LEADER 03910nam 22006975 450 001 9910298299703321 005 20260810145501.0 010 $a3-319-11731-9 024 7 $a10.1007/978-3-319-11731-7 035 $a(CKB)3710000000315898 035 $a(EBL)1968083 035 $a(SSID)ssj0001407862 035 $a(PQKBManifestationID)11876785 035 $a(PQKBTitleCode)TC0001407862 035 $a(PQKBWorkID)11410060 035 $a(PQKB)10896518 035 $a(DE-He213)978-3-319-11731-7 035 $a(MiAaPQ)EBC1968083 035 $z(PPN)258852054 035 $a(PPN)183153308 035 $a(EXLCZ)993710000000315898 100 $a20141208d2015 u| 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 14$aThe Networking of Chaperones by Co-chaperones $eControl of Cellular Protein Homeostasis /$fedited by Gregory Lloyd Blatch, Adrienne Lesley Edkins 205 $a1st ed. 2015. 210 1$aCham :$cSpringer International Publishing :$cImprint: Springer,$d2015. 215 $a1 online resource (286 p.) 225 1 $aSubcellular Biochemistry,$x2542-8810 ;$v78 300 $aDescription based upon print version of record. 311 08$a3-319-11730-0 320 $aIncludes bibliographical references and index. 327 $aPreface -- 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. 330 $aCo-chaperones are important mediators of the outcome of chaperone assisted protein homeostasis, which is a dynamic balance between the integrated processes of protein folding, degradation and translocation. The Networking of Chaperones by Co-chaperones describes how the function of the major molecular chaperones is regulated by a cohort of diverse non-client proteins, known as co-chaperones. The second edition includes the current status of the field and descriptions of a number of novel co-chaperones that have been recently identified. This new edition has a strong focus on the role of co-chaperones in human disease and as putative drug targets. The book will be a resource for both newcomers and established researchers in the field of cell stress and chaperones, as well as those interested in cross-cutting disciplines such as cellular networks and systems biology. 410 0$aSubcellular Biochemistry,$x2542-8810 ;$v78 606 $aMedicine$xResearch 606 $aBiology$xResearch 606 $aLife sciences 606 $aBiochemistry 606 $aBiomedical Research 606 $aLife Sciences 606 $aBiochemistry 615 0$aMedicine$xResearch. 615 0$aBiology$xResearch. 615 0$aLife sciences. 615 0$aBiochemistry. 615 14$aBiomedical Research. 615 24$aLife Sciences. 615 24$aBiochemistry. 676 $a570 676 $a572 676 $a610 702 $aBlatch$b Gregory L.$4edt$4http://id.loc.gov/vocabulary/relators/edt 702 $aEdkins$b Adrienne Lesley$4edt$4http://id.loc.gov/vocabulary/relators/edt 906 $aBOOK 912 $a9910298299703321 996 $aNetworking of Chaperones by Co-Chaperones$93907166 997 $aUNINA