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Chaperone function of calnexin for the folding intermediate of gp80, the major secretory protein in MDCK cells. Regulation by redox state and ATP.

Data up to Jan 2025

Published1994
Citations65
References45

Total Citations Per Year

Abstract

References (45)

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1992 • 318 citations

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1991 • 312 citations

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1992 • 296 citations

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1992 • 286 citations

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1983 • 204 citations

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1993 • 203 citations

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1987 • 201 citations

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1992 • 187 citations

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1992 • 184 citations

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1990 • 180 citations

Cyclosporin A inhibits an initial step in folding of transferrin within the endoplasmic reticulum

1991 • 168 citations

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1993 • 139 citations

Conformational changes associated with proteolytic processing of presecretory proteins allow glutathione-catalyzed formation of native disulfide bonds.

1982 • 125 citations

Exocytotic pathways exist to both the apical and the basolateral cell surface of the polarized epithelial cell MDCK

1985 • 121 citations

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1993 • 113 citations

Identification of a supernova remnant coincident with the soft γ-ray repeater SGR1806 - 20

1993 • 110 citations

The p88 molecular chaperone is identical to the endoplasmic reticulum membrane protein, calnexin.

1992 • 110 citations

BIP associates with newly synthesized subunits of the mouse muscle nicotinic receptor.

1991 • 108 citations

Primary structure and characterization of an Arabidopsis thaliana calnexin-like protein.

1993 • 104 citations

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1993 • 86 citations

[34] Protein analysis using high-resolution two-dimensional polyacrylamide gel electrophoresis

1990 • 81 citations

Identification of the region on the class I histocompatibility molecule that interacts with the molecular chaperone, p88 (calnexin, IP90).

1993 • 77 citations

The endoplasmic reticulum of purkinje neuron body and dendrites: Molecular identity and specializations for Ca2+ transport

1992 • 65 citations

BiP forms stable complexes with unassembled subunits of the acetylcholine receptor in transfected COS cells and in C2 muscle cells

1992 • 58 citations

Purification of a 90-kDa protein (Band VII) from cardiac sarcoplasmic reticulum. Identification as calnexin and localization of casein kinase II phosphorylation sites.

1993 • 50 citations

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1990 • 41 citations

Proteolytic processing of presecretory proteins is required for development of biological activities in pancreatic exocrine proteins.

1983 • 38 citations

CNE1, a Saccharomyces cerevisiae Homologue of the Genes Encoding Mammalian Calnexin and Calreticulin

1993 • 33 citations

Identification of proteins according to biological activity following separation by two-dimensional isoelectric focusing/sodium dodecyl sulfate gel electrophoresis: Analysis of human exocrine pancreatic proteins

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Chaperone function of calnexin for the folding intermediate of gp80, the major secretory… (1994) – Journal of Biological Chemistry | Metascience Observatory Explorer