메뉴 건너뛰기




Volumn 304, Issue 1, 2000, Pages 81-98

Defining the eukaryotic cytosolic chaperonin-binding sites in human tubulins

Author keywords

CCT; Chaperonin; Mutagenesis; Protein folding; Tubulin

Indexed keywords

ALPHA TUBULIN; BETA TUBULIN; CHAPERONIN; CHAPERONIN CONTAINING TCP 1; GAMMA TUBULIN; GUANIDINE; UNCLASSIFIED DRUG;

EID: 0034680592     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4177     Document Type: Article
Times cited : (33)

References (48)
  • 5
    • 0031914188 scopus 로고    scopus 로고
    • Atomic structures of tubulin and FtsZ
    • published erratum appears in Trends Cell Biol. 1998 May;8(5):210
    • (1998) Trends Cell Biol. , vol.8 , pp. 133-137
    • Erickson, H.P.1
  • 11
    • 0034705567 scopus 로고    scopus 로고
    • Individual subunits of the eukaryotic cytosolic chaperonin mediate interactions with binding sites located on subdomains of β-actin
    • (2000) J. Biol. Chem. , vol.275 , pp. 18985-18994
    • Hynes, G.M.1    Willison, K.R.2
  • 13
    • 0006984683 scopus 로고    scopus 로고
    • Introduction and 8 sections on CCT
    • Guidebook to Molecular Chaperones and Protein-Folding Catalysts (Gething, M.-J., ed.), Sambrook/Tooze Publications at Oxford University Press, Oxford
    • (1997) , pp. 207-211
    • Kubota, H.1    Willison, K.R.2
  • 15
  • 17
    • 0030842428 scopus 로고    scopus 로고
    • Elucidation of the subunit orientation in CCT (chaperonin containing TCP1) from the subunit composition of CCT microcomplexes
    • (1997) EMBO J. , vol.16 , pp. 4311-4316
    • Liou, A.K.1    Willison, K.R.2
  • 23
    • 2642593025 scopus 로고    scopus 로고
    • Crystal structure of the bacterial cell-division protein FtsZ
    • (1998) Nature , vol.391 , pp. 203-206
    • Lowe, J.1    Amos, L.A.2
  • 25
    • 0028196813 scopus 로고
    • Facilitated folding of actins and tubulins occurs via a nucleotide-dependent interaction between cytoplasmic chaperonin and distinctive folding intermediates
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2895-2904
    • Melki, R.1    Cowan, N.J.2
  • 30
    • 0032495513 scopus 로고    scopus 로고
    • Structure of the α β tubulin dimer by electron crystallography
    • published erratum appears in Nature 1998 May 14;393(6681):191
    • (1998) Nature , vol.391 , pp. 199-203
    • Nogales, E.1    Wolf, S.G.2    Downing, K.H.3
  • 36
    • 0028293043 scopus 로고
    • In vitro reconstitution of centrosome assembly and function: The central role of γ-tubulin
    • (1994) Cell , vol.76 , pp. 623-637
    • Stearns, T.1    Kirschner, M.2
  • 42
    • 0001010955 scopus 로고    scopus 로고
    • Composition and function of the eukaryotic cytosolic chaperonin-containing TCP-1
    • Molecular Chaperones and Folding Catalysts: Regulation, Cellular Function and Mechanisms (Bukau, B., ed.), Harwood Academic Publishers, The Netherlands
    • (1999) , pp. 555-571
    • Willison, K.R.1
  • 43
    • 0003840284 scopus 로고    scopus 로고
    • The role of the cytosolic chaperonin, CCT, in normal eukaryotic cell growth
    • Molecular Chaperones, Oxford University Press, Oxford. In the press
    • (2000)
    • Willison, K.R.1    Grantham, J.2
  • 44
    • 0001314116 scopus 로고    scopus 로고
    • Structure and function of chaperonins in archaebacteria and eukaryotic cytosol
    • The Chaperonins (Ellis, R. J., ed.), Academic Press Inc., London, UK
    • (1996) , pp. 107-135
    • Willison, K.R.1    Horwich, A.L.2
  • 45
    • 0000991152 scopus 로고
    • The structure, function and genetics of the chaperonin containing TCP-1 (CCT) in eukaryotic cytosol
    • The Biology of Heat Shock Proteins and Molecular Chaperones (Morimoto, R. I., Tissieres, A. and Georgopoulos, C., eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (1994) , pp. 299-312
    • Willison, K.R.1    Kubota, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.