CORE
COnnecting
REpositories
  • Services overviewExplore all CORE services
  • Access to raw data

    • API
    • Dataset
    • FastSync
  • Content discovery

    • Recommender
    • Discovery
  • OAI identifiers

    • OAI Resolver
  • Managing content

    • Dashboard
  • Bespoke contracts

    • Consultancy services
  • Support us

      MembershipSponsorshipResearch partnership
  • About

    • About us
    • Our mission
    • Team
    • Blog
    • FAQs
    • Contact us
  • Community governance

    • Governance
    • Advisory Board
    • Board of supporters
    • Research network
  • Innovations

    • Our research
    • Labs

The Lid Domain of Caenorhabditis elegans Hsc70 Influences ATP Turnover, Cofactor Binding and Protein Folding Activity

Authors
  1. A Buchberger
  2. A Strub
  3. A Szabo
  4. A Wawrzynow
  5. A Wawrzynow
  6. AM Gaiser
  7. AM Gaiser
  8. AM Gaiser
  9. Andreas M. Gaiser
  10. AW Karzai
  11. B Demeler
  12. B Sha
  13. BC Freeman
  14. Christoph J. O. Kaiser
  15. CJ Harrison
  16. CS Gassler
  17. CS Gassler
  18. D Bimston
  19. D Brehmer
  20. D Guhathakurta
  21. D Wall
  22. DB Hayes
  23. DR Palleros
  24. EA Craig
  25. EA Craig
  26. EA Nollen
  27. EA Nollen
  28. EB Bertelsen
  29. EV Pierpaoli
  30. F Rodriguez
  31. FH Niesen
  32. Franziska T. Edelmann
  33. G Buczynski
  34. G Knarr
  35. GC Cajo
  36. H Bendz
  37. H Schroder
  38. H Sondermann
  39. H Sondermann
  40. H Wang
  41. H Wegele
  42. H Wiech
  43. Harm Kampinga
  44. HH Kampinga
  45. J Hageman
  46. J Hohfeld
  47. J Jiang
  48. J Jiang
  49. J Symersky
  50. JA Ali
  51. JC Young
  52. JC Young
  53. JF Swain
  54. JK Stuart
  55. JS McCarty
  56. K Liberek
  57. K Terada
  58. Katharina Papsdorf
  59. Klaus Richter
  60. L Packschies
  61. Li Sun
  62. LJ Worrall
  63. LS Chesnokova
  64. M Marcinowski
  65. M Vogel
  66. MF Heschl
  67. MJ Feige
  68. MK Greene
  69. MP Mayer
  70. MP Mayer
  71. MP Mayer
  72. P Lopez-Buesa
  73. P Wittung-Stafshede
  74. PH Su
  75. R Jordan
  76. R Russell
  77. R Schlecht
  78. RA Aponte
  79. RC Morshauser
  80. RC Morshauser
  81. RS Kamath
  82. S Popp
  83. S Takayama
  84. S Tzankov
  85. SL Popp
  86. SV Slepenkov
  87. T Bocking
  88. T Laufen
  89. T Weikl
  90. V Fernandez-Saiz
  91. W Han
  92. W Rist
  93. WC Suh
  94. WC Suh
  95. WF Stafford III
  96. WJ Welch
  97. X Zhu
  98. Y Minami
  99. YY Shi
Publication date
1 January 2011
Publisher
Public Library of Science
Doi
    View on PubMed

    Abstract

    Hsc70 is a conserved ATP-dependent molecular chaperone, which utilizes the energy of ATP hydrolysis to alter the folding state of its client proteins. In contrast to the Hsc70 systems of bacteria, yeast and humans, the Hsc70 system of C. elegans (CeHsc70) has not been studied to date

      Similar works

      Full text

      thumbnail-image
      Open in the Core reader
      Download PDF

      Available Versions

      Public Library of Science (PLOS)

      redirect
      Last time updated on 18/09/2018

      Crossref

      redirect
      oaiinfo:doi/10.1371%2Fjournal.pon...
      Last time updated on 02/01/2020

      Directory of Open Access Journals

      redirect
      oaioai:doaj.org/article:81a8c43ef...
      Last time updated on 13/10/2017

      Public Library of Science (PLOS)

      redirect
      Last time updated on 05/06/2019

      The Francis Crick Institute

      redirect
      oaioai:figshare.com:article/12700...
      Last time updated on 16/03/2018

      CORE (COnnecting REpositories) is a not-for-profit service hosted by The Open University supported by CORE Members.

      Product
      • Services
      • Membership
      • Sponsorship
      • Labs
      Organisation
      • About us
      • Governance
      • Team
      • Data providers
      Support
      • Terms
      • FAQs
      • Blog
      • Contact us
      Writing about CORE?

      Discover our research outputs and cite our work.

      Follow us:
      COREAccessibilityCookiesPrivacy