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Volumn 48, Issue 4, 1997, Pages 399-407

Phosphofructokinase interacts with molecular chaperonins GroEL and GroES

Author keywords

Chaperonins; GroEL; GroES; Phosphofructokinase

Indexed keywords

6 PHOSPHOFRUCTOKINASE; CHAPERONIN; MUSCLE PROTEIN; RECOMBINANT PROTEIN;

EID: 0031292574     PISSN: 02365383     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (2)

References (12)
  • 2
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    • Purification and properties of the GroES morphogenetic protein of Escherichia coli
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    • (1986) J. Biol. Chem. , vol.261 , pp. 414-419
    • Chandraseknar, G.H.1    Tilly, K.2    Woolford, C.3    Hendrix, R.4    Georgopoulos, C.5
  • 3
    • 0028027055 scopus 로고
    • Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryoelectron microscopy
    • Chen, S., Roseman, A. M., Hunter, A. S., Wood, S. P., Burston, S. G., Ranson, N. A., Clarke, A. R., Saibil, H. R. (1994) Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryoelectron microscopy. Nature 371, 261-264.
    • (1994) Nature , vol.371 , pp. 261-264
    • Chen, S.1    Roseman, A.M.2    Hunter, A.S.3    Wood, S.P.4    Burston, S.G.5    Ranson, N.A.6    Clarke, A.R.7    Saibil, H.R.8
  • 5
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M. J., Sambrook, J. (1992) Protein folding in the cell. Nature 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 6
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F. U. (1996) Molecular chaperones in cellular protein folding. Nature 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 7
    • 0025840379 scopus 로고
    • The chaperonin GroEL binds a polypeptide in an α-helical conformation
    • Landry, S. J., Gierasch, L. M. (1991) The chaperonin GroEL binds a polypeptide in an α-helical conformation. Biochemistry 30, 7359-7362.
    • (1991) Biochemistry , vol.30 , pp. 7359-7362
    • Landry, S.J.1    Gierasch, L.M.2
  • 8
    • 0025205189 scopus 로고
    • (Mg-ATP)-dependent self-assembly of molecular chaperone GroEL
    • B. Lissin, N. M., Venyaminov, S. Yu., Girshovich, A. S. (1990) (Mg-ATP)-dependent self-assembly of molecular chaperone GroEL. Nature 348, 339-342.
    • (1990) Nature , vol.348 , pp. 339-342
    • B. Lissin, N.M.1    Venyaminov, S.Y.2    Girshovich, A.S.3
  • 10
    • 0018182491 scopus 로고
    • Isolation and characterization of muscle phosphofructokinase with varying degrees of phosphorylation
    • Uyeda, K., Miyatake, A., Luby, L. J., Richards, E. G. (1978) Isolation and characterization of muscle phosphofructokinase with varying degrees of phosphorylation. J. Biol. Chem. 25, 8319-8327.
    • (1978) J. Biol. Chem. , vol.25 , pp. 8319-8327
    • Uyeda, K.1    Miyatake, A.2    Luby, L.J.3    Richards, E.G.4
  • 12
    • 0028260023 scopus 로고
    • Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
    • Zahn, R., Spitzfaden, C., Ottiger, H., Wütrich, K., Plückthum, A. (1994) Destabilization of the complete protein secondary structure on binding to the chaperone GroEL. Nature 368, 261-265.
    • (1994) Nature , vol.368 , pp. 261-265
    • Zahn, R.1    Spitzfaden, C.2    Ottiger, H.3    Wütrich, K.4    Plückthum, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.