Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state (Q28278880)

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English	Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state	scientific article

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scholarly article

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Multiple molecular chaperones interact with apolipoprotein B during its maturation. The network of endoplasmic reticulum-resident chaperones (ERp72, GRP94, calreticulin, and BiP) interacts with apolipoprotein b regardless of its lipidation state (English)

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endoplasmic reticulum

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molecular chaperones

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Haya Herscovitz

2

object named as

H Herscovitz

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author name string

K M Linnik

1

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language of work or name

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publication date

14 August 1998

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Journal of Biological Chemistry

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273

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33

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21368-73

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Role of lipid synthesis, chaperone proteins and proteasomes in the assembly and secretion of apoprotein B-containing lipoproteins from cultured liver cells

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Molecular chaperones in cellular protein folding

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Protein folding in the cell

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

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Microsomal triglyceride transfer protein

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

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Demonstration of a physical interaction between microsomal triglyceride transfer protein and apolipoprotein B during the assembly of ApoB-containing lipoproteins

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Association of folding intermediates of glycoproteins with calnexin during protein maturation

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

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Apolipoprotein B is intracellularly associated with an ER-60 protease homologue in HepG2 cells

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Molecular cloning of the human glucose-regulated protein ERp57/GRP58, a thiol-dependent reductase. Identification of its secretory form and inducible expression by the oncogenic transformation

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21 January 2018

Interaction of the thiol-dependent reductase ERp57 with nascent glycoproteins

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

BiP binding sequences in antibodies.

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

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Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP.

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

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Murine mammary-derived cells secrete the N-terminal 41% of human apolipoprotein B on high density lipoprotein-sized lipoproteins containing a triacylglycerol-rich core

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Expression, secretion, and lipid-binding characterization of the N-terminal 17% of apolipoprotein B

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

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1 reference

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Multiple molecular chaperones complex with misfolded large oligomeric glycoproteins in the endoplasmic reticulum

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

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

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Novel covalent chaperone complexes associated with human chorionic gonadotropin beta subunit folding intermediates

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

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Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

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The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

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Participation of a novel 88-kD protein in the biogenesis of murine class I histocompatibility molecules

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Calnexin and BiP act as sequential molecular chaperones during thyroglobulin folding in the endoplasmic reticulum

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Interaction of calreticulin with protein disulfide isomerase

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Degradation and endoplasmic reticulum retention of unassembled alpha- and beta-subunits of Na,K-ATPase correlate with interaction of BiP.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Pharmacologic shifting of a balance between protein refolding and degradation mediated by Hsp90

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https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Isolation and characterization of sulfhydryl and disulfide peptides of human apolipoprotein B-100.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Functional analysis of disulfide linkages clustered within the amino terminus of human apolipoprotein B.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.273.33.21368

21 January 2018

Identifiers

10.1074/JBC.273.33.21368

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