rdf-syntax-grammar
mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    title: Molecular aspects of the stress response
    sub title: chaperones, membranes and networks
  name:
    name part: Csermely, Peter.
  name:
    name part: Vígh, László
    name part: prof
  name:
    name part: SpringerLink (Online service)
  type of resource: text
  genre: bibliography
  genre: Electronic books.
  origin info:
    place:
      place term: nyu
    date issued: 2007
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: electronic
    form: remote
    extent: xviii, 201 pages : illustrations, portraits
  table of contents: Protein misassembly: macromolecular crowding and molecular chaperones / R. John Ellis -- The cellular "networking" of mammalian HSP27 and its functions in the control of protein folding, redox state and apoptosis / André-Patrick Arrigo -- Molecular interaction network of the HSP90 chaperone system / Rongmin Zhao and Walid A. Houry -- Organization of the functions and components of the endoplasmic reticulum / Yuichiro Shimizu and Linda M. Hendershot -- Molecular crime and cellular punishment: active detoxification of misfolded and aggregated proteins in the cell by the chaperone and protease networks / Marie-Pierre Hinault and Pierre Goloubinoff -- Chaperones as parts of cellular networks / Peter Csermely, Csaba Söti and Gregory L. Blatch -- Chaperones as parts of organelle networks / György Szabadkai and Rosario Rizzuto -- Heat shock factor 1 as a coordinator of stress and developmental pathways / Julius Anckar and Lea Sistonen -- Chaperone regulation of the heat shock protein response / Richard Voellmy and Frank Boellmann -- Mechanisms of activation and regulation of the heat shock-sensitive signaling pathways / Sébastien Ian Nadeau and Jacques Landry -- Membrane-regulated stress response: a theoretical and practical approach / László Vígh ... [et al.] -- Beyond the lipid hypothesis: mechanisms underlying phenotypic plasticity in inducible cold tolerance / Scott A.L. Hayward ... [et al.] -- Trehalose as a "chemical chaperone:" fact and fantasy / John H. Crowe -- Chaperones as part of immune networks / Zoltán Prohászka -- The stress of misfolded proteins: C. elegans models for neurodegenerative disease and aging / Heather R. Brignull, James F. Morley and Richard I. Morimoto -- HSP90 and developmental networks / Suzannah Rutherford, Jennifer R. Knapp and Peter Csermely.
  note: edited by Peter Csermely, László Vígh.
  note: Electronic resource.
  note: Electronic reproduction. New York : Springer, 2008. Mode of access: World Wide Web. System requirements: Web browser. Title from title screen (viewed on Jan. 22, 2008). Access may be restricted to users at subscribing institutions.
  note: Includes bibliographical references and index.
  subject:
    topic: Stress, Physiological
    topic: physiopathology
  subject:
    topic: Cell Physiological Phenomena
  subject:
    topic: Molecular Chaperones
  subject:
    topic: Moleculaire biologie
  subject:
    topic: Stress
  subject:
    topic: Heat shock proteins
  subject:
    topic: Molecular chaperones
  subject:
    topic: Protein folding
  subject:
    topic: Stress (Physiology)
  subject:
    topic: Molécules chaperonnes
  subject:
    topic: Protéines de choc thermique
  subject:
    topic: Protéines
    topic: Repliement
  subject:
    topic: Stress
  classification: QP82.2.S8 M62 2007eb
  classification: 572/.633
  classification: QZ 160 M718 2007
  classification: W1 AD559 v.594 2007
  related item:
    identifier: (DLC) 2007295588
    identifier: (OCoLC)77496248
  related item:
    title info:
      title: Advances in experimental medicine and biology ; v. 594
  identifier: 0387399755
  identifier: 9780387399751
  identifier: 978-0-387-39974-4 Springer
  identifier: http://proxy.library.tamu.edu/login
  record info:
    record content source: GW5XE
    record creation date: 080128
    record change date: 20210810090325.0
    record identifier: in00002381212