Jakob Oxidant sensing by reversible disulfide bond formation J Biol Chem 288 2013 26489 26496
    • (2013) J Biol Chem , vol.288 , pp. 26489-26496
    • Cremers, C.M.1    Jakob, U.2
  • 99
    • 77951216943 scopus 로고    scopus 로고
    • Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone
    • C.M. Cremers, D. Reichmann, J. Hausmann, M. Ilbert, and U. Jakob Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone J Biol Chem 285 2010 11243 11251
    • (2010) J Biol Chem , vol.285 , pp. 11243-11251
    • Cremers, C.M.1    Reichmann, D.2    Hausmann, J.3    Ilbert, M.4    Jakob, U.5
  • 100
    • 84863230577 scopus 로고    scopus 로고
    • Order out of disorder: Working cycle of an intrinsically unfolded chaperone
    • D. Reichmann, Y. Xu, C.M. Cremers, M. Ilbert, R. Mittelman, and M.C. Fitzgerald Order out of disorder: working cycle of an intrinsically unfolded chaperone Cell 148 2012 947 957
    • (2012) Cell , vol.148 , pp. 947-957
    • Reichmann, D.1    Xu, Y.2    Cremers, C.M.3    Ilbert, M.4    Mittelman, R.5    Fitzgerald, M.C.6
  • 101
    • 84870065644 scopus 로고    scopus 로고
    • Conditional disorder in chaperone action
    • J.C.A. Bardwell, and U. Jakob Conditional disorder in chaperone action Trends Biochem Sci 37 2012 517 525
    • (2012) Trends Biochem Sci , vol.37 , pp. 517-525
    • Bardwell, J.C.A.1    Jakob, U.2
  • 102
    • 84902446848 scopus 로고    scopus 로고
    • Conditionally and transiently disordered proteins: Awakening cryptic disorder to regulate protein function
    • U. Jakob, R. Kriwacki, and V.N. Uversky Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function Chem Rev 114 2014 6779 6805
    • (2014) Chem Rev , vol.114 , pp. 6779-6805
    • Jakob, U.1    Kriwacki, R.2    Uversky, V.N.3
  • 103
    • 27144448839 scopus 로고    scopus 로고
    • Some like it hot: The structure and function of small heat-shock proteins
    • M. Haslbeck, T. Franzmann, D. Weinfurtner, and J. Buchner Some like it hot: the structure and function of small heat-shock proteins Nat Struct Mol Biol 12 2005 842 846
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 842-846
    • Haslbeck, M.1    Franzmann, T.2    Weinfurtner, D.3    Buchner, J.4
  • 104
    • 70349470609 scopus 로고    scopus 로고
    • Substrate binding site flexibility of the small heat shock protein molecular chaperones
    • N. Jaya, V. Garcia, and E. Vierling Substrate binding site flexibility of the small heat shock protein molecular chaperones Proc Natl Acad Sci U S A 106 2009 15604 15609
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 15604-15609
    • Jaya, N.1    Garcia, V.2    Vierling, E.3
  • 105
    • 84879161353 scopus 로고    scopus 로고
    • The roles of conditional disorder in redox proteins
    • D. Reichmann, and U. Jakob The roles of conditional disorder in redox proteins Curr Opin Struct Biol 23 2013 436 442
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 436-442
    • Reichmann, D.1    Jakob, U.2
  • 110
    • 66649131702 scopus 로고    scopus 로고
    • Redox-regulated chaperones
    • C. Kumsta, and U. Jakob Redox-regulated chaperones Biochemistry 48 2009 4666 4676
    • (2009) Biochemistry , vol.48 , pp. 4666-4676
    • Kumsta, C.1    Jakob, U.2
  • 112
    • 84881158368 scopus 로고    scopus 로고
    • Neutrophil-mediated oxidation of erythrocyte peroxiredoxin 2 as a potential marker of oxidative stress in inflammation
    • S.B. Bayer, G. Maghzal, R. Stocker, M.B. Hampton, and C.C. Winterbourn Neutrophil-mediated oxidation of erythrocyte peroxiredoxin 2 as a potential marker of oxidative stress in inflammation FASEB J 27 2013 3315 3322
    • (2013) FASEB J , vol.27 , pp. 3315-3322
    • Bayer, S.B.1    Maghzal, G.2    Stocker, R.3    Hampton, M.B.4    Winterbourn, C.C.5
  • 113
  • 114
    • 84920886550 scopus 로고    scopus 로고
    • The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions
    • W. Voth, M. Schick, S. Gates, S. Li, F. Vilardi, and I. Gostimskaya The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions Mol Cell 56 2014 116 127
    • (2014) Mol Cell , vol.56 , pp. 116-127
    • Voth, W.1    Schick, M.2    Gates, S.3    Li, S.4    Vilardi, F.5    Gostimskaya, I.6
  • 115
    • 84876082949 scopus 로고    scopus 로고
    • Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked
    • K. Powis, B. Schrul, H. Tienson, I. Gostimskya, M. Breker, and S. High Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked J Cell Sci 126 2013 473
    • (2013) J Cell Sci , vol.126 , pp. 473
    • Powis, K.1    Schrul, B.2    Tienson, H.3    Gostimskya, I.4    Breker, M.5    High, S.6
  • 116
    • 33644852489 scopus 로고    scopus 로고
    • The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol
    • J. Metz, A. Wachter, B. Schmidt, J.M. Bujnicki, and B. Schwappach The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol J Biol Chem 281 2005 410 417
    • (2005) J Biol Chem , vol.281 , pp. 410-417
    • Metz, J.1    Wachter, A.2    Schmidt, B.3    Bujnicki, J.M.4    Schwappach, B.5
  • 117
    • 84861774091 scopus 로고    scopus 로고
    • The complex process of GETting tail-anchored membrane proteins to the ER
    • J.W. Chartron, W.M. Clemons Jr., and C.J. Suloway The complex process of GETting tail-anchored membrane proteins to the ER Curr Opin Struct Biol 22 2012 217 224
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 217-224
    • Chartron, J.W.1    Clemons, Jr.W.M.2    Suloway, C.J.3
  • 118
    • 84881056623 scopus 로고    scopus 로고
    • Endoplasmic reticulum targeting and insertion of tail-anchored membrane proteins by the GET pathway
    • V. Denic, V. Dotsch, and I. Sinning Endoplasmic reticulum targeting and insertion of tail-anchored membrane proteins by the GET pathway Cold Spring Harb Perspect Biol 5 2013 a013334
    • (2013) Cold Spring Harb Perspect Biol , vol.5 , pp. a013334
    • Denic, V.1    Dotsch, V.2    Sinning, I.3
  • 119
    • 78650403609 scopus 로고    scopus 로고
    • ASNA-1 activity modulates sensitivity to cisplatin
    • O. Hemmingsson, G. Kao, M. Still, and P. Naredi ASNA-1 activity modulates sensitivity to cisplatin Cancer Res 70 2010 10321 10328
    • (2010) Cancer Res , vol.70 , pp. 10321-10328
    • Hemmingsson, O.1    Kao, G.2    Still, M.3    Naredi, P.4
  • 121
    • 27144440590 scopus 로고    scopus 로고
    • Inactivation of protease inhibitors and lysozyme by hypochlorous acid: Role of side-chain oxidation and protein unfolding in loss of biological function
    • C.L. Hawkins, and M.J. Davies Inactivation of protease inhibitors and lysozyme by hypochlorous acid: role of side-chain oxidation and protein unfolding in loss of biological function Chem Res Toxicol 18 2005 1600 1610
    • (2005) Chem Res Toxicol , vol.18 , pp. 1600-1610
    • Hawkins, C.L.1    Davies, M.J.2
  • 123
    • 0141905917 scopus 로고    scopus 로고
    • Characterization of non-covalent oligomers of proteins treated with hypochlorous acid
    • A.L.P. Chapman, C.C. Winterbourn, S.O. Brennan, P.A. Jordan, and A.J. Kettle Characterization of non-covalent oligomers of proteins treated with hypochlorous acid Biochem J 375 2003 33 40
    • (2003) Biochem J , vol.375 , pp. 33-40
    • Chapman, A.L.P.1    Winterbourn, C.C.2    Brennan, S.O.3    Jordan, P.A.4    Kettle, A.J.5
  • 125
    • 84856267557 scopus 로고    scopus 로고
    • Conserved YjgF protein family deaminates reactive enamine/imine intermediates of pyridoxal 5′-phosphate (PLP)-dependent enzyme reactions
    • J.A. Lambrecht, J.M. Flynn, and D.M. Downs Conserved YjgF protein family deaminates reactive enamine/imine intermediates of pyridoxal 5′-phosphate (PLP)-dependent enzyme reactions J Biol Chem 287 2012 3454 3461
    • (2012) J Biol Chem , vol.287 , pp. 3454-3461
    • Lambrecht, J.A.1    Flynn, J.M.2    Downs, D.M.3
  • 126
    • 84880079480 scopus 로고    scopus 로고
    • Redox proteomics uncovers peroxynitrite-sensitive proteins that help Escherichia coli to overcome nitrosative stress
    • C. Lindemann, N. Lupilova, A. Muller, B. Warscheid, H.E. Meyer, and K. Kuhlmann Redox proteomics uncovers peroxynitrite-sensitive proteins that help Escherichia coli to overcome nitrosative stress J Biol Chem 288 2013 19698 19714
    • (2013) J Biol Chem , vol.288 , pp. 19698-19714
    • Lindemann, C.1    Lupilova, N.2    Muller, A.3    Warscheid, B.4    Meyer, H.E.5    Kuhlmann, K.6
  • 127
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • J. Frydman Folding of newly translated proteins in vivo: the role of molecular chaperones Annu Rev Biochem 70 2001 603 647
    • (2001) Annu Rev Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 128
    • 84876738471 scopus 로고    scopus 로고
    • Alpha 2 macroglobulin: A physiological guardian
    • A.A. Rehman, H. Ahsan, and F.H. Khan Alpha 2 macroglobulin: a physiological guardian J Cell Physiol 228 2012 1665 1675
    • (2012) J Cell Physiol , vol.228 , pp. 1665-1675
    • Rehman, A.A.1    Ahsan, H.2    Khan, F.H.3
  • 129
  • 130
    • 0019784199 scopus 로고
    • Clearance and binding of two electrophoretic "fast" forms of human alpha 2-macroglobulin
    • M.J. Imber, and S.V. Pizzo Clearance and binding of two electrophoretic "fast" forms of human alpha 2-macroglobulin J Biol Chem 256 1981 8134 8139
    • (1981) J Biol Chem , vol.256 , pp. 8134-8139
    • Imber, M.J.1    Pizzo, S.V.2
  • 131
    • 84901052763 scopus 로고    scopus 로고
    • Hypochlorite-induced structural modifications enhance the chaperone activity of human α2-macroglobulin
    • A.R. Wyatt, J.R. Kumita, R.W. Mifsud, C.A. Gooden, M.R. Wilson, and C.M. Dobson Hypochlorite-induced structural modifications enhance the chaperone activity of human α2-macroglobulin Proc Natl Acad Sci U S A 111 2014 2081 2090
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 2081-2090
    • Wyatt, A.R.1    Kumita, J.R.2    Mifsud, R.W.3    Gooden, C.A.4    Wilson, M.R.5    Dobson, C.M.6
  • 132
    • 84928664327 scopus 로고    scopus 로고
    • Molecular complementarity between simple, universal molecules and ions limited phenotype space in the precursors of cells
    • V. Norris, R.N. Reusch, K. Igarashi, and R. Root-Bernstein Molecular complementarity between simple, universal molecules and ions limited phenotype space in the precursors of cells Biol Direct 10 2014 28 47
    • (2014) Biol Direct , vol.10 , pp. 28-47
    • Norris, V.1    Reusch, R.N.2    Igarashi, K.3    Root-Bernstein, R.4
  • 133
    • 67650759738 scopus 로고    scopus 로고
    • Inorganic polyphosphate: Essential for growth and survival
    • N.N. Rao, M.R. Gómez-García, and A. Kornberg Inorganic polyphosphate: essential for growth and survival Annu Rev Biochem 78 2009 605 647
    • (2009) Annu Rev Biochem , vol.78 , pp. 605-647
    • Rao, N.N.1    Gómez-García, M.R.2    Kornberg, A.3
  • 134
    • 0026526376 scopus 로고
    • The polyphosphate kinase gene of Escherichia coli. Isolation and sequence of the ppk gene and membrane location of the protein
    • M. Akiyama, E. Crooke, and A. Kornberg The polyphosphate kinase gene of Escherichia coli. Isolation and sequence of the ppk gene and membrane location of the protein J Biol Chem 267 1992 22556 22561
    • (1992) J Biol Chem , vol.267 , pp. 22556-22561
    • Akiyama, M.1    Crooke, E.2    Kornberg, A.3
  • 135
    • 12644263413 scopus 로고    scopus 로고
    • Inorganic polyphosphate and the induction of rpoS expression
    • T. Shiba, K. Tsutsumi, and H. Yano Inorganic polyphosphate and the induction of rpoS expression Proc Natl Acad Sci U S A 94 1997 11210 11215
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 11210-11215
    • Shiba, T.1    Tsutsumi, K.2    Yano, H.3
  • 136
    • 67649391056 scopus 로고    scopus 로고
    • Phosphate-enhanced stationary-phase fitness of Escherichia coli is related to inorganic polyphosphate level
    • L.A. Schurig-Briccio, R.N. Farias, M.R. Rintoul, and V.A. Rapisarda Phosphate-enhanced stationary-phase fitness of Escherichia coli is related to inorganic polyphosphate level J Bacteriol 191 2009 4478 4481
    • (2009) J Bacteriol , vol.191 , pp. 4478-4481
    • Schurig-Briccio, L.A.1    Farias, R.N.2    Rintoul, M.R.3    Rapisarda, V.A.4
  • 137
    • 80052213074 scopus 로고    scopus 로고
    • In vitro transcription profiling of the S subunit of bacterial RNA polymerase: Re-definition of the S regulon and identification of S-specific promoter sequence elements
    • A. Maciag, C. Peano, A. Pietrelli, T. Egli, G. De Bellis, and P. Landini In vitro transcription profiling of the S subunit of bacterial RNA polymerase: re-definition of the S regulon and identification of S-specific promoter sequence elements Nucleic Acids Res 39 2011 5338 5355
    • (2011) Nucleic Acids Res , vol.39 , pp. 5338-5355
    • Maciag, A.1    Peano, C.2    Pietrelli, A.3    Egli, T.4    De Bellis, G.5    Landini, P.6
  • 138
    • 77349109095 scopus 로고    scopus 로고
    • Evolution of acidocalcisomes and their role in polyphosphate storage and osmoregulation in eukaryotic microbes
    • R. Docampo, P. Ulrich, and S.N.J. Moreno Evolution of acidocalcisomes and their role in polyphosphate storage and osmoregulation in eukaryotic microbes Phil Trans R Soc B 365 2010 775 784
    • (2010) Phil Trans R Soc B , vol.365 , pp. 775-784
    • Docampo, R.1    Ulrich, P.2    Moreno, S.N.J.3
  • 139
    • 78149439563 scopus 로고    scopus 로고
    • Polyphosphate exerts differential effects on blood clotting, depending on polymer size
    • S.A. Smith, S.H. Choi, R. Davis-Harrison, J. Huyck, J. Boettcher, and C.M. Rienstra Polyphosphate exerts differential effects on blood clotting, depending on polymer size Blood 116 2010 4353 4359
    • (2010) Blood , vol.116 , pp. 4353-4359
    • Smith, S.A.1    Choi, S.H.2    Davis-Harrison, R.3    Huyck, J.4    Boettcher, J.5    Rienstra, C.M.6
  • 140
    • 84878522215 scopus 로고    scopus 로고
    • Polyphosphate and its diverse functions in host cells and pathogens
    • S.N.J. Moreno, and R. Docampo Polyphosphate and its diverse functions in host cells and pathogens PLoS Pathog 9 2013 e1003230
    • (2013) PLoS Pathog , vol.9 , pp. e1003230
    • Moreno, S.N.J.1    Docampo, R.2
  • 142
    • 33750970871 scopus 로고    scopus 로고
    • Polyphosphate stores enhance the ability of Vibrio cholerae to overcome environmental stresses in a low-phosphate environment
    • I.K. Jahid, A.J. Silva, and J.A. Benitez Polyphosphate stores enhance the ability of Vibrio cholerae to overcome environmental stresses in a low-phosphate environment Appl Environ Microbiol 72 2006 7043 7049
    • (2006) Appl Environ Microbiol , vol.72 , pp. 7043-7049
    • Jahid, I.K.1    Silva, A.J.2    Benitez, J.A.3
  • 143
    • 84877842924 scopus 로고    scopus 로고
    • Accumulation of inorganic polyphosphate enables stress endurance and catalytic vigour in Pseudomonas putida KT2440
    • P.I. Nikel, M. Chavarria, E. Martinez-Garcia, A.C. Taylor, and V. de Lorenzo Accumulation of inorganic polyphosphate enables stress endurance and catalytic vigour in Pseudomonas putida KT2440 Microb Cell Fact 12 2013 50 64
    • (2013) Microb Cell Fact , vol.12 , pp. 50-64
    • Nikel, P.I.1    Chavarria, M.2    Martinez-Garcia, E.3    Taylor, A.C.4    De Lorenzo, V.5
  • 144
    • 84920728476 scopus 로고    scopus 로고
    • Oxidative stress protection by polyphosphate - New roles for an old player
    • M.J. Gray, and U. Jakob Oxidative stress protection by polyphosphate - new roles for an old player Curr Opin Microbiol 24 2015 1 6
    • (2015) Curr Opin Microbiol , vol.24 , pp. 1-6
    • Gray, M.J.1    Jakob, U.2
  • 145
    • 0035958678 scopus 로고    scopus 로고
    • Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. Coli
    • A. Kuroda, K. Nomura, R. Ohtomo, J.-I. Kato, T. Ikeda, and N. Takiguchi Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli Science 293 2001 705 708
    • (2001) Science , vol.293 , pp. 705-708
    • Kuroda, A.1    Nomura, K.2    Ohtomo, R.3    Kato, J.-I.4    Ikeda, T.5    Takiguchi, N.6
  • 146
    • 84899505083 scopus 로고    scopus 로고
    • Molecular mechanisms underlying bacterial persisters
    • E. Maisonneuve, and K. Gerdes Molecular mechanisms underlying bacterial persisters Cell 157 2014 539 548
    • (2014) Cell , vol.157 , pp. 539-548
    • Maisonneuve, E.1    Gerdes, K.2
  • 147
    • 33344475818 scopus 로고    scopus 로고
    • A polyphosphate-Lon protease complex in the adaptation of Escherichia coli to amino acid starvation
    • A. Kuroda A polyphosphate-Lon protease complex in the adaptation of Escherichia coli to amino acid starvation Biosci Biotechnol Biochem 70 2014 325 331
    • (2014) Biosci Biotechnol Biochem , vol.70 , pp. 325-331
    • Kuroda, A.1
  • 148
    • 84872241785 scopus 로고    scopus 로고
    • Bacterial persistence and toxin-antitoxin loci
    • K. Gerdes, and E. Maisonneuve Bacterial persistence and toxin-antitoxin loci Annu Rev Microbiol 66 2012 103 123
    • (2012) Annu Rev Microbiol , vol.66 , pp. 103-123
    • Gerdes, K.1    Maisonneuve, E.2
  • 149
    • 0141594599 scopus 로고    scopus 로고
    • Inorganic polyphosphate stimulates mammalian TOR, a kinase involved in the proliferation of mammary cancer cells
    • L. Wang, C.D. Fraley, J. Faridi, A. Kornberg, and R.A. Roth Inorganic polyphosphate stimulates mammalian TOR, a kinase involved in the proliferation of mammary cancer cells Proc Natl Acad Sci U S A 100 2011 11249 11254
    • (2011) Proc Natl Acad Sci U S A , vol.100 , pp. 11249-11254
    • Wang, L.1    Fraley, C.D.2    Faridi, J.3    Kornberg, A.4    Roth, R.A.5
  • 150
    • 36749027664 scopus 로고    scopus 로고
    • Polyphosphate kinase 1, a conserved bacterial enzyme, in a eukaryote, Dictyostelium discoideum, with a role in cytokinesis
    • H. Zhang, M.R. Gomez-Garcia, X. Shi, N.N. Rao, and A. Kornberg Polyphosphate kinase 1, a conserved bacterial enzyme, in a eukaryote, Dictyostelium discoideum, with a role in cytokinesis Proc Natl Acad Sci U S A 104 2007 16486 16491
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 16486-16491
    • Zhang, H.1    Gomez-Garcia, M.R.2    Shi, X.3    Rao, N.N.4    Kornberg, A.5
  • 153
    • 0036133115 scopus 로고    scopus 로고
    • The role of oxidative stress in the pathophysiology of cerebrovascular lesions in Alzheimer's disease
    • G. Aliev, M.A. Smith, D. Seyidova, M.L. Neal, B.T. Lamb, and A. Nunomura The role of oxidative stress in the pathophysiology of cerebrovascular lesions in Alzheimer's disease Brain Pathol 12 2006 21 35
    • (2006) Brain Pathol , vol.12 , pp. 21-35
    • Aliev, G.1    Smith, M.A.2    Seyidova, D.3    Neal, M.L.4    Lamb, B.T.5    Nunomura, A.6
  • 154
    • 84901036297 scopus 로고    scopus 로고
    • Roles of DUOX-mediated hydrogen peroxide in metabolism, host defense, and signaling
    • X. De Deken, B. Corvilain, J.E. Dumont, and F. Miot Roles of DUOX-mediated hydrogen peroxide in metabolism, host defense, and signaling Antioxid Redox Signal 20 2014 2776 2793
    • (2014) Antioxid Redox Signal , vol.20 , pp. 2776-2793
    • De Deken, X.1    Corvilain, B.2    Dumont, J.E.3    Miot, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.