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Journal Abstract Search


215 related items for PubMed ID: 38483986

  • 1. Structural transitions modulate the chaperone activities of Grp94.
    Amankwah YS, Fleifil Y, Unruh E, Collins P, Wang Y, Vitou K, Bates A, Obaseki I, Sugoor M, Alao JP, McCarrick RM, Gewirth DT, Sahu ID, Li Z, Lorigan GA, Kravats AN.
    Proc Natl Acad Sci U S A; 2024 Mar 19; 121(12):e2309326121. PubMed ID: 38483986
    [Abstract] [Full Text] [Related]

  • 2. Grp94 Works Upstream of BiP in Protein Remodeling Under Heat Stress.
    Amankwah YS, Collins P, Fleifil Y, Unruh E, Ruiz Márquez KJ, Vitou K, Kravats AN.
    J Mol Biol; 2022 Oct 15; 434(19):167762. PubMed ID: 35905823
    [Abstract] [Full Text] [Related]

  • 3. Insight into the Nucleotide Based Modulation of the Grp94 Molecular Chaperone Using Multiscale Dynamics.
    Alao JP, Obaseki I, Amankwah YS, Nguyen Q, Sugoor M, Unruh E, Popoola HO, Tehver R, Kravats AN.
    J Phys Chem B; 2023 Jun 22; 127(24):5389-5409. PubMed ID: 37294929
    [Abstract] [Full Text] [Related]

  • 4. The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation.
    Sun M, Kotler JLM, Liu S, Street TO.
    J Biol Chem; 2019 Apr 19; 294(16):6387-6396. PubMed ID: 30787103
    [Abstract] [Full Text] [Related]

  • 5. 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]

  • 6. The endoplasmic reticulum chaperone BiP is a closure-accelerating cochaperone of Grp94.
    Huang B, Sun M, Hoxie R, Kotler JLM, Friedman LJ, Gelles J, Street TO.
    Proc Natl Acad Sci U S A; 2022 Feb 01; 119(5):. PubMed ID: 35078937
    [Abstract] [Full Text] [Related]

  • 7. 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]

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  • 11. GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum.
    Marzec M, Eletto D, Argon Y.
    Biochim Biophys Acta; 2012 Mar 25; 1823(3):774-87. PubMed ID: 22079671
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  • 12. Structural transitions modulate the chaperone activities of Grp94.
    Mirikar D, Bushman Y, Truman AW.
    Trends Biochem Sci; 2024 Sep 25; 49(9):752-753. PubMed ID: 38906726
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  • 16. Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER.
    McClellan AJ, Endres JB, Vogel JP, Palazzi D, Rose MD, Brodsky JL.
    Mol Biol Cell; 1998 Dec 25; 9(12):3533-45. PubMed ID: 9843586
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  • 19. 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
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  • 20. Visualization of conformational transition of GRP94 in solution.
    Sun S, Zhu R, Zhu M, Wang Q, Li N, Yang B.
    Life Sci Alliance; 2024 Feb 07; 7(2):. PubMed ID: 37949474
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