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Items: 1 to 20 of 160

1.

Kar2p availability defines distinct forms of endoplasmic reticulum stress in living cells.

Lajoie P, Moir RD, Willis IM, Snapp EL.

Mol Biol Cell. 2012 Mar;23(5):955-64. doi: 10.1091/mbc.E11-12-0995.

2.

Endoplasmic reticulum stress regulation of the Kar2p/BiP chaperone alleviates proteotoxicity via dual degradation pathways.

Hsu CL, Prasad R, Blackman C, Ng DT.

Mol Biol Cell. 2012 Feb;23(4):630-41. doi: 10.1091/mbc.E11-04-0297.

3.

Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast.

Okamura K, Kimata Y, Higashio H, Tsuru A, Kohno K.

Biochem Biophys Res Commun. 2000 Dec 20;279(2):445-50.

PMID:
11118306
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Deletion of yeast p24 genes activates the unfolded protein response.

Belden WJ, Barlowe C.

Mol Biol Cell. 2001 Apr;12(4):957-69.

8.

Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins.

Kimata Y, Kimata YI, Shimizu Y, Abe H, Farcasanu IC, Takeuchi M, Rose MD, Kohno K.

Mol Biol Cell. 2003 Jun;14(6):2559-69.

9.

Essential roles of the Kar2/BiP molecular chaperone downstream of the UPR pathway in Cryptococcus neoformans.

Jung KW, Kang HA, Bahn YS.

PLoS One. 2013;8(3):e58956. doi: 10.1371/journal.pone.0058956.

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BiP availability distinguishes states of homeostasis and stress in the endoplasmic reticulum of living cells.

Lai CW, Aronson DE, Snapp EL.

Mol Biol Cell. 2010 Jun 15;21(12):1909-21. doi: 10.1091/mbc.E09-12-1066.

12.

BiP-bound and nonclustered mode of Ire1 evokes a weak but sustained unfolded protein response.

Ishiwata-Kimata Y, Promlek T, Kohno K, Kimata Y.

Genes Cells. 2013 Apr;18(4):288-301. doi: 10.1111/gtc.12035.

13.

Dissection of the translocation and chaperoning functions of yeast BiP/Kar2p in vivo.

Holkeri H, Paunola E, Jämsä E, Makarow M.

J Cell Sci. 1998 Mar;111 ( Pt 6):749-57.

14.

Saccharomyces cerevisiae Rot1p is an ER-localized membrane protein that may function with BiP/Kar2p in protein folding.

Takeuchi M, Kimata Y, Hirata A, Oka M, Kohno K.

J Biochem. 2006 Mar;139(3):597-605.

PMID:
16567426
15.

Changes in BiP availability reveal hypersensitivity to acute endoplasmic reticulum stress in cells expressing mutant huntingtin.

Lajoie P, Snapp EL.

J Cell Sci. 2011 Oct 1;124(Pt 19):3332-43. doi: 10.1242/jcs.087510. Erratum in: J Cell Sci. 2012 Feb 1;125(Pt 3):789.

16.

Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP.

Kabani M, Kelley SS, Morrow MW, Montgomery DL, Sivendran R, Rose MD, Gierasch LM, Brodsky JL.

Mol Biol Cell. 2003 Aug;14(8):3437-48.

17.

The activity of yeast Hog1 MAPK is required during endoplasmic reticulum stress induced by tunicamycin exposure.

Torres-Quiroz F, García-Marqués S, Coria R, Randez-Gil F, Prieto JA.

J Biol Chem. 2010 Jun 25;285(26):20088-96. doi: 10.1074/jbc.M109.063578.

18.

Management of the endoplasmic reticulum stress by activation of the heat shock response in yeast.

Hou J, Tang H, Liu Z, Österlund T, Nielsen J, Petranovic D.

FEMS Yeast Res. 2014 May;14(3):481-94. doi: 10.1111/1567-1364.12125.

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