02928nam 2200613 450 99646659080331620220919140017.03-540-48782-410.1007/BFb0074073(CKB)1000000000437188(SSID)ssj0000327380(PQKBManifestationID)12097417(PQKBTitleCode)TC0000327380(PQKBWorkID)10301355(PQKB)11767569(DE-He213)978-3-540-48782-1(MiAaPQ)EBC5577799(Au-PeEL)EBL5577799(OCoLC)1066179851(MiAaPQ)EBC6875767(Au-PeEL)EBL6875767(PPN)155210440(EXLCZ)99100000000043718820220919d1994 uy 0engurnn|008mamaatxtccrTransition to chaos in classical and quantum mechanics lectures given at the 3rd session of the Centro Internazionale Matematico Estivo (C.I.M.E.) held in Montecatini Terme, Italy, July 6-13, 1991 /edited by Sandro Graffi [and five others]1st ed. 1994.Berlin, Germany ;New York, New York :Springer-Verlag,[1994]©19941 online resource (VIII, 196 p.) C.I.M.E. Foundation Subseries ;1589Bibliographic Level Mode of Issuance: Monograph3-540-58416-1 Non commutative methods in semiclassical analysis -- Equidistribution of periodic orbits: An overview of classical VS quantum results -- Action minimizing orbits in hamiltomian systems.The Session was intended to give a broad survey of the mathematical problems arising in the chaotic transition of deterministic dynamical systems, both in classical and quantum mechanics. The lectures of Mather and Forni thoroughly cover the area- preserving twist maps, and include an up-to-date version of the Aubry-Mather theory. The lectures of Bellissard describe the quantum aspects: classical limit, localization, spectral properties of the relevant Schrödinger operators and thus represent an exhaus- tive introduction to the mathematics of "quantum chaos". The lectures of Degli Esposti et al. reviews equidistribu- tion of unstable periodic orbits and classical limit of quantized toral symplectomorphisms.C.I.M.E. Foundation Subseries ;1589Chaotic behavior in systemsCongressesQuantum theoryChaotic behavior in systemsQuantum theory.530.12Graffi S(Sandro),1943-Centro internazionale matematico estivo.MiAaPQMiAaPQMiAaPQBOOK996466590803316Transition to Chaos in Classical and Quantum Mechanics2831150UNISA03244nam 2200373z- 450 991022004260332120210211(CKB)3800000000216351(oapen)https://directory.doabooks.org/handle/20.500.12854/49612(oapen)doab49612(EXLCZ)99380000000021635120202102d2017 |y 0engurmn|---annantxtrdacontentcrdamediacrrdacarrierThe HSP70 Molecular Chaperone MachinesFrontiers Media SA20171 online resource (69 p.)Frontiers Research Topics2-88945-125-9 Members of the HSP70 family form a central hub of the molecular chaperone network, controlling protein homeostasis in prokaryotes and in the ATP-containing compartments of the eukaryotic cells. The heat-inducible form HSPA1A (HSP70), its constitutive cytosolic cognate HSPA8 (Hsc70), its endoplasmic reticulum form HSPA5 (BiP), and its mitochondrial form HSPA9 (Mortalin), as well as the more distantly related HSPHs (HSP110s), make up 1-2 % of the total mass of proteins in human cells. They use the energy of ATP-hydrolysis to prevent and forcefully revert the process of protein misfolding and aggregation during and following various stresses, presumably by working as unfoldases to lift aberrant conformers out of kinetic traps. As such, HSP70s, in cooperation with their J-domain co-chaperones and nucleotide exchange factors (NEFs) and co-disaggregases, form an efficient network of cellular defenses against the accumulation of cytotoxic misfolded protein conformers, which may cause degenerative diseases such as Parkinson's and Alzheimer's disease, diabetes, and aging in general. In addition to their function in repair of stress-induced damage, HSP70s fulfill many housekeeping functions, including assisting the de novo folding and maturation of proteins, driving the translocation of protein precursors across narrow membrane pores into organelles, and by controlling the oligomeric state of key regulator protein complexes involved in signal transduction and vesicular trafficking. For reasons not well understood, HSP70s are also found on the surface of some animal cells, in particular cancer cells where they may serve as specific targets for cancer immunotherapy. Here, we gathered seven mini reviews, each presenting a complementary aspect of HSP70's structure and function in bacteria and eukaryotes, under physiological and stressful conditions. These articles highlight how, the various members of this conserved family of molecular chaperones, assisted by their various J-domain and NEF cochaperones and co-disaggregases, harness ATP hydrolysis to perform a great diversity of life-sustaining cellular functions using a similar molecular mechanism.DisaggregaseHeat-Shock ProteinsMisfolding diseasesproteostasisunfoldaseMatthias P. Mayerauth1332335Pierre GoloubinoffauthBOOK9910220042603321The HSP70 Molecular Chaperone Machines3040852UNINA