메뉴 건너뛰기




Volumn 582, Issue 29, 2008, Pages 3973-3978

Redox properties of the A-domain of the HMGB1 protein

Author keywords

Disulfide bond; HMGB1; Kinetics; NMR spectroscopy; Redox; Thermodynamics

Indexed keywords

HIGH MOBILITY GROUP B1 PROTEIN;

EID: 56649091195     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.09.061     Document Type: Article
Times cited : (37)

References (17)
  • 2
    • 35748967851 scopus 로고    scopus 로고
    • High-mobility group box 1 (HMGB1) protein at the crossroads between innate and adaptive immunity
    • Bianchi M.E., and Manfredi A.A. High-mobility group box 1 (HMGB1) protein at the crossroads between innate and adaptive immunity. Immunol. Rev. 220 (2007) 35-46
    • (2007) Immunol. Rev. , vol.220 , pp. 35-46
    • Bianchi, M.E.1    Manfredi, A.A.2
  • 3
    • 0033578010 scopus 로고    scopus 로고
    • Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins
    • Ohndorf U.M., Rould M.A., He Q., Pabo C.O., and Lippard S.J. Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins. Nature 399 (1999) 708-712
    • (1999) Nature , vol.399 , pp. 708-712
    • Ohndorf, U.M.1    Rould, M.A.2    He, Q.3    Pabo, C.O.4    Lippard, S.J.5
  • 4
    • 33749125188 scopus 로고    scopus 로고
    • Molecular basis for the redox control of nuclear transport of the structural chromatin protein Hmgb1
    • Hoppe G., Talcott K.E., Bhattacharya S.K., Crabb J.W., and Sears J.E. Molecular basis for the redox control of nuclear transport of the structural chromatin protein Hmgb1. Exp. Cell. Res. 312 (2006) 3526-3538
    • (2006) Exp. Cell. Res. , vol.312 , pp. 3526-3538
    • Hoppe, G.1    Talcott, K.E.2    Bhattacharya, S.K.3    Crabb, J.W.4    Sears, J.E.5
  • 6
    • 0031933143 scopus 로고    scopus 로고
    • Determining the structures of large proteins and protein complexes by NMR
    • Clore G.M., and Gronenborn A.M. Determining the structures of large proteins and protein complexes by NMR. Trends Biotechnol. 16 (1998) 22-34
    • (1998) Trends Biotechnol. , vol.16 , pp. 22-34
    • Clore, G.M.1    Gronenborn, A.M.2
  • 7
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer F.Q., and Buettner G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic. Biol. Med. 30 (2001) 1191-1212
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 8
    • 34548819311 scopus 로고    scopus 로고
    • Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions
    • Greenfield N.J. Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions. Nat. Protoc. 1 (2006) 2527-2535
    • (2006) Nat. Protoc. , vol.1 , pp. 2527-2535
    • Greenfield, N.J.1
  • 9
    • 56649099490 scopus 로고    scopus 로고
    • The thioredoxin system
    • Banerjee R. (Ed), Wiley-Interscience, Hoboken
    • Holmgren A. The thioredoxin system. In: Banerjee R. (Ed). Redox Biochemistry (2008), Wiley-Interscience, Hoboken 68-74
    • (2008) Redox Biochemistry , pp. 68-74
    • Holmgren, A.1
  • 10
    • 0019193130 scopus 로고
    • Enzymatic reduction of alloxan by thioredoxin and NADPH-thioredoxin reductase
    • Holmgren A., and Lyckeborg C. Enzymatic reduction of alloxan by thioredoxin and NADPH-thioredoxin reductase. Proc. Natl. Acad. Sci. USA 77 (1980) 5149-5152
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5149-5152
    • Holmgren, A.1    Lyckeborg, C.2
  • 11
    • 0023956149 scopus 로고
    • Disulphide bonds and protein stability
    • Creighton T.E. Disulphide bonds and protein stability. Bioessays 8 (1988) 57-63
    • (1988) Bioessays , vol.8 , pp. 57-63
    • Creighton, T.E.1
  • 12
    • 0028839833 scopus 로고
    • The content of glutathione and glutathione S-transferases and the glutathione peroxidase activity in rat liver nuclei determined by a non-aqueous technique of cell fractionation
    • Soboll S., Grundel S., Harris J., Kolb-Bachofen V., Ketterer B., and Sies H. The content of glutathione and glutathione S-transferases and the glutathione peroxidase activity in rat liver nuclei determined by a non-aqueous technique of cell fractionation. Biochem. J. 311 Part 3 (1995) 889-894
    • (1995) Biochem. J. , vol.311 , Issue.PART 3 , pp. 889-894
    • Soboll, S.1    Grundel, S.2    Harris, J.3    Kolb-Bachofen, V.4    Ketterer, B.5    Sies, H.6
  • 13
    • 0022527573 scopus 로고
    • Native state of high mobility group chromosomal proteins 1 and 2 is rapidly lost by oxidation of sulfhydryl groups during storage
    • Kohlstaedt L.A., King D.S., and Cole R.D. Native state of high mobility group chromosomal proteins 1 and 2 is rapidly lost by oxidation of sulfhydryl groups during storage. Biochemistry 25 (1986) 4562-4565
    • (1986) Biochemistry , vol.25 , pp. 4562-4565
    • Kohlstaedt, L.A.1    King, D.S.2    Cole, R.D.3
  • 14
    • 0142137129 scopus 로고    scopus 로고
    • Monocytic cells hyperacetylate chromatin protein HMGB1 to redirect it towards secretion
    • Bonaldi T., et al. Monocytic cells hyperacetylate chromatin protein HMGB1 to redirect it towards secretion. EMBO J. 22 (2003) 5551-5560
    • (2003) EMBO J. , vol.22 , pp. 5551-5560
    • Bonaldi, T.1
  • 15
    • 0036775236 scopus 로고    scopus 로고
    • The nuclear protein HMGB1 is secreted by monocytes via a non-classical, vesicle-mediated secretory pathway
    • Gardella S., Andrei C., Ferrera D., Lotti L.V., Torrisi M.R., Bianchi M.E., and Rubartelli A. The nuclear protein HMGB1 is secreted by monocytes via a non-classical, vesicle-mediated secretory pathway. EMBO Rep. 3 (2002) 995-1001
    • (2002) EMBO Rep. , vol.3 , pp. 995-1001
    • Gardella, S.1    Andrei, C.2    Ferrera, D.3    Lotti, L.V.4    Torrisi, M.R.5    Bianchi, M.E.6    Rubartelli, A.7
  • 16
    • 0018728098 scopus 로고
    • Reduction of disulfides by thioredoxin
    • Holmgren A. Reduction of disulfides by thioredoxin. J. Biol. Chem. 254 (1979) 9113-9119
    • (1979) J. Biol. Chem. , vol.254 , pp. 9113-9119
    • Holmgren, A.1
  • 17
    • 0033626528 scopus 로고    scopus 로고
    • 13C NMR chemical shifts can predict disulfide bond formation
    • 13C NMR chemical shifts can predict disulfide bond formation. J. Biomol. NMR 18 (2000) 165-171
    • (2000) J. Biomol. NMR , vol.18 , pp. 165-171
    • Sharma, D.1    Rajarathnam, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.