메뉴 건너뛰기




Volumn 1764, Issue 8, 2006, Pages 1356-1362

The oxidised histone octamer does not form a H3 disulphide bond

Author keywords

H3 dimer; Histone octamer; Hydrogen bond modulation; Oxidation; Reduction

Indexed keywords

CYSTEINE; DIMER; HISTONE; HISTONE H3; POTASSIUM CHLORIDE; POTASSIUM DIHYDROGEN PHOSPHATE; S NITROSOGLUTATHIONE; TETRAMER;

EID: 33747798039     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.06.014     Document Type: Article
Times cited : (5)

References (32)
  • 1
    • 0037311294 scopus 로고    scopus 로고
    • Histone chaperones and nucleosome assembly
    • Akey C.W., and Luger K. Histone chaperones and nucleosome assembly. Curr. Opin. Struct. Biol. 13 (2003) 6-14
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 6-14
    • Akey, C.W.1    Luger, K.2
  • 2
    • 0034522793 scopus 로고    scopus 로고
    • Asymmetries in the nucleosome core particle at 2.5 Å resolution
    • Harp J.M., Hanson B.L., Timm D.E., and Bunick G.J. Asymmetries in the nucleosome core particle at 2.5 Å resolution. Acta Crystallogr. D56 (2000) 1513-1534
    • (2000) Acta Crystallogr. , vol.D56 , pp. 1513-1534
    • Harp, J.M.1    Hanson, B.L.2    Timm, D.E.3    Bunick, G.J.4
  • 3
  • 4
    • 0025837183 scopus 로고
    • The nucleosomal core octamer at 3.1 Å resolution: a tripartite protein assembly and a left-handed superhelix
    • Arents G., Burlingame R.W., Wang B.C., Love W.E., and Moudrianakis E.N. The nucleosomal core octamer at 3.1 Å resolution: a tripartite protein assembly and a left-handed superhelix. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 10148-10152
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 10148-10152
    • Arents, G.1    Burlingame, R.W.2    Wang, B.C.3    Love, W.E.4    Moudrianakis, E.N.5
  • 9
    • 0037090937 scopus 로고    scopus 로고
    • Regulation of microsomal and cytosolic glutathione S-transferase activities by S-nitrosylation
    • Ji Y., Toader V., and Bennett B.M. Regulation of microsomal and cytosolic glutathione S-transferase activities by S-nitrosylation. Biochem. Pharmacol. 63 (2002) 1397-1404
    • (2002) Biochem. Pharmacol. , vol.63 , pp. 1397-1404
    • Ji, Y.1    Toader, V.2    Bennett, B.M.3
  • 10
    • 15944380094 scopus 로고    scopus 로고
    • Microsomal glutathione transferase 1 is not S-nitrosylated in rat liver microsomes or in endotoxin challenged rats
    • Shi Q., and Lou Y.J. Microsomal glutathione transferase 1 is not S-nitrosylated in rat liver microsomes or in endotoxin challenged rats. Pharmacol. Res. 51 (2005) 303-310
    • (2005) Pharmacol. Res. , vol.51 , pp. 303-310
    • Shi, Q.1    Lou, Y.J.2
  • 12
    • 0033212815 scopus 로고    scopus 로고
    • Integration of macromolecular diffraction data
    • Leslie A.G.W. Integration of macromolecular diffraction data. Acta Crystallogr. D55 (1999) 1696-1702
    • (1999) Acta Crystallogr. , vol.D55 , pp. 1696-1702
    • Leslie, A.G.W.1
  • 13
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50 (1994) 760-763
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 14
    • 84920325457 scopus 로고
    • AMoRe: an automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. D50 (1994) 157-163
    • (1994) Acta Crystallogr. , vol.D50 , pp. 157-163
    • Navaza, J.1
  • 15
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dobson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D50 (1997) 240-255
    • (1997) Acta Crystallogr. , vol.D50 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dobson, E.J.3
  • 16
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model building tools for molecular graphics
    • Emsley P., and Cowtan K. Coot: model building tools for molecular graphics. Acta Crystallogr. D60 (2004) 2126-2132
    • (2004) Acta Crystallogr. , vol.D60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 17
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin V.S., and Wilson K.S. Automated refinement of protein models. Acta Crystallogr. D49 (1994) 129-149
    • (1994) Acta Crystallogr. , vol.D49 , pp. 129-149
    • Lamzin, V.S.1    Wilson, K.S.2
  • 19
    • 84893482610 scopus 로고
    • A solution for the best rotation to relate two sets of vectors
    • Kabsch W. A solution for the best rotation to relate two sets of vectors. Acta Crystallogr. A32 (1976) 922-923
    • (1976) Acta Crystallogr. , vol.A32 , pp. 922-923
    • Kabsch, W.1
  • 20
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and Swiss-PDBViewer: an environment for comparative protein modeling
    • Guex N., and Peitsh M.C. SWISS-MODEL and Swiss-PDBViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsh, M.C.2
  • 22
    • 33646195686 scopus 로고    scopus 로고
    • Detection of protein assemblies in crystals
    • Berthold M.R., et al. (Ed), Springer-Verlag, Berlin
    • Krissinel E., and Henrick K. Detection of protein assemblies in crystals. In: Berthold M.R., et al. (Ed). CompLife 2005, LNBI 3695 (2005), Springer-Verlag, Berlin 163-174
    • (2005) CompLife 2005, LNBI 3695 , pp. 163-174
    • Krissinel, E.1    Henrick, K.2
  • 23
    • 0017855202 scopus 로고
    • Cross-linking of nucleosomal histones with monofunctional imodoesters
    • Wyns L., Lasters I., and Hamers R. Cross-linking of nucleosomal histones with monofunctional imodoesters. Nucleic Acids Res. 5 (1978) 2345-2348
    • (1978) Nucleic Acids Res. , vol.5 , pp. 2345-2348
    • Wyns, L.1    Lasters, I.2    Hamers, R.3
  • 24
    • 17744364870 scopus 로고    scopus 로고
    • Regulation of MAP kinase-dependent apoptotic pathway: implication of reactive oxygen and nitrogen species
    • Sumbayev V.V., and Yasinska I.M. Regulation of MAP kinase-dependent apoptotic pathway: implication of reactive oxygen and nitrogen species. Arch. Biochem. Biophys. 436 (2005) 406-412
    • (2005) Arch. Biochem. Biophys. , vol.436 , pp. 406-412
    • Sumbayev, V.V.1    Yasinska, I.M.2
  • 25
    • 0035815274 scopus 로고    scopus 로고
    • Structural basis of the redox switch in the OxyR transcription factor
    • Choi H., Kim S., Mukhopadhyay P., Cho S., Woo J., Storz G., and Ryu S. Structural basis of the redox switch in the OxyR transcription factor. Cell 105 (2001) 103-113
    • (2001) Cell , vol.105 , pp. 103-113
    • Choi, H.1    Kim, S.2    Mukhopadhyay, P.3    Cho, S.4    Woo, J.5    Storz, G.6    Ryu, S.7
  • 26
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • Gilbert H.F. Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol. Relat. Areas Mol. Biol. 63 (1990) 69-172
    • (1990) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 27
    • 2342518271 scopus 로고    scopus 로고
    • Role of oxidant species in aging
    • Stadtman E.R. Role of oxidant species in aging. Curr. Med. Chem. 11 (2004) 1105-1112
    • (2004) Curr. Med. Chem. , vol.11 , pp. 1105-1112
    • Stadtman, E.R.1
  • 28
    • 0037013155 scopus 로고    scopus 로고
    • OxyR: a molecular code for redox-related signaling
    • Kim S.O., Merchant K., Nudelman R., and Beyer W.F. OxyR: a molecular code for redox-related signaling. Cell 109 (2002) 383-396
    • (2002) Cell , vol.109 , pp. 383-396
    • Kim, S.O.1    Merchant, K.2    Nudelman, R.3    Beyer, W.F.4
  • 29
    • 0037864487 scopus 로고    scopus 로고
    • Hydrogen bonding in redox-modulated molecular recognition. An experimental and theoretical investigation
    • Gray M., Cuello A.O., Cooke G., and Rotello V.O. Hydrogen bonding in redox-modulated molecular recognition. An experimental and theoretical investigation. J. Am. Chem. Soc. 125 (2003) 7882-7888
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 7882-7888
    • Gray, M.1    Cuello, A.O.2    Cooke, G.3    Rotello, V.O.4
  • 30
    • 0346220393 scopus 로고    scopus 로고
    • The role of dynamics in allosteric regulation
    • Kern D., and Zuiderweg E.R.P. The role of dynamics in allosteric regulation. Curr. Opin. Struct. Biol. 13 (2003) 748-757
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 748-757
    • Kern, D.1    Zuiderweg, E.R.P.2
  • 31
    • 33646239638 scopus 로고    scopus 로고
    • Histone H3 variants and their potential role in indexing mammalian genomes: the "H3 barcode hypothesis"
    • Hake S.B., and David Allis C. Histone H3 variants and their potential role in indexing mammalian genomes: the "H3 barcode hypothesis". Proc. Natl. Acad. Sci. 103 (2006) 6428-6435
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 6428-6435
    • Hake, S.B.1    David Allis, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.