Molecular Chaperones
Editat de R. J. Ellis, R. a. Laskey, G.H. Lorimeren Limba Engleză Paperback – 6 noi 2012
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Specificații
ISBN-13: 9789401049351
ISBN-10: 9401049351
Pagini: 136
Ilustrații: IX, 121 p.
Dimensiuni: 210 x 297 x 7 mm
Greutate: 0.35 kg
Ediția:Softcover reprint of the original 1st ed. 1993
Editura: SPRINGER NETHERLANDS
Colecția Springer
Locul publicării:Dordrecht, Netherlands
ISBN-10: 9401049351
Pagini: 136
Ilustrații: IX, 121 p.
Dimensiuni: 210 x 297 x 7 mm
Greutate: 0.35 kg
Ediția:Softcover reprint of the original 1st ed. 1993
Editura: SPRINGER NETHERLANDS
Colecția Springer
Locul publicării:Dordrecht, Netherlands
Public țintă
ResearchCuprins
1 The general concept of molecular chaperones.- 2 The role of nucleoplasmin in chromatin assembly and disassembly.- Discussion: S. Lindquist, A. Horwich, N. W. Green, M.-J. Gething, W. Neupert, R. J. Ellis.- 3 The Escherichia coli chaperones involved in DNA replication.- Discussion: R. Jaenicke, M.-J. Gething, R. J. Ellis.- 4 The role of heat-shock proteins in thermotolerance.- Discussion: P. Viitanen, R. Jaenicke, A. Horwich, F.-U. Hard, R. J. Ellis, W. J. Welch.- 5 What does protein refolding in vitro tell us about protein folding in the cell?.- Discussion: A. R. Clarke, F.-U. Hard, G. H. Lorimer, R. J. Ellis, P. Viitanen.- 6 Chaperonins and protein folding: unity and disunity of mechanisms.- Discussion: N. C. Price, R. Jaenicke, F.-U. Hard, R. B. Freedman, M. Yoshida, W. J. Welch, B. O’Hara.- 7 A chaperonin from a thermophilic bacterium, Thermus thermophilus.- Discussion: G. H. Lorimer, R. Jaenicke, P. Viitanen, H. Saibil.- 8 Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1.- Discussion: N. J. Cowan, P. Viitanen, P. Mickletheaite, M.-J. Gething, H. Saibil, R. Jaenicke, C. Georgopoulos, F.-U. Hard, K. Willison.- 9 Heat shock proteins functioning as molecular chaperones: their roles in normal and stressed cells.- Discussion: M.-J. Gething, A. R. Clarke, P. Viitanen, P. Lund, I. G. Haas, C. Georgopoulos.- 10 The role of molecular chaperones in protein transport into the endoplasmic reticulum.- Discussion: S. Lindquist, W. J. Welch, P. Viitanen, G. H. Lorimer.- 11 Recognition of ligands by SecB, a molecular chaperone involved in bacterial protein export.- Discussion: J. Murphy, P. Lund, W. J. Welch, P. Viitanen, R. Jaenicke, F.-U. Hartl, T. E. Creighton, R. A. Laskey, G. H. Lorimer.- 12 Roles of molecular chaperones inprotein targeting to mitochondria.- Discussion: W. J. Welch, A. Baker, M.-J. Gething, R. Jaenicke.- 13 Molecular chaperones and the immune response.- Discussion: W. J. Welch, M.-J. Gething, P. Lund, A. R. Coates, I. G. Haas, P. Viitanen.- 14 Tumour suppressor genes and molecular chaperones.- Discussion: W. J. Welch, P. Viitanen, G. H. Lorimer, M. Zylicz, M. F. Perutz116.