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Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the endoplasmic reticulum

Data up to Jan 2025

Published1994
Citations430
References27

Total Citations Per Year

Abstract

References (27)

Protein folding in the cell

1992 • 4,138 citations

An hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein

1986 • 1,457 citations

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding

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Peptide-binding specificity of the molecular chaperone BiP

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1993 • 650 citations

Hsp90 chaperones protein folding in vitro

1992 • 514 citations

Coordinated regulation of a set of genes by glucose and calcium ionophores in mammalian cells

1987 • 442 citations

ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (GRP94).

1987 • 294 citations

Tumor rejection antigen gp96/grp94 is an ATPase: implications for protein folding and antigen presentation.

1993 • 293 citations

Hsp90 chaperonins possess ATPase activity and bind heat shock transcription factors and peptidyl prolyl isomerases.

1993 • 245 citations

The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains.

1992 • 243 citations

Endoplasmic reticulum contains a common, abundant calcium-binding glycoprotein, endoplasmin

1986 • 236 citations

Structural and functional reconstitution of the glucocorticoid receptor-hsp90 complex.

1990 • 190 citations

Interaction of BiP with newly synthesized immunoglobulin light chain molecules: cycles of sequential binding and release.

1992 • 187 citations

The 170-kDa glucose-regulated stress protein is an endoplasmic reticulum protein that binds immunoglobulin.

1993 • 163 citations

The glucose-regulated protein grp94 is related to heat shock protein hsp90

1987 • 161 citations

HLA-DR associates with specific stress proteins and is retained in the endoplasmic reticulum in invariant chain negative cells.

1992 • 148 citations

Translocation of ATP into the lumen of rough endoplasmic reticulum-derived vesicles and its binding to luminal proteins including BiP (GRP 78) and GRP 94.

1992 • 131 citations

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1983 • 128 citations

Intracellular immunoglobulin chain synthesis in non-secreting variants of a mouse myeloma: Detection of inactive light-chain messenger RNA

1974 • 118 citations

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1992 • 101 citations

Secretion of a λ2 immunoglobulin chain is prevented by a single amino acid substitution in its variable region

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A mutation in the ectodomain of herpes simplex virus 1 glycoprotein B causes defective processing and retention in the endoplasmic reticulum

1991 • 52 citations

Monoclonal Antibodies Specific for Variable and Constant Domains of Murine λ Chains

1989 • 18 citations

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Sequential interaction of the chaperones BiP and GRP94 with immunoglobulin chains in the… (1994) – Nature | Metascience Observatory Explorer