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Journal Abstract Search

306 related items for PubMed ID: 23645669

  • 1. The Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channel.
    Buck TM, Plavchak L, Roy A, Donnelly BF, Kashlan OB, Kleyman TR, Subramanya AR, Brodsky JL.
    J Biol Chem; 2013 Jun 21; 288(25):18366-80. PubMed ID: 23645669
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  • 2. Interactions between intersubunit transmembrane domains regulate the chaperone-dependent degradation of an oligomeric membrane protein.
    Buck TM, Jordahl AS, Yates ME, Preston GM, Cook E, Kleyman TR, Brodsky JL.
    Biochem J; 2017 Feb 01; 474(3):357-376. PubMed ID: 27903760
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  • 6. Diminished Ost3-dependent N-glycosylation of the BiP nucleotide exchange factor Sil1 is an adaptive response to reductive ER stress.
    Stevens KLP, Black AL, Wells KM, Yeo KYB, Steuart RFL, Stirling CJ, Schulz BL, Mousley CJ.
    Proc Natl Acad Sci U S A; 2017 Nov 21; 114(47):12489-12494. PubMed ID: 29109265
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  • 9. Hsp70 promotes epithelial sodium channel functional expression by increasing its association with coat complex II and its exit from endoplasmic reticulum.
    Chanoux RA, Robay A, Shubin CB, Kebler C, Suaud L, Rubenstein RC.
    J Biol Chem; 2012 Jun 01; 287(23):19255-65. PubMed ID: 22496374
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  • 10. The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.
    Zacchi LF, Wu HC, Bell SL, Millen L, Paton AW, Paton JC, Thomas PJ, Zolkiewski M, Brodsky JL.
    J Biol Chem; 2014 May 02; 289(18):12727-47. PubMed ID: 24627482
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  • 11. Epithelial sodium channel biogenesis and quality control in the early secretory pathway.
    Buck TM, Brodsky JL.
    Curr Opin Nephrol Hypertens; 2018 Sep 02; 27(5):364-372. PubMed ID: 29916852
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  • 12. Cytoplasmic Hsp70 promotes ubiquitination for endoplasmic reticulum-associated degradation of a misfolded mutant of the yeast plasma membrane ATPase, PMA1.
    Han S, Liu Y, Chang A.
    J Biol Chem; 2007 Sep 07; 282(36):26140-9. PubMed ID: 17631501
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  • 13. The Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD).
    Hrizo SL, Gusarova V, Habiel DM, Goeckeler JL, Fisher EA, Brodsky JL.
    J Biol Chem; 2007 Nov 09; 282(45):32665-75. PubMed ID: 17823116
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  • 14. The Grp170 nucleotide exchange factor executes a key role during ERAD of cellular misfolded clients.
    Inoue T, Tsai B.
    Mol Biol Cell; 2016 May 15; 27(10):1650-62. PubMed ID: 27030672
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  • 15. The interplay of Hrd3 and the molecular chaperone system ensures efficient degradation of malfolded secretory proteins.
    Mehnert M, Sommermeyer F, Berger M, Kumar Lakshmipathy S, Gauss R, Aebi M, Jarosch E, Sommer T.
    Mol Biol Cell; 2015 Jan 15; 26(2):185-94. PubMed ID: 25428985
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  • 16. SLC26A9 is selected for endoplasmic reticulum associated degradation (ERAD) via Hsp70-dependent targeting of the soluble STAS domain.
    Needham PG, Goeckeler-Fried JL, Zhang C, Sun Z, Wetzel AR, Bertrand CA, Brodsky JL.
    Biochem J; 2021 Dec 22; 478(24):4203-4220. PubMed ID: 34821356
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  • 17. A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors.
    Craven RA, Egerton M, Stirling CJ.
    EMBO J; 1996 Jun 03; 15(11):2640-50. PubMed ID: 8654361
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  • 18. Endoplasmic reticulum-associated degradation of the renal potassium channel, ROMK, leads to type II Bartter syndrome.
    O'Donnell BM, Mackie TD, Subramanya AR, Brodsky JL.
    J Biol Chem; 2017 Aug 04; 292(31):12813-12827. PubMed ID: 28630040
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  • 19. Paraoxonase 2 is an ER chaperone that regulates the epithelial Na+ channel.
    Shi S, Buck TM, Nickerson AJ, Brodsky JL, Kleyman TR.
    Am J Physiol Cell Physiol; 2022 Jan 01; 322(1):C111-C121. PubMed ID: 34852210
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  • 20. Paraoxonase 3 functions as a chaperone to decrease functional expression of the epithelial sodium channel.
    Shi S, Montalbetti N, Wang X, Rush BM, Marciszyn AL, Baty CJ, Tan RJ, Carattino MD, Kleyman TR.
    J Biol Chem; 2020 Apr 10; 295(15):4950-4962. PubMed ID: 32079677
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