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

143 related items for PubMed ID: 12189140

  • 1. Radicicol-sensitive peptide binding to the N-terminal portion of GRP94.
    Vogen S, Gidalevitz T, Biswas C, Simen BB, Stein E, Gulmen F, Argon Y.
    J Biol Chem; 2002 Oct 25; 277(43):40742-50. PubMed ID: 12189140
    [Abstract] [Full Text] [Related]

  • 2. Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94. II. Ligand-mediated activation of GRP94 molecular chaperone and peptide binding activity.
    Wassenberg JJ, Reed RC, Nicchitta CV.
    J Biol Chem; 2000 Jul 28; 275(30):22806-14. PubMed ID: 10816560
    [Abstract] [Full Text] [Related]

  • 3. Identification of the N-terminal peptide binding site of glucose-regulated protein 94.
    Gidalevitz T, Biswas C, Ding H, Schneidman-Duhovny D, Wolfson HJ, Stevens F, Radford S, Argon Y.
    J Biol Chem; 2004 Apr 16; 279(16):16543-52. PubMed ID: 14754890
    [Abstract] [Full Text] [Related]

  • 4. The ATPase cycle of the endoplasmic chaperone Grp94.
    Frey S, Leskovar A, Reinstein J, Buchner J.
    J Biol Chem; 2007 Dec 07; 282(49):35612-20. PubMed ID: 17925398
    [Abstract] [Full Text] [Related]

  • 5. Interaction of radicicol with members of the heat shock protein 90 family of molecular chaperones.
    Schulte TW, Akinaga S, Murakata T, Agatsuma T, Sugimoto S, Nakano H, Lee YS, Simen BB, Argon Y, Felts S, Toft DO, Neckers LM, Sharma SV.
    Mol Endocrinol; 1999 Sep 07; 13(9):1435-48. PubMed ID: 10478836
    [Abstract] [Full Text] [Related]

  • 6. Structural transitions accompanying the activation of peptide binding to the endoplasmic reticulum Hsp90 chaperone GRP94.
    Wearsch PA, Voglino L, Nicchitta CV.
    Biochemistry; 1998 Apr 21; 37(16):5709-19. PubMed ID: 9548957
    [Abstract] [Full Text] [Related]

  • 7. Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation.
    Soldano KL, Jivan A, Nicchitta CV, Gewirth DT.
    J Biol Chem; 2003 Nov 28; 278(48):48330-8. PubMed ID: 12970348
    [Abstract] [Full Text] [Related]

  • 8. Adenosine nucleotides and the regulation of GRP94-client protein interactions.
    Rosser MF, Trotta BM, Marshall MR, Berwin B, Nicchitta CV.
    Biochemistry; 2004 Jul 13; 43(27):8835-45. PubMed ID: 15236592
    [Abstract] [Full Text] [Related]

  • 9. Ligand interactions in the adenosine nucleotide-binding domain of the Hsp90 chaperone, GRP94. I. Evidence for allosteric regulation of ligand binding.
    Rosser MF, Nicchitta CV.
    J Biol Chem; 2000 Jul 28; 275(30):22798-805. PubMed ID: 10816561
    [Abstract] [Full Text] [Related]

  • 10. Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone.
    Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT.
    J Biol Chem; 2004 Oct 29; 279(44):46162-71. PubMed ID: 15292259
    [Abstract] [Full Text] [Related]

  • 11. Interaction of endoplasmic reticulum chaperone GRP94 with peptide substrates is adenine nucleotide-independent.
    Wearsch PA, Nicchitta CV.
    J Biol Chem; 1997 Feb 21; 272(8):5152-6. PubMed ID: 9030582
    [Abstract] [Full Text] [Related]

  • 12. GRP94, an ER chaperone with protein and peptide binding properties.
    Argon Y, Simen BB.
    Semin Cell Dev Biol; 1999 Oct 21; 10(5):495-505. PubMed ID: 10597632
    [Abstract] [Full Text] [Related]

  • 13. Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: implications for paralog-specific drug design.
    Immormino RM, Metzger LE, Reardon PN, Dollins DE, Blagg BS, Gewirth DT.
    J Mol Biol; 2009 May 22; 388(5):1033-42. PubMed ID: 19361515
    [Abstract] [Full Text] [Related]

  • 14. Transfer of GRP94(Gp96)-associated peptides onto endosomal MHC class I molecules.
    Berwin B, Rosser MF, Brinker KG, Nicchitta CV.
    Traffic; 2002 May 22; 3(5):358-66. PubMed ID: 11967129
    [Abstract] [Full Text] [Related]

  • 15. Dimerization characteristics of the 94-kDa glucose-regulated protein.
    Nemoto T, Matsusaka T, Ota M, Takagi T, Collinge DB, Walther-Larsen H.
    J Biochem; 1996 Aug 22; 120(2):249-56. PubMed ID: 8889807
    [Abstract] [Full Text] [Related]

  • 16. Molecular mechanisms of peptide loading by the tumor rejection antigen/heat shock chaperone gp96 (GRP94).
    Sastry S, Linderoth N.
    J Biol Chem; 1999 Apr 23; 274(17):12023-35. PubMed ID: 10207025
    [Abstract] [Full Text] [Related]

  • 17. The ER Chaperones BiP and Grp94 Regulate the Formation of Insulin-Like Growth Factor 2 (IGF2) Oligomers.
    Jin Y, Kotler JLM, Wang S, Huang B, Halpin JC, Street TO.
    J Mol Biol; 2021 Jun 25; 433(13):166963. PubMed ID: 33811917
    [Abstract] [Full Text] [Related]

  • 18. Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone GRP94/gp96.
    Nicchitta CV.
    Curr Opin Immunol; 1998 Feb 25; 10(1):103-9. PubMed ID: 9523119
    [Abstract] [Full Text] [Related]

  • 19. Biophysical analysis of the endoplasmic reticulum-resident chaperone/heat shock protein gp96/GRP94 and its complex with peptide antigen.
    Linderoth NA, Simon MN, Rodionova NA, Cadene M, Laws WR, Chait BT, Sastry S.
    Biochemistry; 2001 Feb 06; 40(5):1483-95. PubMed ID: 11170476
    [Abstract] [Full Text] [Related]

  • 20. Endoplasmic reticulum chaperone GRP94 subunit assembly is regulated through a defined oligomerization domain.
    Wearsch PA, Nicchitta CV.
    Biochemistry; 1996 Dec 24; 35(51):16760-9. PubMed ID: 8988013
    [Abstract] [Full Text] [Related]

    Page: [Next] [New Search]
    of 8.