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Volumn 9, Issue 2, 2015, Pages 415-419

Backbone resonance assignments of ferric human cytochrome c and the pro-apoptotic G41S mutant in the ferric and ferrous states

Author keywords

Apoptosis; Human cytochrome c; Mitochondria; Paramagnetic NMR

Indexed keywords

CYTOCHROME C; IRON; MUTANT PROTEIN;

EID: 84941943538     PISSN: 18742718     EISSN: 1874270X     Source Type: Journal    
DOI: 10.1007/s12104-015-9621-3     Document Type: Article
Times cited : (6)

References (23)
  • 1
    • 0034823714 scopus 로고    scopus 로고
    • A further clue to understanding the mobility of mitochondrial yeast cytochrome c: a (15)N T1rho investigation of the oxidized and reduced species
    • Barker PD et al (2001) A further clue to understanding the mobility of mitochondrial yeast cytochrome c: a (15)N T1rho investigation of the oxidized and reduced species. Eur J Biochem 268:4468–4476
    • (2001) Eur J Biochem , vol.268 , pp. 4468-4476
    • Barker, P.D.1
  • 2
    • 83055197001 scopus 로고    scopus 로고
    • Probing a complex of cytochrome C and cardiolipin by magnetic circular dichroism spectroscopy: implications for the initial events in apoptosis
    • Bradley JM, Silkstone G, Wilson MT, Cheesman MR, Butt JN (2011) Probing a complex of cytochrome C and cardiolipin by magnetic circular dichroism spectroscopy: implications for the initial events in apoptosis. J Am Chem Soc 133:19676–19679
    • (2011) J Am Chem Soc , vol.133 , pp. 19676-19679
    • Bradley, J.M.1    Silkstone, G.2    Wilson, M.T.3    Cheesman, M.R.4    Butt, J.N.5
  • 3
    • 0031627465 scopus 로고    scopus 로고
    • An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli
    • Cai M, Huang Y, Sakaguchi K, Clore GM, Gronenborn AM, Craigie R (1998) An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli. J Biomol NMR 11:97–102
    • (1998) J Biomol NMR , vol.11 , pp. 97-102
    • Cai, M.1    Huang, Y.2    Sakaguchi, K.3    Clore, G.M.4    Gronenborn, A.M.5    Craigie, R.6
  • 7
    • 84869442007 scopus 로고    scopus 로고
    • Origin of the conformational heterogeneity of cardiolipin-bound cytochrome C
    • Hong Y, Muenzner J, Grimm SK, Pletneva EV (2012) Origin of the conformational heterogeneity of cardiolipin-bound cytochrome C. J Am Chem Soc 134:18713–18723. doi:10.1021/ja307426k
    • (2012) J Am Chem Soc , vol.134 , pp. 18713-18723
    • Hong, Y.1    Muenzner, J.2    Grimm, S.K.3    Pletneva, E.V.4
  • 8
    • 79953745644 scopus 로고    scopus 로고
    • The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: from respiration to apoptosis
    • Huttemann M et al (2011) The multiple functions of cytochrome c and their regulation in life and death decisions of the mammalian cell: from respiration to apoptosis. Mitochondrion 11:369–381. doi:10.1016/j.mito.2011.01.010
    • (2011) Mitochondrion , vol.11 , pp. 369-381
    • Huttemann, M.1
  • 9
    • 0036963585 scopus 로고    scopus 로고
    • Expression and characterization of recombinant human cytochrome c in E. coli
    • Jeng WY, Chen CY, Chang HC, Chuang WJ (2002) Expression and characterization of recombinant human cytochrome c in E. coli. J Bioenerg Biomembr 34:423–431
    • (2002) J Bioenerg Biomembr , vol.34 , pp. 423-431
    • Jeng, W.Y.1    Chen, C.Y.2    Chang, H.C.3    Chuang, W.J.4
  • 10
    • 84894238312 scopus 로고    scopus 로고
    • Enhancing the peroxidase activity of cytochrome c by mutation of residue 41: implications for the peroxidase mechanism and cytochrome c release
    • Josephs TM, Morison IM, Day CL, Wilbanks SM, Ledgerwood EC (2014) Enhancing the peroxidase activity of cytochrome c by mutation of residue 41: implications for the peroxidase mechanism and cytochrome c release. Biochem J 458:259–265. doi:10.1042/bj20131386
    • (2014) Biochem J , vol.458 , pp. 259-265
    • Josephs, T.M.1    Morison, I.M.2    Day, C.L.3    Wilbanks, S.M.4    Ledgerwood, E.C.5
  • 11
    • 27744433524 scopus 로고    scopus 로고
    • Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors
    • Kagan VE et al (2005) Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors. Nat Chem Biol 1:223–232
    • (2005) Nat Chem Biol , vol.1 , pp. 223-232
    • Kagan, V.E.1
  • 12
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86:147–157
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 14
    • 41349097770 scopus 로고    scopus 로고
    • A mutation of human cytochrome c enhances the intrinsic apoptotic pathway but causes only thrombocytopenia
    • Morison IM et al (2008) A mutation of human cytochrome c enhances the intrinsic apoptotic pathway but causes only thrombocytopenia. Nat Genet 40:387–389
    • (2008) Nat Genet , vol.40 , pp. 387-389
    • Morison, I.M.1
  • 15
    • 80052810923 scopus 로고    scopus 로고
    • Analysis of non-uniformly sampled spectra with multi-dimensional decomposition
    • Orekhov VY, Jaravine VA (2011) Analysis of non-uniformly sampled spectra with multi-dimensional decomposition. Prog Nucl Magn Reson Spectrosc 59:271–292. doi:10.1016/j.pnmrs.2011.02.002
    • (2011) Prog Nucl Magn Reson Spectrosc , vol.59 , pp. 271-292
    • Orekhov, V.Y.1    Jaravine, V.A.2
  • 17
    • 0032574759 scopus 로고    scopus 로고
    • Bacterial expression of a mitochondrial cytochrome c. Trimethylation of lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition
    • Pollock WB, Rosell FI, Twitchett MB, Dumont ME, Mauk AG (1998) Bacterial expression of a mitochondrial cytochrome c. Trimethylation of lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition. Biochemistry 37:6124–6131
    • (1998) Biochemistry , vol.37 , pp. 6124-6131
    • Pollock, W.B.1    Rosell, F.I.2    Twitchett, M.B.3    Dumont, M.E.4    Mauk, A.G.5
  • 19
    • 84888402530 scopus 로고    scopus 로고
    • The hydrogen-peroxide-induced radical behaviour in human cytochrome c-phospholipid complexes: implications for the enhanced pro-apoptotic activity of the G41S mutant
    • Rajagopal BS et al (2013) The hydrogen-peroxide-induced radical behaviour in human cytochrome c-phospholipid complexes: implications for the enhanced pro-apoptotic activity of the G41S mutant. Biochem J 456:441–452. doi:10.1042/bj20130758
    • (2013) Biochem J , vol.456 , pp. 441-452
    • Rajagopal, B.S.1
  • 21
    • 84863088972 scopus 로고    scopus 로고
    • Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy
    • Volkov AN, Vanwetswinkel S, Van de Water K, van Nuland NA (2012) Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy. J Biomol NMR 52:245–256. doi:10.1007/s10858-012-9607-8
    • (2012) J Biomol NMR , vol.52 , pp. 245-256
    • Volkov, A.N.1    Vanwetswinkel, S.2    Van de Water, K.3    van Nuland, N.A.4
  • 22
    • 19444382397 scopus 로고    scopus 로고
    • The CCPN data model for NMR spectroscopy: development of a software pipeline
    • Vranken WF et al (2005) The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59:687–696. doi:10.1002/prot.20449
    • (2005) Proteins , vol.59 , pp. 687-696
    • Vranken, W.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.