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Volumn 52, Issue 6, 2012, Pages 1101-1110

Identification of a redox-sensitive switch within the JAK2 catalytic domain

Author keywords

Islet; Cysteine; Cytokines; Diabetes; Free radicals; Janus kinase; Redox

Indexed keywords

DITHIOTHREITOL; JANUS KINASE 2;

EID: 84862819547     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2011.12.025     Document Type: Article
Times cited : (32)

References (65)
  • 3
    • 33646359238 scopus 로고    scopus 로고
    • Reactive oxygen species: Influence on cerebral vascular tone
    • F.M. Faraci Reactive oxygen species: influence on cerebral vascular tone J. Appl. Physiol. 100 2006 739 743
    • (2006) J. Appl. Physiol. , vol.100 , pp. 739-743
    • Faraci, F.M.1
  • 5
    • 0037115158 scopus 로고    scopus 로고
    • Reactive oxygen species and cell signaling: Respiratory burst in macrophage signaling
    • H.J. Forman, and M. Torres Reactive oxygen species and cell signaling: respiratory burst in macrophage signaling Am. J. Respir. Crit. Care Med. 166 2002 S4 8
    • (2002) Am. J. Respir. Crit. Care Med. , vol.166 , pp. 4-8
    • Forman, H.J.1    Torres, M.2
  • 7
    • 33750620057 scopus 로고    scopus 로고
    • Oxidative stress and redox regulation of lung inflammation in COPD
    • I. Rahman, and I.M. Adcock Oxidative stress and redox regulation of lung inflammation in COPD Eur. Respir. J. 28 2006 219 242
    • (2006) Eur. Respir. J. , vol.28 , pp. 219-242
    • Rahman, I.1    Adcock, I.M.2
  • 8
    • 48249085391 scopus 로고    scopus 로고
    • Oxidative stress as a major culprit in kidney disease in diabetes
    • J.M. Forbes, M.T. Coughlan, and M.E. Cooper Oxidative stress as a major culprit in kidney disease in diabetes Diabetes 57 2008 1446 1454
    • (2008) Diabetes , vol.57 , pp. 1446-1454
    • Forbes, J.M.1    Coughlan, M.T.2    Cooper, M.E.3
  • 9
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • D. Harman Aging: a theory based on free radical and radiation chemistry J. Gerontol. 11 1956 298 300
    • (1956) J. Gerontol. , vol.11 , pp. 298-300
    • Harman, D.1
  • 10
    • 33745247801 scopus 로고    scopus 로고
    • Oxidative stress and ageing: Is ageing a cysteine deficiency syndrome?
    • W. Droge Oxidative stress and ageing: is ageing a cysteine deficiency syndrome? Philos. Trans. R. Soc. London B Biol. Sci. 360 2005 2355 2372
    • (2005) Philos. Trans. R. Soc. London B Biol. Sci. , vol.360 , pp. 2355-2372
    • Droge, W.1
  • 11
    • 0842287505 scopus 로고    scopus 로고
    • JAK2 contributes to the intrinsic capacity of primary hematopoietic cells to respond to stem cell factor
    • N. Radosevic, D. Winterstein, J.R. Keller, H. Neubauer, K. Pfeffer, and D. Linnekin JAK2 contributes to the intrinsic capacity of primary hematopoietic cells to respond to stem cell factor Exp. Hematol. 32 2004 149 156
    • (2004) Exp. Hematol. , vol.32 , pp. 149-156
    • Radosevic, N.1    Winterstein, D.2    Keller, J.R.3    Neubauer, H.4    Pfeffer, K.5    Linnekin, D.6
  • 13
    • 18244432009 scopus 로고    scopus 로고
    • Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis
    • H. Neubauer, A. Cumano, M. Muller, H. Wu, U. Huffstadt, and K. Pfeffer Jak2 deficiency defines an essential developmental checkpoint in definitive hematopoiesis Cell 93 1998 397 409
    • (1998) Cell , vol.93 , pp. 397-409
    • Neubauer, H.1    Cumano, A.2    Muller, M.3    Wu, H.4    Huffstadt, U.5    Pfeffer, K.6
  • 15
    • 0035581273 scopus 로고    scopus 로고
    • Activation of JAK2 by the oxidative stress generated with oxidized low-density lipoprotein
    • C. Maziere, M.A. Conte, and J.C. Maziere Activation of JAK2 by the oxidative stress generated with oxidized low-density lipoprotein Free Radic. Biol. Med. 31 2001 1334 1340
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1334-1340
    • Maziere, C.1    Conte, M.A.2    Maziere, J.C.3
  • 16
    • 4544265993 scopus 로고    scopus 로고
    • Jak2 tyrosine kinase mediates oxidative stress-induced apoptosis in vascular smooth muscle cells
    • E.M. Sandberg, and P.P. Sayeski Jak2 tyrosine kinase mediates oxidative stress-induced apoptosis in vascular smooth muscle cells J. Biol. Chem. 279 2004 34547 34552
    • (2004) J. Biol. Chem. , vol.279 , pp. 34547-34552
    • Sandberg, E.M.1    Sayeski, P.P.2
  • 18
    • 0032416113 scopus 로고    scopus 로고
    • Activation of the JAK-STAT pathway by reactive oxygen species
    • A.R. Simon, U. Rai, B.L. Fanburg, and B.H. Cochran Activation of the JAK-STAT pathway by reactive oxygen species Am. J. Physiol. 275 1998 C1640 1652
    • (1998) Am. J. Physiol. , vol.275 , pp. 1640-1652
    • Simon, A.R.1    Rai, U.2    Fanburg, B.L.3    Cochran, B.H.4
  • 19
    • 33846191009 scopus 로고    scopus 로고
    • Excessive nitric oxide attenuates leptin-mediated signal transducer and activator of transcription 3 activation
    • E.H. Jang, C.S. Park, S.K. Lee, J.E. Pie, and J.H. Kang Excessive nitric oxide attenuates leptin-mediated signal transducer and activator of transcription 3 activation Life Sci. 80 2007 609 617
    • (2007) Life Sci. , vol.80 , pp. 609-617
    • Jang, E.H.1    Park, C.S.2    Lee, S.K.3    Pie, J.E.4    Kang, J.H.5
  • 21
    • 0032526629 scopus 로고    scopus 로고
    • Macrophage-derived nitric oxide regulates T cell activation via reversible disruption of the Jak3/STAT5 signaling pathway
    • R.M. Bingisser, P.A. Tilbrook, P.G. Holt, and U.R. Kees Macrophage-derived nitric oxide regulates T cell activation via reversible disruption of the Jak3/STAT5 signaling pathway J. Immunol. 160 1998 5729 5734
    • (1998) J. Immunol. , vol.160 , pp. 5729-5734
    • Bingisser, R.M.1    Tilbrook, P.A.2    Holt, P.G.3    Kees, U.R.4
  • 23
    • 15244343041 scopus 로고    scopus 로고
    • Inducers of oxidative stress block ciliary neurotrophic factor activation of Jak/STAT signaling in neurons
    • N. Kaur, B. Lu, R.K. Monroe, S.M. Ward, and S.W. Halvorsen Inducers of oxidative stress block ciliary neurotrophic factor activation of Jak/STAT signaling in neurons J. Neurochem. 92 2005 1521 1530
    • (2005) J. Neurochem. , vol.92 , pp. 1521-1530
    • Kaur, N.1    Lu, B.2    Monroe, R.K.3    Ward, S.M.4    Halvorsen, S.W.5
  • 24
    • 33745849702 scopus 로고    scopus 로고
    • Cadmium blocks receptor-mediated Jak/STAT signaling in neurons by oxidative stress
    • R.K. Monroe, and S.W. Halvorsen Cadmium blocks receptor-mediated Jak/STAT signaling in neurons by oxidative stress Free Radic. Biol. Med. 41 2006 493 502
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 493-502
    • Monroe, R.K.1    Halvorsen, S.W.2
  • 25
    • 33745580391 scopus 로고    scopus 로고
    • Oxidative stress inhibits IFN-α-induced antiviral gene expression by blocking the JAK-STAT pathway
    • D. Di Bona, M. Cippitelli, C. Fionda, C. Camma, A. Licata, A. Santoni, and A. Craxi Oxidative stress inhibits IFN-α-induced antiviral gene expression by blocking the JAK-STAT pathway J. Hepatol. 45 2006 271 279
    • (2006) J. Hepatol. , vol.45 , pp. 271-279
    • Di Bona, D.1    Cippitelli, M.2    Fionda, C.3    Camma, C.4    Licata, A.5    Santoni, A.6    Craxi, A.7
  • 26
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: Revisiting PTPs and the control of cell signaling
    • N.K. Tonks Redox redux: revisiting PTPs and the control of cell signaling Cell 121 2005 667 670
    • (2005) Cell , vol.121 , pp. 667-670
    • Tonks, N.K.1
  • 27
    • 10644227929 scopus 로고    scopus 로고
    • Development of a modified in-gel assay to identify protein tyrosine phosphatases that are oxidized and inactivated in vivo
    • T.C. Meng, S.F. Hsu, and N.K. Tonks Development of a modified in-gel assay to identify protein tyrosine phosphatases that are oxidized and inactivated in vivo Methods 35 2005 28 36
    • (2005) Methods , vol.35 , pp. 28-36
    • Meng, T.C.1    Hsu, S.F.2    Tonks, N.K.3
  • 29
    • 0038749600 scopus 로고    scopus 로고
    • Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B
    • R.L. van Montfort, M. Congreve, D. Tisi, R. Carr, and H. Jhoti Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B Nature 423 2003 773 777
    • (2003) Nature , vol.423 , pp. 773-777
    • Van Montfort, R.L.1    Congreve, M.2    Tisi, D.3    Carr, R.4    Jhoti, H.5
  • 30
    • 37349100875 scopus 로고    scopus 로고
    • Multiple cysteine residues are implicated in Janus kinase 2-mediated catalysis
    • N.M. Mamoon, J.K. Smith, K. Chatti, S. Lee, K. Kundrapu, and R.J. Duhe Multiple cysteine residues are implicated in Janus kinase 2-mediated catalysis Biochemistry 46 2007 14810 14818
    • (2007) Biochemistry , vol.46 , pp. 14810-14818
    • Mamoon, N.M.1    Smith, J.K.2    Chatti, K.3    Lee, S.4    Kundrapu, K.5    Duhe, R.J.6
  • 32
    • 84862793895 scopus 로고
    • Prolactin and the secretion of insulin and glucagon by the pancreas
    • P.P. Foa, G. Galansino, and E. Costa Prolactin and the secretion of insulin and glucagon by the pancreas Am. J. Physiol. 182 1955 493 496
    • (1955) Am. J. Physiol. , vol.182 , pp. 493-496
    • Foa, P.P.1    Galansino, G.2    Costa, E.3
  • 33
    • 77049138622 scopus 로고
    • Effects of anterior pituitary extracts and of growth hormone preparations on the islets of Langerhans and the pancreas
    • B. Kinash, I. Macdougall, M.A. Evans, F.E. Bryans, and R.E. Haist Effects of anterior pituitary extracts and of growth hormone preparations on the islets of Langerhans and the pancreas Diabetes 2 1953 112 121
    • (1953) Diabetes , vol.2 , pp. 112-121
    • Kinash, B.1    MacDougall, I.2    Evans, M.A.3    Bryans, F.E.4    Haist, R.E.5
  • 34
    • 4344581494 scopus 로고    scopus 로고
    • Distinctive roles for prolactin and growth hormone in the activation of signal transducer and activator of transcription 5 in pancreatic islets of Langerhans
    • T.C. Brelje, L.E. Stout, N.V. Bhagroo, and R.L. Sorenson Distinctive roles for prolactin and growth hormone in the activation of signal transducer and activator of transcription 5 in pancreatic islets of Langerhans Endocrinology 145 2004 4162 4175
    • (2004) Endocrinology , vol.145 , pp. 4162-4175
    • Brelje, T.C.1    Stout, L.E.2    Bhagroo, N.V.3    Sorenson, R.L.4
  • 37
    • 33750865703 scopus 로고    scopus 로고
    • STAT5 activity in pancreatic β-cells influences the severity of diabetes in animal models of type 1 and 2 diabetes
    • M. Jackerott, A. Moldrup, P. Thams, E.D. Galsgaard, J. Knudsen, Y.C. Lee, and J.H. Nielsen STAT5 activity in pancreatic β-cells influences the severity of diabetes in animal models of type 1 and 2 diabetes Diabetes 55 2006 2705 2712
    • (2006) Diabetes , vol.55 , pp. 2705-2712
    • Jackerott, M.1    Moldrup, A.2    Thams, P.3    Galsgaard, E.D.4    Knudsen, J.5    Lee, Y.C.6    Nielsen, J.H.7
  • 38
    • 0842284799 scopus 로고    scopus 로고
    • β-Cell glucose toxicity, lipotoxicity, and chronic oxidative stress in type 2 diabetes
    • R.P. Robertson, J. Harmon, P.O. Tran, and V. Poitout β-Cell glucose toxicity, lipotoxicity, and chronic oxidative stress in type 2 diabetes Diabetes 53 Suppl. 1 2004 S119 124
    • (2004) Diabetes , vol.53 , Issue.SUPPL. 1 , pp. 119-124
    • Robertson, R.P.1    Harmon, J.2    Tran, P.O.3    Poitout, V.4
  • 39
    • 1842479256 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the Janus kinase 2 activation loop is essential for a high-activity catalytic state but dispensable for a basal catalytic state
    • K. Chatti, W.L. Farrar, and R.J. Duhe Tyrosine phosphorylation of the Janus kinase 2 activation loop is essential for a high-activity catalytic state but dispensable for a basal catalytic state Biochemistry 43 2004 4272 4283
    • (2004) Biochemistry , vol.43 , pp. 4272-4283
    • Chatti, K.1    Farrar, W.L.2    Duhe, R.J.3
  • 40
    • 0029086236 scopus 로고
    • Characterization of active and inactive forms of the JAK2 protein-tyrosine kinase produced via the baculovirus expression vector system
    • R.J. Duhe, and W.L. Farrar Characterization of active and inactive forms of the JAK2 protein-tyrosine kinase produced via the baculovirus expression vector system J. Biol. Chem. 270 1995 23084 23089
    • (1995) J. Biol. Chem. , vol.270 , pp. 23084-23089
    • Duhe, R.J.1    Farrar, W.L.2
  • 41
    • 0036327366 scopus 로고    scopus 로고
    • Characterization of the in vitro kinase activity of a partially purified soluble GST/JAK2 fusion protein
    • R.J. Duhe, E.A. Clark, and W.L. Farrar Characterization of the in vitro kinase activity of a partially purified soluble GST/JAK2 fusion protein Mol. Cell. Biochem. 236 2002 23 35
    • (2002) Mol. Cell. Biochem. , vol.236 , pp. 23-35
    • Duhe, R.J.1    Clark, E.A.2    Farrar, W.L.3
  • 42
    • 0028926254 scopus 로고
    • Morphological and functional characterization of β TC-6 cells-an insulin-secreting cell line derived from transgenic mice
    • V. Poitout, L.E. Stout, M.B. Armstrong, T.F. Walseth, R.L. Sorenson, and R.P. Robertson Morphological and functional characterization of β TC-6 cells-an insulin-secreting cell line derived from transgenic mice Diabetes 44 1995 306 313
    • (1995) Diabetes , vol.44 , pp. 306-313
    • Poitout, V.1    Stout, L.E.2    Armstrong, M.B.3    Walseth, T.F.4    Sorenson, R.L.5    Robertson, R.P.6
  • 43
    • 5644248079 scopus 로고    scopus 로고
    • Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet β cells in diabetes
    • R.P. Robertson Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet β cells in diabetes J. Biol. Chem. 279 2004 42351 42354
    • (2004) J. Biol. Chem. , vol.279 , pp. 42351-42354
    • Robertson, R.P.1
  • 44
    • 0028818886 scopus 로고
    • How do protein kinases discriminate between serine/threonine and tyrosine? Structural insights from the insulin receptor protein-tyrosine kinase
    • S.S. Taylor, E. Radzio-Andzelm, and T. Hunter How do protein kinases discriminate between serine/threonine and tyrosine? Structural insights from the insulin receptor protein-tyrosine kinase FASEB J. 9 1995 1255 1266
    • (1995) FASEB J. , vol.9 , pp. 1255-1266
    • Taylor, S.S.1    Radzio-Andzelm, E.2    Hunter, T.3
  • 45
    • 61349149899 scopus 로고    scopus 로고
    • Dissecting specificity in the Janus kinases: The structures of JAK-specific inhibitors complexed to the JAK1 and JAK2 protein tyrosine kinase domains
    • N.K. Williams, R.S. Bamert, O. Patel, C. Wang, P.M. Walden, A.F. Wilks, E. Fantino, J. Rossjohn, and I.S. Lucet Dissecting specificity in the Janus kinases: the structures of JAK-specific inhibitors complexed to the JAK1 and JAK2 protein tyrosine kinase domains J. Mol. Biol. 387 2009 219 232
    • (2009) J. Mol. Biol. , vol.387 , pp. 219-232
    • Williams, N.K.1    Bamert, R.S.2    Patel, O.3    Wang, C.4    Walden, P.M.5    Wilks, A.F.6    Fantino, E.7    Rossjohn, J.8    Lucet, I.S.9
  • 46
    • 34347374690 scopus 로고    scopus 로고
    • Evidence that IL-6-type cytokine signaling in cardiomyocytes is inhibited by oxidative stress: Parthenolide targets JAK1 activation by generating ROS
    • M. Kurdi, and G.W. Booz Evidence that IL-6-type cytokine signaling in cardiomyocytes is inhibited by oxidative stress: parthenolide targets JAK1 activation by generating ROS J. Cell. Physiol. 212 2007 424 431
    • (2007) J. Cell. Physiol. , vol.212 , pp. 424-431
    • Kurdi, M.1    Booz, G.W.2
  • 47
    • 0028823396 scopus 로고
    • A kinase-deficient splice variant of the human JAK3 is expressed in hematopoietic and epithelial cancer cells
    • K.S. Lai, Y. Jin, D.K. Graham, B.A. Witthuhn, J.N. Ihle, and E.T. Liu A kinase-deficient splice variant of the human JAK3 is expressed in hematopoietic and epithelial cancer cells J. Biol. Chem. 270 1995 25028 25036
    • (1995) J. Biol. Chem. , vol.270 , pp. 25028-25036
    • Lai, K.S.1    Jin, Y.2    Graham, D.K.3    Witthuhn, B.A.4    Ihle, J.N.5    Liu, E.T.6
  • 48
    • 46449110295 scopus 로고    scopus 로고
    • Thiol chemistry in peroxidase catalysis and redox signaling
    • A. Bindoli, J.M. Fukuto, and H.J. Forman Thiol chemistry in peroxidase catalysis and redox signaling Antioxid. Redox Signal. 10 2008 1549 1564
    • (2008) Antioxid. Redox Signal. , vol.10 , pp. 1549-1564
    • Bindoli, A.1    Fukuto, J.M.2    Forman, H.J.3
  • 49
    • 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
  • 50
    • 0029065402 scopus 로고
    • Thiol/disulfide exchange equilibria and disulfide bond stability
    • H.F. Gilbert Thiol/disulfide exchange equilibria and disulfide bond stability Methods Enzymol. 251 1995 8 28
    • (1995) Methods Enzymol. , vol.251 , pp. 8-28
    • Gilbert, H.F.1
  • 52
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • C. Hwang, A.J. Sinskey, and H.F. Lodish Oxidized redox state of glutathione in the endoplasmic reticulum Science 257 1992 1496 1502
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 53
    • 56549083161 scopus 로고    scopus 로고
    • A novel disulphide switch mechanism in Ero1α balances ER oxidation in human cells
    • C. Appenzeller-Herzog, J. Riemer, B. Christensen, E.S. Sorensen, and L. Ellgaard A novel disulphide switch mechanism in Ero1α balances ER oxidation in human cells EMBO J. 27 2008 2977 2987
    • (2008) EMBO J. , vol.27 , pp. 2977-2987
    • Appenzeller-Herzog, C.1    Riemer, J.2    Christensen, B.3    Sorensen, E.S.4    Ellgaard, L.5
  • 54
    • 9944235916 scopus 로고    scopus 로고
    • The role of cysteine residues as redox-sensitive regulatory switches
    • D. Barford The role of cysteine residues as redox-sensitive regulatory switches Curr. Opin. Struct. Biol. 14 2004 679 686
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 679-686
    • Barford, D.1
  • 55
    • 0020395140 scopus 로고
    • Biological disulfides: The third messenger? Modulation of phosphofructokinase activity by thiol/disulfide exchange
    • H.F. Gilbert Biological disulfides: the third messenger? Modulation of phosphofructokinase activity by thiol/disulfide exchange J. Biol. Chem. 257 1982 12086 12091
    • (1982) J. Biol. Chem. , vol.257 , pp. 12086-12091
    • Gilbert, H.F.1
  • 57
    • 11144221439 scopus 로고    scopus 로고
    • Widespread sulfenic acid formation in tissues in response to hydrogen peroxide
    • A.T. Saurin, H. Neubert, J.P. Brennan, and P. Eaton Widespread sulfenic acid formation in tissues in response to hydrogen peroxide Proc. Natl. Acad. Sci. U. S. A. 101 2004 17982 17987
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 17982-17987
    • Saurin, A.T.1    Neubert, H.2    Brennan, J.P.3    Eaton, P.4
  • 58
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte, and R.F. Doolittle A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157 1982 105 132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 60
    • 0035970286 scopus 로고    scopus 로고
    • Distinct cysteine sulfhydryl environments detected by analysis of Raman S-hh markers of Cys→Ser mutant proteins
    • S.W. Raso, P.L. Clark, C. Haase-Pettingell, J. King, and G.J. Thomas Jr. Distinct cysteine sulfhydryl environments detected by analysis of Raman S-hh markers of Cys→Ser mutant proteins J. Mol. Biol. 307 2001 899 911
    • (2001) J. Mol. Biol. , vol.307 , pp. 899-911
    • Raso, S.W.1    Clark, P.L.2    Haase-Pettingell, C.3    King, J.4    Thomas Jr., G.J.5
  • 61
    • 70349482669 scopus 로고    scopus 로고
    • Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies
    • Y.H. Seo, and K.S. Carroll Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies Proc. Natl. Acad. Sci. U. S. A. 106 2009 16163 16168
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 16163-16168
    • Seo, Y.H.1    Carroll, K.S.2
  • 62
    • 0027131771 scopus 로고
    • Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation
    • A. Claiborne, H. Miller, D. Parsonage, and R.P. Ross Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation FASEB J. 7 1993 1483 1490
    • (1993) FASEB J. , vol.7 , pp. 1483-1490
    • Claiborne, A.1    Miller, H.2    Parsonage, D.3    Ross, R.P.4
  • 63
    • 77956140082 scopus 로고    scopus 로고
    • Cysteine sulfenic acid as an intermediate in disulfide bond formation and nonenzymatic protein folding
    • D.S. Rehder, and C.R. Borges Cysteine sulfenic acid as an intermediate in disulfide bond formation and nonenzymatic protein folding Biochemistry 49 2010 7748 7755
    • (2010) Biochemistry , vol.49 , pp. 7748-7755
    • Rehder, D.S.1    Borges, C.R.2
  • 64
    • 0027439438 scopus 로고
    • The conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATP
    • A.C. Carrera, K. Alexandrov, and T.M. Roberts The conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATP Proc. Natl. Acad. Sci. U. S. A. 90 1993 442 446
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 442-446
    • Carrera, A.C.1    Alexandrov, K.2    Roberts, T.M.3
  • 65
    • 0030953469 scopus 로고    scopus 로고
    • Activation of Jak2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop
    • J. Feng, B.A. Witthuhn, T. Matsuda, F. Kohlhuber, I.M. Kerr, and J.N. Ihle Activation of Jak2 catalytic activity requires phosphorylation of Y1007 in the kinase activation loop Mol. Cell. Biol. 17 1997 2497 2501
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2497-2501
    • Feng, J.1    Witthuhn, B.A.2    Matsuda, T.3    Kohlhuber, F.4    Kerr, I.M.5    Ihle, J.N.6


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