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Items: 1 to 20 of 102

1.

Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP).

Hurtley SM, Bole DG, Hoover-Litty H, Helenius A, Copeland CS.

J Cell Biol. 1989 Jun;108(6):2117-26.

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Epitope tagging of the human endoplasmic reticulum HSP70 protein, BiP, to facilitate analysis of BiP--substrate interactions.

Murray PJ, Watowich SS, Lodish HF, Young RA, Hilton DJ.

Anal Biochem. 1995 Aug 10;229(2):170-9.

PMID:
7485969
6.

Manipulating disulfide bond formation and protein folding in the endoplasmic reticulum.

Braakman I, Helenius J, Helenius A.

EMBO J. 1992 May;11(5):1717-22.

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Heavy chain binding protein (BiP/GRP78) and endoplasmin are exported from the endoplasmic reticulum in rat exocrine pancreatic cells, similar to protein disulfide-isomerase.

Takemoto H, Yoshimori T, Yamamoto A, Miyata Y, Yahara I, Inoue K, Tashiro Y.

Arch Biochem Biophys. 1992 Jul;296(1):129-36.

PMID:
1318687
13.

Assembly of influenza hemagglutinin trimers and its role in intracellular transport.

Copeland CS, Doms RW, Bolzau EM, Webster RG, Helenius A.

J Cell Biol. 1986 Oct;103(4):1179-91.

14.

Immunocytochemical localization of BiP to the rough endoplasmic reticulum: evidence for protein sorting by selective retention.

Bole DG, Dowin R, Doriaux M, Jamieson JD.

J Histochem Cytochem. 1989 Dec;37(12):1817-23.

PMID:
2685110
15.

Immunoglobulin heavy chain-binding protein binds to misfolded mutant insulin receptors with mutations in the extracellular domain.

Accili D, Kadowaki T, Kadowaki H, Mosthaf L, Ullrich A, Taylor SI.

J Biol Chem. 1992 Jan 5;267(1):586-90.

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HLA-B27 in transgenic rats forms disulfide-linked heavy chain oligomers and multimers that bind to the chaperone BiP.

Tran TM, Satumtira N, Dorris ML, May E, Wang A, Furuta E, Taurog JD.

J Immunol. 2004 Apr 15;172(8):5110-9.

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