LEADER 01267nam--2200409---450- 001 990003027360203316 005 20071204103607.0 010 $a978-88-7228-488-9 035 $a000302736 035 $aUSA01000302736 035 $a(ALEPH)000302736USA01 035 $a000302736 100 $a20071204d2006----km-y0itay50------ba 101 $aeng 102 $aIT 105 $a||||||||001yy 200 1 $aAncient economies modern methodologies$earchaeology, comparative history, models and institutions$fedited by Peter F. Bang, Mamoru Ikeguchi and Hartmut G. 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First, Bross discusses the basics of the Hsp60 chaperonin in terms of its structure and the molecular mechanisms determining its function. Second, the author highlights the multiple roles of Hsp60 for cellular systems and regulatory pathways, especially in connection with neurodegenerative diseases caused by Hsp60 deficiency. Finally, the author highlights controversial observations suggesting additional, non-standard functions of Hsp60 in and outside mitochondria as well as possible gaps in our understanding of the chaperonin. This volume serves as a snapshot suitable for experienced researcher working in fields related to molecular chaperones yet still accessible to researchers entering the field. 410 0$aProtein Folding and Structure,$x2199-3157 606 $aProteins 606 $aBioorganic chemistry 606 $aMolecular biology 606 $aProtein Science$3https://scigraph.springernature.com/ontologies/product-market-codes/L14040 606 $aBioorganic Chemistry$3https://scigraph.springernature.com/ontologies/product-market-codes/C19010 606 $aMolecular Medicine$3https://scigraph.springernature.com/ontologies/product-market-codes/B1700X 615 0$aProteins. 615 0$aBioorganic chemistry. 615 0$aMolecular biology. 615 14$aProtein Science. 615 24$aBioorganic Chemistry. 615 24$aMolecular Medicine. 676 $a572.645 700 $aBross$b Peter$4aut$4http://id.loc.gov/vocabulary/relators/aut$01060287 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910298447903321 996 $aThe Hsp60 Chaperonin$92512273 997 $aUNINA