메뉴 건너뛰기




Volumn 288, Issue 37, 2013, Pages 26480-26488

The redox biochemistry of protein sulfenylation and sulfinylation

Author keywords

[No Author keywords available]

Indexed keywords

ACID MODIFICATION; CELLULAR TARGETS; OXIDATION STATE; POST-TRANSLATIONAL MODIFICATIONS; PROTEIN FUNCTIONS; REACTIVE OXYGEN SPECIES; SIGNALING EVENTS; SULFENYLATION;

EID: 84883674898     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R113.467738     Document Type: Review
Times cited : (257)

References (100)
  • 1
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • Finkel, T. (2011) Signal transduction by reactive oxygen species. J. Cell Biol. 194, 7-15
    • (2011) J. Cell Biol. , vol.194 , pp. 7-15
    • Finkel, T.1
  • 2
    • 77956171017 scopus 로고    scopus 로고
    • Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization
    • Hall, A., Parsonage, D., Poole, L. B., and Karplus, P. A. (2010) Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization. J. Mol. Biol. 402, 194-209
    • (2010) J. Mol. Biol. , vol.402 , pp. 194-209
    • Hall, A.1    Parsonage, D.2    Poole, L.B.3    Karplus, P.A.4
  • 4
    • 84868206533 scopus 로고    scopus 로고
    • Understanding the pKa of redox cysteines: The key role of hydrogen bonding
    • Roos, G., Foloppe, N., and Messens, J. (2013) Understanding the pKa of redox cysteines: the key role of hydrogen bonding. Antioxid. Redox Signal. 18, 94-127
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 94-127
    • Roos, G.1    Foloppe, N.2    Messens, J.3
  • 5
    • 46249108461 scopus 로고    scopus 로고
    • Regulation of ROS signal transduction byNADPHoxidase 4 localization
    • Chen, K., Kirber, M. T., Xiao, H., Yang, Y., and Keaney, J. F. (2008) Regulation of ROS signal transduction byNADPHoxidase 4 localization. J. Cell Biol. 181, 1129-1139
    • (2008) J. Cell Biol. , vol.181 , pp. 1129-1139
    • Chen, K.1    Kirber, M.T.2    Xiao, H.3    Yang, Y.4    Keaney, J.F.5
  • 7
    • 70350050576 scopus 로고    scopus 로고
    • Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: Kinetics, acidity constants, and conformational dynamics
    • Hugo, M., Turell, L., Manta, B., Botti, H., Monteiro, G., Netto, L. E. S., Alvarez, B., Radi, R., and Trujillo, M. (2009) Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: kinetics, acidity constants, and conformational dynamics. Biochemistry 48, 9416-9426
    • (2009) Biochemistry , vol.48 , pp. 9416-9426
    • Hugo, M.1    Turell, L.2    Manta, B.3    Botti, H.4    Monteiro, G.5    Netto, L.E.S.6    Alvarez, B.7    Radi, R.8    Trujillo, M.9
  • 9
    • 67650292926 scopus 로고    scopus 로고
    • Simultaneous detection of cysteine sulfenate, sulfinate, and sulfonate during cysteine interfacial ozonolysis
    • Enami, S., Hoffmann, M. R., and Colussi, A. J. (2009) Simultaneous detection of cysteine sulfenate, sulfinate, and sulfonate during cysteine interfacial ozonolysis. J. Phys. Chem. B 113, 9356-9358
    • (2009) J. Phys. Chem. B , vol.113 , pp. 9356-9358
    • Enami, S.1    Hoffmann, M.R.2    Colussi, A.J.3
  • 11
    • 0000910788 scopus 로고
    • Chemistry of sulfenic acids. 7. Reason for the high reactivity of sulfenic acids. Stabilization by intramolecular hydrogen-bonding and electronegativity effects
    • Davis, F. A., Jenkins, L. A., and Billmers, R. L. (1986) Chemistry of sulfenic acids. 7. Reason for the high reactivity of sulfenic acids. Stabilization by intramolecular hydrogen-bonding and electronegativity effects. J. Org. Chem. 51, 1033-1040
    • (1986) J. Org. Chem. , vol.51 , pp. 1033-1040
    • Davis, F.A.1    Jenkins, L.A.2    Billmers, R.L.3
  • 12
    • 77956140082 scopus 로고    scopus 로고
    • Cysteine sulfenic acid as an intermediate in disulfide bond formation and nonenzymatic protein folding
    • Rehder, D. S., and Borges, C. R. (2010) Cysteine sulfenic acid as an intermediate in disulfide bond formation and nonenzymatic protein folding. Biochemistry 49, 7748-7755
    • (2010) Biochemistry , vol.49 , pp. 7748-7755
    • Rehder, D.S.1    Borges, C.R.2
  • 13
    • 34547399134 scopus 로고    scopus 로고
    • A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR
    • Lee, J. W., Soonsanga, S., and Helmann, J. D. (2007) A complex thiolate switch regulates the Bacillus subtilis organic peroxide sensor OhrR. Proc. Natl. Acad. Sci. U.S.A. 104, 8743-8748
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 8743-8748
    • Lee, J.W.1    Soonsanga, S.2    Helmann, J.D.3
  • 14
    • 0038411479 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
    • Salmeen, A., Andersen, J. N., Myers, M. P., Meng, T. C., Hinks, J. A., Tonks, N. K., and Barford, D. (2003) Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate. Nature 423, 769-773
    • (2003) Nature , vol.423 , pp. 769-773
    • Salmeen, A.1    Andersen, J.N.2    Myers, M.P.3    Meng, T.C.4    Hinks, J.A.5    Tonks, N.K.6    Barford, D.7
  • 15
    • 0001637467 scopus 로고
    • Formation and reactions of sulfenic acids in proteins
    • Allison, W. S. (1976) Formation and reactions of sulfenic acids in proteins. Acc. Chem. Res. 9, 293-299
    • (1976) Acc. Chem. Res. , vol.9 , pp. 293-299
    • Allison, W.S.1
  • 16
    • 38649084667 scopus 로고    scopus 로고
    • Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid
    • Salsbury, F. R., Jr., Knutson, S. T., Poole, L. B., and Fetrow, J. S. (2008) Functional site profiling and electrostatic analysis of cysteines modifiable to cysteine sulfenic acid. Protein Sci. 17, 299-312
    • (2008) Protein Sci. , vol.17 , pp. 299-312
    • Salsbury Jr., F.R.1    Knutson, S.T.2    Poole, L.B.3    Fetrow, J.S.4
  • 17
    • 79851510345 scopus 로고    scopus 로고
    • Chemical "omics" approaches for understanding protein cysteine oxidation in biology
    • Leonard, S. E., and Carroll, K. S. (2011) Chemical "omics" approaches for understanding protein cysteine oxidation in biology. Curr. Opin. Chem. Biol. 15, 88-102
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 88-102
    • Leonard, S.E.1    Carroll, K.S.2
  • 19
    • 70349284540 scopus 로고    scopus 로고
    • Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells
    • Leonard, S. E., Reddie, K. G., and Carroll, K. S. (2009) Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells. ACS Chem. Biol. 4, 783-799
    • (2009) ACS Chem. Biol. , vol.4 , pp. 783-799
    • Leonard, S.E.1    Reddie, K.G.2    Carroll, K.S.3
  • 20
    • 79958198412 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatases: Structural and chemical aspects
    • Tanner, J. J., Parsons, Z. D., Cummings, A. H., Zhou, H., and Gates, K. S. (2011) Redox regulation of protein tyrosine phosphatases: structural and chemical aspects. Antioxid. Redox Signal. 15, 77-97
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 77-97
    • Tanner, J.J.1    Parsons, Z.D.2    Cummings, A.H.3    Zhou, H.4    Gates, K.S.5
  • 21
    • 0037036358 scopus 로고    scopus 로고
    • Reversible inactivation of the tumor suppressor PTEN by H2O2
    • Lee, S. R., Yang, K. S., Kwon, J., Lee, C., Jeong, W., and Rhee, S. G. (2002) Reversible inactivation of the tumor suppressor PTEN by H2O2. J. Biol. Chem. 277, 20336-20342
    • (2002) J. Biol. Chem. , vol.277 , pp. 20336-20342
    • Lee, S.R.1    Yang, K.S.2    Kwon, J.3    Lee, C.4    Jeong, W.5    Rhee, S.G.6
  • 22
    • 64349117191 scopus 로고    scopus 로고
    • Redox regulation of SH2-domain-containing protein tyrosine phosphatases by two backdoor cysteines
    • Chen, C. Y., Willard, D., and Rudolph, J. (2009) Redox regulation of SH2-domain-containing protein tyrosine phosphatases by two backdoor cysteines. Biochemistry 48, 1399-1409
    • (2009) Biochemistry , vol.48 , pp. 1399-1409
    • Chen, C.Y.1    Willard, D.2    Rudolph, J.3
  • 23
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • Meng, T. C., Fukada, T., and Tonks, N. K. (2002) Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell 9, 387-399
    • (2002) Mol. Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 24
    • 22744444805 scopus 로고    scopus 로고
    • Receptor-stimulated oxidation of SHP-2 promotes T-cell adhesion through SLP-76-ADAP
    • Kwon, J., Qu, C. K., Maeng, J. S., Falahati, R., Lee, C., and Williams, M. S. (2005) Receptor-stimulated oxidation of SHP-2 promotes T-cell adhesion through SLP-76-ADAP. EMBO J. 24, 2331-2341
    • (2005) EMBO J , vol.24 , pp. 2331-2341
    • Kwon, J.1    Qu, C.K.2    Maeng, J.S.3    Falahati, R.4    Lee, C.5    Williams, M.S.6
  • 26
    • 22544453858 scopus 로고    scopus 로고
    • Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth
    • Giannoni, E., Buricchi, F., Raugei, G., Ramponi, G., and Chiarugi, P. (2005) Intracellular reactive oxygen species activate Src tyrosine kinase during cell adhesion and anchorage-dependent cell growth. Mol. Cell. Biol. 25, 6391-6403
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6391-6403
    • Giannoni, E.1    Buricchi, F.2    Raugei, G.3    Ramponi, G.4    Chiarugi, P.5
  • 29
    • 0346749513 scopus 로고    scopus 로고
    • Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt
    • Murata, H., Ihara, Y., Nakamura, H., Yodoi, J., Sumikawa, K., and Kondo, T. (2003) Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt. J. Biol. Chem. 278, 50226-50233
    • (2003) J. Biol. Chem. , vol.278 , pp. 50226-50233
    • Murata, H.1    Ihara, Y.2    Nakamura, H.3    Yodoi, J.4    Sumikawa, K.5    Kondo, T.6
  • 30
    • 79954504166 scopus 로고    scopus 로고
    • Basic principles and emerging concepts in the redox control of transcription factors
    • Brigelius-Flohé, R., and Flohé, L. (2011) Basic principles and emerging concepts in the redox control of transcription factors. Antioxid. Redox Signal. 15, 2335-2381
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 2335-2381
    • Brigelius-Flohé, R.1    Flohé, L.2
  • 31
  • 32
    • 33750230997 scopus 로고    scopus 로고
    • An oxidation-sensing mechanism is used by the global regulator MgrA in Staphylococcus aureus
    • Chen, P. R., Bae, T., Williams, W. A., Duguid, E. M., Rice, P. A., Schneewind, O., and He, C. (2006) An oxidation-sensing mechanism is used by the global regulator MgrA in Staphylococcus aureus. Nat. Chem. Biol. 2, 591-595
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 591-595
    • Chen, P.R.1    Bae, T.2    Williams, W.A.3    Duguid, E.M.4    Rice, P.A.5    Schneewind, O.6    He, C.7
  • 33
    • 84864824413 scopus 로고    scopus 로고
    • Activity of the tetrapyrrole regulator CrtJ is controlled by oxidation of a redox active cysteine located in the DNA binding domain
    • Cheng, Z., Wu, J., Setterdahl, A., Reddie, K., Carroll, K., Hammad, L. A., Karty, J. A., and Bauer, C. E. (2012) Activity of the tetrapyrrole regulator CrtJ is controlled by oxidation of a redox active cysteine located in the DNA binding domain. Mol. Microbiol. 85, 734-746
    • (2012) Mol. Microbiol. , vol.85 , pp. 734-746
    • Cheng, Z.1    Wu, J.2    Setterdahl, A.3    Reddie, K.4    Carroll, K.5    Hammad, L.A.6    Karty, J.A.7    Bauer, C.E.8
  • 34
    • 0037076330 scopus 로고    scopus 로고
    • The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative
    • Fuangthong, M., and Helmann, J. D. (2002) The OhrR repressor senses organic hydroperoxides by reversible formation of a cysteine-sulfenic acid derivative. Proc. Natl. Acad. Sci. U.S.A. 99, 6690-6695
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 6690-6695
    • Fuangthong, M.1    Helmann, J.D.2
  • 35
    • 79551673521 scopus 로고    scopus 로고
    • Vibrio cholerae anaerobic induction of virulence gene expression is controlled by thiol-based switches of virulence regulator AphB
    • Liu, Z., Yang, M., Peterfreund, G. L., Tsou, A. M., Selamoglu, N., Daldal, F., Zhong, Z., Kan, B., and Zhu, J. (2011) Vibrio cholerae anaerobic induction of virulence gene expression is controlled by thiol-based switches of virulence regulator AphB. Proc. Natl. Acad. Sci. U.S.A. 108, 810-815
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 810-815
    • Liu, Z.1    Yang, M.2    Peterfreund, G.L.3    Tsou, A.M.4    Selamoglu, N.5    Daldal, F.6    Zhong, Z.7    Kan, B.8    Zhu, J.9
  • 36
    • 69949138465 scopus 로고    scopus 로고
    • Crystal structures of the reduced, sulfenic acid, and mixed disulfide forms of SarZ, a redox active global regulator in Staphylococcus aureus
    • Poor, C. B., Chen, P. R., Duguid, E., Rice, P. A., and He, C. (2009) Crystal structures of the reduced, sulfenic acid, and mixed disulfide forms of SarZ, a redox active global regulator in Staphylococcus aureus. J. Biol. Chem. 284, 23517-23524
    • (2009) J. Biol. Chem. , vol.284 , pp. 23517-23524
    • Poor, C.B.1    Chen, P.R.2    Duguid, E.3    Rice, P.A.4    He, C.5
  • 37
    • 0037110454 scopus 로고    scopus 로고
    • A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation
    • Delaunay, A., Pflieger, D., Barrault, M. B., Vinh, J., and Toledano, M. B. (2002) A thiol peroxidase is an H2O2 receptor and redox-transducer in gene activation. Cell 111, 471-481
    • (2002) Cell , vol.111 , pp. 471-481
    • Delaunay, A.1    Pflieger, D.2    Barrault, M.B.3    Vinh, J.4    Toledano, M.B.5
  • 38
    • 60549093028 scopus 로고    scopus 로고
    • Chemical dissection of an essential redox switch in yeast
    • Paulsen, C. E., and Carroll, K. S. (2009) Chemical dissection of an essential redox switch in yeast. Chem. Biol. 16, 217-225
    • (2009) Chem. Biol. , vol.16 , pp. 217-225
    • Paulsen, C.E.1    Carroll, K.S.2
  • 39
    • 77950887186 scopus 로고    scopus 로고
    • Activation of NRF2 by nitrosative agents and H2O2 involves KEAP1 disulfide formation
    • Fourquet, S., Guerois, R., Biard, D., and Toledano, M. B. (2010) Activation of NRF2 by nitrosative agents and H2O2 involves KEAP1 disulfide formation. J. Biol. Chem. 285, 8463-8471
    • (2010) J. Biol. Chem. , vol.285 , pp. 8463-8471
    • Fourquet, S.1    Guerois, R.2    Biard, D.3    Toledano, M.B.4
  • 45
    • 84875912087 scopus 로고    scopus 로고
    • Reversible inactivation of deubiquitinases by reactive oxygen species in vitro and in cells
    • Lee, J. G., Baek, K., Soetandyo, N., and Ye, Y. (2013) Reversible inactivation of deubiquitinases by reactive oxygen species in vitro and in cells. Nat. Commun. 4, 1568
    • (2013) Nat. Commun. , vol.4 , pp. 1568
    • Lee, J.G.1    Baek, K.2    Soetandyo, N.3    Ye, Y.4
  • 46
    • 38049185042 scopus 로고    scopus 로고
    • Molecular basis of the redox regulation of SUMO proteases: A protective mechanism of intermolecular disulfide linkage against irreversible sulfhydryl oxidation
    • Xu, Z., Lam, L. S., Lam, L. H., Chau, S. F., Ng, T. B., and Au, S. W. (2008) Molecular basis of the redox regulation of SUMO proteases: a protective mechanism of intermolecular disulfide linkage against irreversible sulfhydryl oxidation. FASEB J. 22, 127-137
    • (2008) FASEB J , vol.22 , pp. 127-137
    • Xu, Z.1    Lam, L.S.2    Lam, L.H.3    Chau, S.F.4    Ng, T.B.5    Au, S.W.6
  • 47
    • 31544432283 scopus 로고    scopus 로고
    • Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes
    • Bossis, G., and Melchior, F. (2006) Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes. Mol. Cell 21, 349-357
    • (2006) Mol. Cell , vol.21 , pp. 349-357
    • Bossis, G.1    Melchior, F.2
  • 48
    • 79961185085 scopus 로고    scopus 로고
    • Role of reactive oxygen species and redox in regulating the function of transient receptor potential channels
    • Song, M. Y., Makino, A., and Yuan, J. X. (2011) Role of reactive oxygen species and redox in regulating the function of transient receptor potential channels. Antioxid. Redox Signal. 15, 1549-1565
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 1549-1565
    • Song, M.Y.1    Makino, A.2    Yuan, J.X.3
  • 52
    • 0041323072 scopus 로고    scopus 로고
    • Catalytic and chemical competence of regulation of Cdc25 phosphatase by oxidation/reduction
    • Sohn, J., and Rudolph, J. (2003) Catalytic and chemical competence of regulation of Cdc25 phosphatase by oxidation/reduction. Biochemistry 42, 10060-10070
    • (2003) Biochemistry , vol.42 , pp. 10060-10070
    • Sohn, J.1    Rudolph, J.2
  • 53
    • 57549095616 scopus 로고    scopus 로고
    • Expanding the functional diversity of proteins through cysteine oxidation
    • Reddie, K. G., and Carroll, K. S. (2008) Expanding the functional diversity of proteins through cysteine oxidation. Curr. Opin. Chem. Biol. 12, 746-754
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , pp. 746-754
    • Reddie, K.G.1    Carroll, K.S.2
  • 54
    • 79958199102 scopus 로고    scopus 로고
    • The role of cysteine oxidation in DJ-1 function and dysfunction
    • Wilson, M. A. (2011) The role of cysteine oxidation in DJ-1 function and dysfunction. Antioxid. Redox Signal. 15, 111-122
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 111-122
    • Wilson, M.A.1
  • 55
    • 0036363570 scopus 로고    scopus 로고
    • Quantitation of protein sulfinic and sulfonic acid, irreversibly oxidized protein cysteine sites in cellular proteins
    • Hamann, M., Zhang, T., Hendrich, S., and Thomas, J. A. (2002) Quantitation of protein sulfinic and sulfonic acid, irreversibly oxidized protein cysteine sites in cellular proteins. Methods Enzymol. 348, 146-156
    • (2002) Methods Enzymol. , vol.348 , pp. 146-156
    • Hamann, M.1    Zhang, T.2    Hendrich, S.3    Thomas, J.A.4
  • 56
    • 3843064487 scopus 로고    scopus 로고
    • The sulfinic acid switch in proteins
    • Jacob, C., Holme, A. L., and Fry, F. H. (2004) The sulfinic acid switch in proteins. Org. Biomol. Chem. 2, 1953-1956
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 1953-1956
    • Jacob, C.1    Holme, A.L.2    Fry, F.H.3
  • 58
    • 84862692522 scopus 로고    scopus 로고
    • Chemoselective ligation of sulfinic acids with aryl-nitroso compounds
    • Lo Conte, M., and Carroll, K. S. (2012) Chemoselective ligation of sulfinic acids with aryl-nitroso compounds. Angew. Chem. Int. Ed. Engl. 51, 6502-6505
    • (2012) Angew. Chem. Int. Ed. Engl. , vol.51 , pp. 6502-6505
    • Lo Conte, M.1    Carroll, K.S.2
  • 59
    • 17644390613 scopus 로고    scopus 로고
    • Controlled elimination of intracellular H2O2: Regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification
    • Rhee, S. G., Yang, K. S., Kang, S. W., Woo, H. A., and Chang, T. S. (2005) Controlled elimination of intracellular H2O2: regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification. Antioxid. Redox Signal. 7, 619-626
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 619-626
    • Rhee, S.G.1    Yang, K.S.2    Kang, S.W.3    Woo, H.A.4    Chang, T.S.5
  • 60
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Wood, Z. A., Poole, L. B., and Karplus, P. A. (2003) Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling. Science 300, 650-653
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 62
    • 0037064080 scopus 로고    scopus 로고
    • Inactivation of human peroxiredoxin i during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid
    • Yang, K. S., Kang, S. W., Woo, H. A., Hwang, S. C., Chae, H. Z., Kim, K., and Rhee, S. G. (2002) Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. J. Biol. Chem. 277, 38029-38036
    • (2002) J. Biol. Chem. , vol.277 , pp. 38029-38036
    • Yang, K.S.1    Kang, S.W.2    Woo, H.A.3    Hwang, S.C.4    Chae, H.Z.5    Kim, K.6    Rhee, S.G.7
  • 63
    • 84877886960 scopus 로고    scopus 로고
    • Hyperoxidation of peroxiredoxins 2 and 3. Rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine
    • Peskin, A. V., Dickerhof, N., Poynton, R. A., Paton, L. N., Pace, P. E., Hampton, M. B., and Winterbourn, C. C. (2013) Hyperoxidation of peroxiredoxins 2 and 3. Rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine. J. Biol. Chem. 288, 14170-14177
    • (2013) J. Biol. Chem. , vol.288 , pp. 14170-14177
    • Peskin, A.V.1    Dickerhof, N.2    Poynton, R.A.3    Paton, L.N.4    Pace, P.E.5    Hampton, M.B.6    Winterbourn, C.C.7
  • 64
    • 79251550085 scopus 로고    scopus 로고
    • Reduction of cysteine sulfinic acid in eukaryotic, typical 2-Cys peroxiredoxins by sulfiredoxin
    • Lowther, W. T., and Haynes, A. C. (2011) Reduction of cysteine sulfinic acid in eukaryotic, typical 2-Cys peroxiredoxins by sulfiredoxin. Antioxid. Redox Signal. 15, 99-109
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 99-109
    • Lowther, W.T.1    Haynes, A.C.2
  • 65
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. Crevisiae sulphiredoxin
    • Biteau, B., Labarre, J., and Toledano, M. B. (2003) ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425, 980-984
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 69
    • 65249159732 scopus 로고    scopus 로고
    • Formation of a stabilized cysteine sulfinic acid is critical for the mitochondrial function of the parkinsonism protein DJ-1
    • Blackinton, J., Lakshminarasimhan, M., Thomas, K. J., Ahmad, R., Greggio, E., Raza, A. S., Cookson, M. R., and Wilson, M. A. (2009) Formation of a stabilized cysteine sulfinic acid is critical for the mitochondrial function of the parkinsonism protein DJ-1. J. Biol. Chem. 284, 6476-6485
    • (2009) J. Biol. Chem. , vol.284 , pp. 6476-6485
    • Blackinton, J.1    Lakshminarasimhan, M.2    Thomas, K.J.3    Ahmad, R.4    Greggio, E.5    Raza, A.S.6    Cookson, M.R.7    Wilson, M.A.8
  • 70
    • 67649771389 scopus 로고    scopus 로고
    • Oxidizable residues mediating protein stability and cytoprotective interaction of DJ-1 with apoptosis signal-regulating kinase 1
    • Waak, J., Weber, S. S., Görner, K., Schall, C., Ichijo, H., Stehle, T., and Kahle, P. J. (2009) Oxidizable residues mediating protein stability and cytoprotective interaction of DJ-1 with apoptosis signal-regulating kinase 1. J. Biol. Chem. 284, 14245-14257
    • (2009) J. Biol. Chem. , vol.284 , pp. 14245-14257
    • Waak, J.1    Weber, S.S.2    Görner, K.3    Schall, C.4    Ichijo, H.5    Stehle, T.6    Kahle, P.J.7
  • 71
    • 33750901634 scopus 로고    scopus 로고
    • Zinc coordination environments in proteins as redox sensors and signal transducers
    • Maret, W. (2006) Zinc coordination environments in proteins as redox sensors and signal transducers. Antioxid. Redox Signal. 8, 1419-1441
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 1419-1441
    • Maret, W.1
  • 72
    • 0035798684 scopus 로고    scopus 로고
    • Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase
    • Fu, X., Kassim, S. Y., Parks, W. C., and Heinecke, J. W. (2001) Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase. J. Biol. Chem. 276, 41279-41287
    • (2001) J. Biol. Chem. , vol.276 , pp. 41279-41287
    • Fu, X.1    Kassim, S.Y.2    Parks, W.C.3    Heinecke, J.W.4
  • 73
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases- structure, function, and biochemistry
    • Visse, R., and Nagase, H. (2003) Matrix metalloproteinases and tissue inhibitors of metalloproteinases-structure, function, and biochemistry. Circ. Res. 92, 827-839
    • (2003) Circ. Res. , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 75
    • 49149116129 scopus 로고    scopus 로고
    • Structural and functional model systems for analysis of the active center of nitrile hydratase
    • Yano, T., Ozawa, T., and Masuda, H. (2008) Structural and functional model systems for analysis of the active center of nitrile hydratase. Chem. Lett. 37, 672-677
    • (2008) Chem. Lett. , vol.37 , pp. 672-677
    • Yano, T.1    Ozawa, T.2    Masuda, H.3
  • 77
    • 70350043513 scopus 로고    scopus 로고
    • Structural basis for catalytic activation of thiocyanate hydrolase involving metal-ligated cysteine modification
    • Arakawa, T., Kawano, Y., Katayama, Y., Nakayama, H., Dohmae, N., Yohda, M., and Odaka, M. (2009) Structural basis for catalytic activation of thiocyanate hydrolase involving metal-ligated cysteine modification. J. Am. Chem. Soc. 131, 14838-14843
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 14838-14843
    • Arakawa, T.1    Kawano, Y.2    Katayama, Y.3    Nakayama, H.4    Dohmae, N.5    Yohda, M.6    Odaka, M.7
  • 79
    • 84871309537 scopus 로고    scopus 로고
    • Redox regulation of epidermal growth factor receptor signaling through cysteine oxidation
    • Truong, T. H., and Carroll, K. S. (2012) Redox regulation of epidermal growth factor receptor signaling through cysteine oxidation. Biochemistry 51, 9954-9965
    • (2012) Biochemistry , vol.51 , pp. 9954-9965
    • Truong, T.H.1    Carroll, K.S.2
  • 81
    • 57749089406 scopus 로고    scopus 로고
    • Facile synthesis and biological evaluation of a cell-permeable probe to detect redox-regulated proteins
    • Seo, Y. H., and Carroll, K. S. (2009) Facile synthesis and biological evaluation of a cell-permeable probe to detect redox-regulated proteins. Bioorg. Med. Chem. Lett. 19, 356-359
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 356-359
    • Seo, Y.H.1    Carroll, K.S.2
  • 83
    • 70349482669 scopus 로고    scopus 로고
    • Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies
    • Seo, Y. H., and Carroll, K. S. (2009) Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies. Proc. Natl. Acad. Sci. U.S.A. 106, 16163-16168
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16163-16168
    • Seo, Y.H.1    Carroll, K.S.2
  • 84
    • 84864778316 scopus 로고    scopus 로고
    • The reversible formation of cysteine sulfenic acid promotes B-cell activation and proliferation
    • Crump, K. E., Juneau, D. G., Poole, L. B., Haas, K. M., and Grayson, J. M. (2012) The reversible formation of cysteine sulfenic acid promotes B-cell activation and proliferation. Eur. J. Immunol. 42, 2152-2164
    • (2012) Eur. J. Immunol. , vol.42 , pp. 2152-2164
    • Crump, K.E.1    Juneau, D.G.2    Poole, L.B.3    Haas, K.M.4    Grayson, J.M.5
  • 85
    • 84874102375 scopus 로고    scopus 로고
    • RegB kinase activity is repressed by oxidative formation of cysteine sulfenic acid
    • Wu, J., Cheng, Z., Reddie, K., Carroll, K., Hammad, L. A., Karty, J. A., and Bauer, C. E. (2013) RegB kinase activity is repressed by oxidative formation of cysteine sulfenic acid. J. Biol. Chem. 288, 4755-4762
    • (2013) J. Biol. Chem. , vol.288 , pp. 4755-4762
    • Wu, J.1    Cheng, Z.2    Reddie, K.3    Carroll, K.4    Hammad, L.A.5    Karty, J.A.6    Bauer, C.E.7
  • 86
    • 84856215059 scopus 로고    scopus 로고
    • Plastidic phosphoglycerate kinase from Phaeodactylum tricornutum: On the critical role of cysteine residues for the enzyme function
    • Bosco, M. B., Aleanzi, M. C., and Iglesias, A. Á. (2012) Plastidic phosphoglycerate kinase from Phaeodactylum tricornutum: on the critical role of cysteine residues for the enzyme function. Protist 163, 188-203
    • (2012) Protist , vol.163 , pp. 188-203
    • Bosco, M.B.1    Aleanzi, M.C.2    Iglesias, A.Á.3
  • 87
    • 84872767045 scopus 로고    scopus 로고
    • Energetic coupling between an oxidizable cysteine and the phosphorylatable N-terminus of human liver pyruvate kinase
    • Holyoak, T., Zhang, B., Deng, J., Tang, Q., Prasannan, C. B., and Fenton, A. W. (2013) Energetic coupling between an oxidizable cysteine and the phosphorylatable N-terminus of human liver pyruvate kinase. Biochemistry 52, 466-476
    • (2013) Biochemistry , vol.52 , pp. 466-476
    • Holyoak, T.1    Zhang, B.2    Deng, J.3    Tang, Q.4    Prasannan, C.B.5    Fenton, A.W.6
  • 88
    • 11144221439 scopus 로고    scopus 로고
    • Widespread sulfenic acid formation in tissues in response to hydrogen peroxide
    • Saurin, A. T., Neubert, H., Brennan, J. P., and Eaton, P. (2004) Widespread sulfenic acid formation in tissues in response to hydrogen peroxide. Proc. Natl. Acad. Sci. U.S.A. 101, 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
  • 90
    • 77956205147 scopus 로고    scopus 로고
    • Postischemic deactivation of cardiac aldose reductase. Role of glutathione S-transferase P and glutaredoxin in regeneration of reduced thiols from sulfenic acids
    • Wetzelberger, K., Baba, S. P., Thirunavukkarasu, M., Ho, Y. S., Maulik, N., Barski, O. A., Conklin, D. J., and Bhatnagar, A. (2010) Postischemic deactivation of cardiac aldose reductase. Role of glutathione S-transferase P and glutaredoxin in regeneration of reduced thiols from sulfenic acids. J. Biol. Chem. 285, 26135-26148
    • (2010) J. Biol. Chem. , vol.285 , pp. 26135-26148
    • Wetzelberger, K.1    Baba, S.P.2    Thirunavukkarasu, M.3    Ho, Y.S.4    Maulik, N.5    Barski, O.A.6    Conklin, D.J.7    Bhatnagar, A.8
  • 91
    • 79960604985 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase A is a stereospecific methionine oxidase
    • Lim, J. C., You, Z., Kim, G., and Levine, R. L. (2011) Methionine sulfoxide reductase A is a stereospecific methionine oxidase. Proc. Natl. Acad. Sci. U.S.A. 108, 10472-10477
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 10472-10477
    • Lim, J.C.1    You, Z.2    Kim, G.3    Levine, R.L.4
  • 94
    • 84869988993 scopus 로고    scopus 로고
    • Cysteine reactivity distinguishes redox sensing by the heat-inducible and constitutive forms of heat shock protein 70
    • Miyata, Y., Rauch, J. N., Jinwal, U. K., Thompson, A. D., Srinivasan, S., Dickey, C. A., and Gestwicki, J. E. (2012) Cysteine reactivity distinguishes redox sensing by the heat-inducible and constitutive forms of heat shock protein 70. Chem. Biol. 19, 1391-1399
    • (2012) Chem. Biol. , vol.19 , pp. 1391-1399
    • Miyata, Y.1    Rauch, J.N.2    Jinwal, U.K.3    Thompson, A.D.4    Srinivasan, S.5    Dickey, C.A.6    Gestwicki, J.E.7
  • 95
    • 70249123518 scopus 로고    scopus 로고
    • Hemoglobin glutathionylation can occur through cysteine sulfenic acid intermediate: Electrospray ionization LTQ-Orbitrap hybrid mass spectrometry studies
    • Regazzoni, L., Panusa, A., Yeum, K. J., Carini, M., and Aldini, G. (2009) Hemoglobin glutathionylation can occur through cysteine sulfenic acid intermediate: electrospray ionization LTQ-Orbitrap hybrid mass spectrometry studies. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 877, 3456-3461
    • (2009) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.877 , pp. 3456-3461
    • Regazzoni, L.1    Panusa, A.2    Yeum, K.J.3    Carini, M.4    Aldini, G.5
  • 97
    • 38849100878 scopus 로고    scopus 로고
    • Glutathionylation of β-actin via a cysteinyl sulfenic acid intermediary
    • Johansson, M., and Lundberg, M. (2007) Glutathionylation of β-actin via a cysteinyl sulfenic acid intermediary. BMC Biochem. 8, 26
    • (2007) BMC Biochem. , vol.8 , pp. 26
    • Johansson, M.1    Lundberg, M.2
  • 98
    • 26244431890 scopus 로고    scopus 로고
    • The atomic resolution crystal structure of the YajL (ThiJ) protein from Escherichia coli: A close prokaryotic homologue of the Parkinsonism-associated protein DJ-1
    • Wilson, M. A., Ringe, D., and Petsko, G. A. (2005) The atomic resolution crystal structure of the YajL (ThiJ) protein from Escherichia coli: a close prokaryotic homologue of the Parkinsonism-associated protein DJ-1. J. Mol. Biol. 353, 678-691
    • (2005) J. Mol. Biol. , vol.353 , pp. 678-691
    • Wilson, M.A.1    Ringe, D.2    Petsko, G.A.3
  • 99
    • 29144528214 scopus 로고    scopus 로고
    • Single-site oxidation, cysteine 108 to cysteine sulfinic acid, in D-amino acid oxidase from Trigonopsis variabilis and its structural and functional consequences
    • Slavica, A., Dib, I., and Nidetzky, B. (2005) Single-site oxidation, cysteine 108 to cysteine sulfinic acid, in D-amino acid oxidase from Trigonopsis variabilis and its structural and functional consequences. Appl. Environ. Microbiol. 71, 8061-8068
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 8061-8068
    • Slavica, A.1    Dib, I.2    Nidetzky, B.3
  • 100
    • 84858324200 scopus 로고    scopus 로고
    • Lipocalin-type prostaglandin D synthase protects against oxidative stress-induced neuronal cell death
    • Fukuhara, A., Yamada, M., Fujimori, K., Miyamoto, Y., Kusumoto, T., Nakajima, H., and Inui, T. (2012) Lipocalin-type prostaglandin D synthase protects against oxidative stress-induced neuronal cell death. Biochem. J. 443, 75-84
    • (2012) Biochem. J. , vol.443 , pp. 75-84
    • Fukuhara, A.1    Yamada, M.2    Fujimori, K.3    Miyamoto, Y.4    Kusumoto, T.5    Nakajima, H.6    Inui, T.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.