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BiP and Calreticulin Form an Abundant Complex That Is Independent of Endoplasmic Reticulum Stress

Data up to Jan 2025

Published1998
Citations77
References48

Total Citations Per Year

Abstract

References (48)

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Interconversion of three differentially modified and assembled forms of BiP.

1992 • 180 citations

Misfolding and aggregation of newly synthesized proteins in the endoplasmic reticulum.

1992 • 177 citations

Protein quality control along the route to the plant vacuole.

1997 • 172 citations

N-linked oligosaccharides are necessary and sufficient for association of glycosylated forms of bovine RNase with calnexin and calreticulin.

1996 • 149 citations

Calreticulin Interacts with Newly Synthesized Human Immunodeficiency Virus Type 1 Envelope Glycoprotein, Suggesting a Chaperone Function Similar to That of Calnexin

1996 • 134 citations

Endoplasmic Reticulum Form of Calreticulin Modulates Glucocorticoid-sensitive Gene Expression

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1993 • 116 citations

Identification and characterization of cDNA clones encoding plant calreticulin in barley.

1994 • 106 citations

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1992 • 99 citations

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1987 • 90 citations

Binding of BiP to an assembly‐defective protein in plant cells

1994 • 88 citations

Isolation of a full-length cDNA encoding calreticulin from a PCR library of in vitro zygotes of maize

1996 • 85 citations

A pathogen-induced gene of barley encodes a HSP90 homologue showing striking similarity to vertebrate forms resident in the endoplasmic reticulum

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1991 • 82 citations

The Binding Protein Associates with Monomeric Phaseolin

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Deleted Work

1955 • 0 citations

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BiP and Calreticulin Form an Abundant Complex That Is Independent of Endoplasmic… (1998) – The Plant Cell | Metascience Observatory Explorer