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The endoplasmic reticulum as a protein-folding compartment

Data up to Jan 2025

Published1992
Citations296
References41

Total Citations Per Year

Abstract

References (41)

Protein folding in the cell

1992 • 4,138 citations

Speculations on the functions of the major heat shock and glucose-regulated proteins

1986 • 1,574 citations

MOLECULAR CHAPERONES

1991 • 1,089 citations

Protein Oligomerization in the Endoplasmic Reticulum

1989 • 993 citations

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

1992 • 965 citations

Experimental and Theoretical Aspects of Protein Folding

1975 • 965 citations

Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells

1989 • 884 citations

Human cyclins A and B1 are differentially located in the cell and undergo cell cycle-dependent nuclear transport.

1991 • 858 citations

Immunoglobulin heavy chain binding protein

1983 • 849 citations

KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene

1989 • 684 citations

SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane.

1991 • 544 citations

Protein disulfide isomerase: Multiple roles in the modification of nascent secretory proteins

1989 • 466 citations

Glycoproteins: what are the sugar chains for?

1989 • 459 citations

Loss of BiP/GRP78 function blocks translocation of secretory proteins in yeast.

1990 • 435 citations

Protein folding: local structures, domains, subunits, and assemblies

1991 • 432 citations

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

1992 • 405 citations

Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein.

1987 • 343 citations

Defective co-translational formation of disulphide bonds in protein disulphide-isomerase-deficient microsomes

1988 • 330 citations

Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum.

1992 • 318 citations

Folding of influenza hemagglutinin in the endoplasmic reticulum.

1991 • 318 citations

Cyclosporin A slows collagen triple-helix formation in vivo: indirect evidence for a physiologic role of peptidyl-prolyl cis-trans-isomerase.

1991 • 313 citations

A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein.

1989 • 296 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

Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum

1992 • 286 citations

The cyclophilin homolog ninaA is a tissue-specific integral membrane protein required for the proper synthesis of a subset of Drosophila rhodopsins

1991 • 271 citations

ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase.

1990 • 254 citations

Developmental regulation of IgM secretion: The role of the carboxy-terminal cysteine

1990 • 245 citations

Perturbation of cellular calcium blocks exit of secretory proteins from the rough endoplasmic reticulum.

1990 • 229 citations

A Peptide Sequence Confers Retention and Rapid Degradation in the Endoplasmic Reticulum

1990 • 219 citations

Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiP.

1991 • 210 citations

[5]Disulfide bonds as probes of protein folding pathways

1986 • 203 citations

Post‐Translational Processing of Procollagens

1985 • 200 citations

Formation of an intrachain disulfide bond on nascent immunoglobulin light chains.

1979 • 199 citations

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

1992 • 177 citations

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

1991 • 168 citations

Biochemical characterization of the 94- and 78-kilodalton glucose-regulated proteins in hamster fibroblasts.

1984 • 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

The biosynthesis of rat serum albumin. In vivo studies on the formation of the disulfide bonds.

1982 • 124 citations

Formation and intracellular transport of a heterodimeric viral spike protein complex.

1991 • 89 citations

Folding and assembly of newly synthesized thyroglobulin occurs in a pre-Golgi compartment

1991 • 87 citations

An internalized amino-terminal signal sequence retains full activity in vivo but not in vitro.

1987 • 24 citations

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