01475nam2-2200409---450-99000118240020331620050526114911.0000118240USA01000118240(ALEPH)000118240USA0100011824020031001d1968----km-y0itay0103----bagerDE||||||||001yy<<Band 2>>:<<Das>> System des Privatrechts, die Staatslehre und die Prinzipien des VolkerrechtsHeinrich AhrensAalenEd. Scientia (Darmstadt, tip. Weihert)1968XVI, 532 p.200120010010001182282001Naturrecht, oder Philosophie des Rechts und des Staatesauf dem Grunde des ethischen Zusammenhanges von Recht und KulturAHRENS,Heinrich501618ITsalbcISBD990001182400203316II.1.D. 907/2(IV-A-939/2)32998 L.M.IV-AIX-A-113(2)32998 L.M.IV-ABKUMASIAV41020031001USA011309SIAV41020031001USA011315SIAV31020031002USA010953SIAV41020031020USA011752SIAV41020031020USA011753PATRY9020040406USA011725COPAT39020050526USA011149System des Privatrechts, die Staatslehre und die Prinzipien des Volkerrechts982536UNISA03933nam 22006615 450 991029844790332120200706230348.03-319-26088-X10.1007/978-3-319-26088-4(CKB)3430000000002623(EBL)4188214(SSID)ssj0001596873(PQKBManifestationID)16296499(PQKBTitleCode)TC0001596873(PQKBWorkID)14886749(PQKB)11557305(DE-He213)978-3-319-26088-4(MiAaPQ)EBC4188214(PPN)190882891(EXLCZ)99343000000000262320151208d2015 u| 0engur|n|---|||||txtccrThe Hsp60 Chaperonin /by Peter Bross1st ed. 2015.Cham :Springer International Publishing :Imprint: Springer,2015.1 online resource (90 p.)Protein Folding and Structure,2199-3157Description based upon print version of record.3-319-26086-3 Includes bibliographical references.Introduction -- Historical sketch of the discovery and recognition of the function of chaperonins -- Molecular structure of chaperonins -- Folding by enclosure in the chaperonin cavity -- Evolutionary origins and family relations -- Chaperoning mechanisms: folding helpers, folding protectors or misfolding blockers? -- Sequence variations in proteins affecting chaperonin dependence -- Genetic organization of type I chaperonin genes -- Regulation of type I chaperonin gene expression -- Subcellular localization -- Posttranslational modifications -- Variations in Hsp60 and Hsp10 in humans -- Type I chaperonins are essential for cell viability and mutations cause deficiency phenotypes -- Human diseases caused by genetic mutations in the Hsp60/Hsp10 system -- Molecular investigations of disease mechanisms -- Molecular investigations of disease mechanisms -- Outlook.In this unique overview of the Hsp60 chaperonin, Peter Bross addresses molecular biologists, medical research scientists and individuals interested in molecular or general biology. 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.Protein Folding and Structure,2199-3157ProteinsBioorganic chemistryMolecular biologyProtein Sciencehttps://scigraph.springernature.com/ontologies/product-market-codes/L14040Bioorganic Chemistryhttps://scigraph.springernature.com/ontologies/product-market-codes/C19010Molecular Medicinehttps://scigraph.springernature.com/ontologies/product-market-codes/B1700XProteins.Bioorganic chemistry.Molecular biology.Protein Science.Bioorganic Chemistry.Molecular Medicine.572.645Bross Peterauthttp://id.loc.gov/vocabulary/relators/aut1060287MiAaPQMiAaPQMiAaPQBOOK9910298447903321The Hsp60 Chaperonin2512273UNINA