Molecular Chaperones
Published on 30. September 1993
Book
Hardback
IX, 121 pages
978-0-412-55060-7 (ISBN)
Description
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.
More details
Edition
1993 ed.
Language
English
Place of publication
Dordrecht
Netherlands
Target group
College/higher education
Professional and scholarly
Research
Illustrations
IX, 121 p.
Dimensions
Height: 303 mm
Width: 215 mm
Thickness: 13 mm
Weight
643 gr
ISBN-13
978-0-412-55060-7 (9780412550607)
DOI
10.1007/978-94-011-2108-8
Schweitzer Classification
Other editions
Additional editions
R.J. Ellis | R.A. Laskey | G.H. Lorimer
Molecular Chaperones
E-Book
12/2012
Springer
€149.79
Available for download
R.J. Ellis | R.A. Laskey | G.H. Lorimer
Molecular Chaperones
Book
11/2012
Springer
€160.49
Shipment within 15-20 days
Content
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.