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03399nam a22004815i 4500 |
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978-3-319-11731-7 |
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DE-He213 |
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cr nn 008mamaa |
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141208s2015 gw | s |||| 0|eng d |
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|a 9783319117317
|9 978-3-319-11731-7
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|a 10.1007/978-3-319-11731-7
|2 doi
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|a The Networking of Chaperones by Co-chaperones
|h [electronic resource] :
|b Control of Cellular Protein Homeostasis /
|c edited by Gregory Lloyd Blatch, Adrienne Lesley Edkins.
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|a Cham :
|b Springer International Publishing :
|b Imprint: Springer,
|c 2015.
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| 300 |
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|a XV, 276 p. 35 illus., 31 illus. in color.
|b online resource.
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|a text
|b txt
|2 rdacontent
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|a computer
|b c
|2 rdamedia
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|a online resource
|b cr
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|a text file
|b PDF
|2 rda
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|a Subcellular Biochemistry,
|x 0306-0225 ;
|v 78
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|a Preface -- List of Contributors- About the Editors- GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: Nucleotide exchange factors for Hsp70 molecular chaperones -- Functions of the Hsp90-Binding FKBP Immunophilins -- Hsp70/Hsp90 organising protein (Hop): beyond interactions with chaperones and prion proteins -- Specification of Hsp70 function by Type I and Type II Hsp40 -- Cdc37 as a Co-chaperone to Hsp90 -- p23 and Aha1- UCS proteins: chaperones for myosin and co-chaperones for Hsp90 -- Chaperonin - Co-chaperonin Interactions -- Co-chaperones of the mammalian endoplasmic reticulum -- The evolution and function of co-chaperones in mitochondria -- CHIP: a co-chaperone for degradation by the proteasome -- The role of HSP70 and its co-chaperones in protein misfolding, aggregation and disease -- Index.
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|a Co-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is a dynamic balance between the integrated processes of protein folding, degradation and translocation. The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by a cohort of diverse non-client proteins, known as co-chaperones. The second edition includes the current status of the field and descriptions of a number of novel co-chaperones that have been recently identified. This new edition has a strong focus on the role of co-chaperones in human disease and as putative drug targets. The book will be a resource for both newcomers and established researchers in the field of cell stress and chaperones, as well as those interested in cross-cutting disciplines such as cellular networks and systems biology.
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| 650 |
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|a Medicine.
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| 650 |
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|a Life sciences.
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| 650 |
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|a Biochemistry.
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| 650 |
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4 |
|a Biomedicine.
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| 650 |
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|a Biomedicine general.
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| 650 |
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4 |
|a Life Sciences, general.
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| 650 |
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|a Biochemistry, general.
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| 700 |
1 |
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|a Blatch, Gregory Lloyd.
|e editor.
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| 700 |
1 |
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|a Edkins, Adrienne Lesley.
|e editor.
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| 710 |
2 |
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|a SpringerLink (Online service)
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| 773 |
0 |
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|t Springer eBooks
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| 776 |
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8 |
|i Printed edition:
|z 9783319117300
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| 830 |
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|a Subcellular Biochemistry,
|x 0306-0225 ;
|v 78
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| 856 |
4 |
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|u http://dx.doi.org/10.1007/978-3-319-11731-7
|z Full Text via HEAL-Link
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| 912 |
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|a ZDB-2-SBL
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| 950 |
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|a Biomedical and Life Sciences (Springer-11642)
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