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OverviewFull Product DetailsAuthor: Mary-Jane Gething (Department of Biochemistry, Department of Biochemistry, Melbourne University, Australia)Publisher: Oxford University Press Imprint: Oxford University Press Dimensions: Width: 18.80cm , Height: 3.40cm , Length: 24.60cm Weight: 1.276kg ISBN: 9780198599487ISBN 10: 019859948 Pages: 580 Publication Date: 27 November 1997 Audience: Professional and scholarly , Professional & Vocational Format: Paperback Publisher's Status: Active Availability: To order ![]() Stock availability from the supplier is unknown. We will order it for you and ship this item to you once it is received by us. Table of Contents1: HSP70 proteins 2: HSP110/SSE proteins 3: HSP40 (DNAJ-related) proteins 4: GRPE-like proteins 5: HSP90 proteins 6: CPN60 and CPN10 proteins 7: Cytosolic chaperonins 8: HSP100 proteins 9: Small HSPs 10: Calnexin and calreticulin 11: PDI and thioredoxin-related proteins 12: Peptidyl-prolyl isomerases 12A: Cyclophilin PPIases 12B: FK-506 binding proteins 12C: Parvulin PP1ases 13: Individual chaperonins 14: Protein specific chaperones 15: Intramolecular chaperones 16: Molecular chaperone machine 17: Cellular regulation of chaperone activityReviewsThis book describes important aspects of the structure, function, and regulation of all known chaperones and enzymes involved in protein folding. The information is up-to-date and the text is arranged in a concise and easy to read format. This is a useful handbook, not only for scientists in the protein folding field, but also for those working in related areas for whom the comprehensive summaries will be especially valuable. 4 Stars. --Doody's Journal<br> The book is divided into 17 parts, with the first 15 cataloguing the different classes of molecular chaperones. Information on nearly 200 chaperones have been included. Each part contains a brief entry, typically between one to three pages in length, of each family member. In the literature, many chaperones are referred to by more than one name, and a particularly useful feature in the book is the listing of these alternative names. Other information includes isolation, gene sequence, biological activities, regulation, biological interactions and mutagenesis studies. . . . [T]he book is a must for everyone working in the field of molecular chaperones. In addition, since protein folding is an integral part of the general field of protein science, it will also be invaluable to anyone interested in that field. The book should be on the shelf of every library housing biologically and biochemically relevant literature. --The Quarterly Review of Biology<br> <br> This book describes important aspects of the structure, function, and regulation of all known chaperones and enzymes involved in protein folding. The information is up-to-date and the text is arranged in a concise and easy to read format. This is a useful handbook, not only for scientists in the protein folding field, but also for those working in related areas for whom the comprehensive summaries will be especially valuable. 4 Stars. --Doody's Journal<p><br> The book is divided into 17 parts, with the first 15 cataloguing the different classes of molecular chaperones. Information on nearly 200 chaperones have been included. Each part contains a brief entry, typically between one to three pages in length, of each family member. In the literature, many chaperones are referred to by more than one name, and a particularly useful feature in the book is the listing of these alternative names. Other information includes isolation, gene sequence, biological activities, regulation, biolo """This book describes important aspects of the structure, function, and regulation of all known chaperones and enzymes involved in protein folding. The information is up-to-date and the text is arranged in a concise and easy to read format. This is a useful handbook, not only for scientists in the protein folding field, but also for those working in related areas for whom the comprehensive summaries will be especially valuable. 4 Stars."" --Doody's Journal""The book is divided into 17 parts, with the first 15 cataloguing the different classes of molecular chaperones. Information on nearly 200 chaperones have been included. Each part contains a brief entry, typically between one to three pages in length, of each family member. In the literature, many chaperones are referred to by more than one name, and a particularly useful feature in the book is the listing of these alternative names. Other information includes isolation, gene sequence, biological activities, regulation, biological interactions and mutagenesis studies. . . . [T]he book is a must for everyone working in the field of molecular chaperones. In addition, since protein folding is an integral part of the general field of protein science, it will also be invaluable to anyone interested in that field. The book should be on the shelf of every library housing biologically and biochemically relevant literature.""--The Quarterly Review of Biology" Author InformationDr Mary-Jane Gething (Partner in the Sambrook & Tooze Partnership, our co-publishers of the Guidebooks Series) Dept of Biochemistry, Melbourne University, Parkville 3052, Australia. Tel: 00 61 3 9344 5948. Fax: 00613 9347 9109. Email: gething@ariel.ucs.unimelb.edu.au Tab Content 6Author Website:Countries AvailableAll regions |