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1
Life and death of a BiP substrate.
Semin Cell Dev Biol. 2010 Jul;21(5):472-8. doi: 10.1016/j.semcdb.2009.12.008. Epub 2009 Dec 21.
2
The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends.
J Biol Chem. 2019 Feb 8;294(6):2098-2108. doi: 10.1074/jbc.REV118.002804. Epub 2018 Dec 18.
3
Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.
IET Syst Biol. 2012 Apr;6(2):54-63. doi: 10.1049/iet-syb.2011.0006.
5
The large Hsp70 Grp170 binds to unfolded protein substrates in vivo with a regulation distinct from conventional Hsp70s.
J Biol Chem. 2014 Jan 31;289(5):2899-907. doi: 10.1074/jbc.M113.507491. Epub 2013 Dec 10.
6
BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions.
J Mol Biol. 2015 Apr 10;427(7):1589-608. doi: 10.1016/j.jmb.2015.02.011. Epub 2015 Feb 16.
8
Co-chaperones of the mammalian endoplasmic reticulum.
Subcell Biochem. 2015;78:179-200. doi: 10.1007/978-3-319-11731-7_9.
10
The heat shock protein 70 molecular chaperone network in the pancreatic endoplasmic reticulum - a quantitative approach.
FEBS J. 2007 Oct;274(19):5175-87. doi: 10.1111/j.1742-4658.2007.06039.x. Epub 2007 Sep 10.

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2
Mechanical effect of protein glycosylation on BiP-mediated post-translational translocation and folding in the endoplasmic reticulum.
Biophys Rev. 2025 Apr 7;17(2):435-447. doi: 10.1007/s12551-025-01313-x. eCollection 2025 Apr.
4
7
Loss of SIL1 Affects Actin Dynamics and Leads to Abnormal Neural Migration.
Mol Neurobiol. 2025 Jan;62(1):335-350. doi: 10.1007/s12035-024-04272-8. Epub 2024 Jun 8.
8
Protein networking: nicotinic acetylcholine receptors and their protein-protein-associations.
Mol Cell Biochem. 2024 Jul;479(7):1627-1642. doi: 10.1007/s11010-024-05032-x. Epub 2024 May 21.
9
Recombinant cellular model system for human muscle-type nicotinic acetylcholine receptor α1β1δε.
Cell Stress Chaperones. 2023 Nov;28(6):1013-1025. doi: 10.1007/s12192-023-01395-0. Epub 2023 Nov 25.

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3
A luminal flavoprotein in endoplasmic reticulum-associated degradation.
Proc Natl Acad Sci U S A. 2009 Sep 1;106(35):14831-6. doi: 10.1073/pnas.0900742106. Epub 2009 Aug 19.
5
One step at a time: endoplasmic reticulum-associated degradation.
Nat Rev Mol Cell Biol. 2008 Dec;9(12):944-57. doi: 10.1038/nrm2546. Epub 2008 Nov 12.
6
Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3.
EMBO J. 2008 Nov 5;27(21):2862-72. doi: 10.1038/emboj.2008.199. Epub 2008 Oct 16.
7
Regulated release of ERdj3 from unfolded proteins by BiP.
EMBO J. 2008 Nov 5;27(21):2873-82. doi: 10.1038/emboj.2008.207. Epub 2008 Oct 16.
8
Mammalian BiP controls posttranslational ER translocation of the hepatitis B virus large envelope protein.
FEBS Lett. 2008 Sep 22;582(21-22):3179-84. doi: 10.1016/j.febslet.2008.07.062. Epub 2008 Aug 15.
9
ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER.
Science. 2008 Jul 25;321(5888):569-72. doi: 10.1126/science.1159293.
10
Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding.
Cell. 2008 Jun 13;133(6):1068-79. doi: 10.1016/j.cell.2008.05.022.

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