
Actin
Oxford University Press
4th Edition
Published on 28. January 1999
Book
Paperback/Softback
288 pages
978-0-19-850463-4 (ISBN)
Article exhausted; check different version
Description
Actins are a highly conserved family of proteins found in virtually all eukaryotic cells. They have prolific roles in cell motility - from the contraction of striated muscle to the movement of organelles within cells, and are known to interact with a diverse number of proteins families from myosins to gelsolins. This up-to-date edition gives a comprehensive account of actin sequence, mutation and structure as well as providing insight into ligand-binding sites and
drug and toxin binding. Illustrated throughout, this modern text also contains an extensive bibliography for the interested reader.
drug and toxin binding. Illustrated throughout, this modern text also contains an extensive bibliography for the interested reader.
More details
Series
Edition
4th Revised edition
Language
English
Place of publication
Oxford
United Kingdom
Target group
Professional and scholarly
Edition type
Revised edition
Illustrations
8 halftones, 38 line drawings
Dimensions
Height: 246 mm
Width: 188 mm
Thickness: 16 mm
Weight
619 gr
ISBN-13
978-0-19-850463-4 (9780198504634)
Copyright in bibliographic data and cover images is held by Nielsen Book Services Limited or by the publishers or by their respective licensors: all rights reserved.
Schweitzer Classification
Other editions
Previous edition
Peter Sheterline | etc.
Actin
Book
07/1996
3rd Edition
Academic Press
€55.55
Article exhausted; check for reprint
Persons
Author
Department of Human Anatomy and Cell BiologyUniversity of Liverpool
EMBL
Department of BiologyUniversity of York
Content
Introduction ; Biological characteristics of actin ; Functional properties of actin ; Actin structure ; The actin sequence ; Molecular genetic manipulation of actin ; Actin structure ; Covalent derivation sites ; Post-translational sites ; Post-translational modificaiton sites ; Proteolytic cleavage sites ; Ligand-binding sites ; Cation-binding sites ; Nucleotide-binding sites ; Self-association sites ; Actin-binding-protein sites ; Drug and toxin binding ; Acknowledgements ; Bibliography ; Protein Sequence Alignments