Molecular Chaperones

Häftad, Engelska, 2012

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Beskrivning

Currently one of the hottest topics in biochemistry, the concept of molecular chaperones has challenged the paradigm of protein self-assembly. Key figures in many disciplines review all aspects of molecular chaperones in this volume, which arises from a Royal Society discussion meeting. Overview chapters discuss the significance of chaperones in biochemistry, molecular genetics and cell biology. Each chapter is well referenced providing access to the literature.

Produktinformation

Utgivningsdatum:2012-11-06
Mått:210 x 297 x 8 mm
Vikt:374 g
Format:Häftad
Språk:Engelska
Antal sidor:121
Förlag:Springer
ISBN:9789401049351

Utforska kategorier

Biokemi inom Naturvetenskap och teknik
Cellbiologi inom Naturvetenskap och teknik
Farmakologi inom Medicin

Innehållsförteckning

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.