These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Journal Abstract Search

377 related items for PubMed ID: 18973809

  • 1.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 2. Protein memory through altered folding mediated by intramolecular chaperones.
    Shinde UP, Liu JJ, Inouye M.
    Nature; 1997 Oct 02; 389(6650):520-2. PubMed ID: 9333245
    [Abstract] [Full Text] [Related]

  • 3.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 4. Folding pathway mediated by an intramolecular chaperone: the structural and functional characterization of the aqualysin I propeptide.
    Marie-Claire C, Yabuta Y, Suefuji K, Matsuzawa H, Shinde U.
    J Mol Biol; 2001 Jan 05; 305(1):151-65. PubMed ID: 11114254
    [Abstract] [Full Text] [Related]

  • 5. Identification of the interactions critical for propeptide-catalyzed folding of Tk-subtilisin.
    Tanaka S, Matsumura H, Koga Y, Takano K, Kanaya S.
    J Mol Biol; 2009 Nov 27; 394(2):306-19. PubMed ID: 19766655
    [Abstract] [Full Text] [Related]

  • 6.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 7.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 8. Structure of POIA1, a homologous protein to the propeptide of subtilisin: implication for protein foldability and the function as an intramolecular chaperone.
    Sasakawa H, Yoshinaga S, Kojima S, Tamura A.
    J Mol Biol; 2002 Mar 15; 317(1):159-67. PubMed ID: 11916386
    [Abstract] [Full Text] [Related]

  • 9. Folding pathway mediated by an intramolecular chaperone: characterization of the structural changes in pro-subtilisin E coincident with autoprocessing.
    Shinde U, Inouye M.
    J Mol Biol; 1995 Sep 08; 252(1):25-30. PubMed ID: 7666430
    [Abstract] [Full Text] [Related]

  • 10. Inhibitor-assisted refolding of protease: a protease inhibitor as an intramolecular chaperone.
    Kojima S, Iwahara A, Yanai H.
    FEBS Lett; 2005 Aug 15; 579(20):4430-6. PubMed ID: 16061231
    [Abstract] [Full Text] [Related]

  • 11.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 12. Propeptide does not act as an intramolecular chaperone but facilitates protein disulfide isomerase-assisted folding of a conotoxin precursor.
    Buczek O, Olivera BM, Bulaj G.
    Biochemistry; 2004 Feb 03; 43(4):1093-101. PubMed ID: 14744155
    [Abstract] [Full Text] [Related]

  • 13. Principles of chaperone-mediated protein folding.
    Hartl FU.
    Philos Trans R Soc Lond B Biol Sci; 1995 Apr 29; 348(1323):107-12. PubMed ID: 7770479
    [Abstract] [Full Text] [Related]

  • 14.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 15.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 16.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 17.
    ; . PubMed ID:
    [No Abstract] [Full Text] [Related]

  • 18. The effect of molecular chaperones on in vivo and in vitro folding processes.
    Schwarz E, Lilie H, Rudolph R.
    Biol Chem; 1996 Apr 29; 377(7-8):411-6. PubMed ID: 8922274
    [Abstract] [Full Text] [Related]

  • 19. Chaperoning Anfinsen: the steric foldases.
    Pauwels K, Van Molle I, Tommassen J, Van Gelder P.
    Mol Microbiol; 2007 May 29; 64(4):917-22. PubMed ID: 17501917
    [Abstract] [Full Text] [Related]

  • 20. From hatching to dispatching: the multiple cellular roles of the Hsp70 molecular chaperone machinery.
    Meimaridou E, Gooljar SB, Chapple JP.
    J Mol Endocrinol; 2009 Jan 29; 42(1):1-9. PubMed ID: 18852216
    [Abstract] [Full Text] [Related]

    Page: [Next] [New Search]
    of 19.