Functional analysis of disulfide linkages clustered within the amino terminus of human apolipoprotein B. (Q52529684)

2 May 2018

title

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

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2 May 2018

author

Roger S. McLeod

5

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author name string

Tran K

1

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Borén J

2

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Macri J

3

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Wang Y

4

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Avramoglu RK

6

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Adeli K

7

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Yao Z

8

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language of work or name

English

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publication date

1 March 1998

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2 May 2018

Journal of Biological Chemistry

published in

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volume

273

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issue

13

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page(s)

7244-7251

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Apolipoprotein B: Structural and Metabolic Heterogeneity

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The amino terminus of apolipoprotein B is necessary but not sufficient for microsomal triglyceride transfer protein responsiveness

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

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

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Folding of the amino-terminal domain of apolipoprotein B initiates microsomal triglyceride transfer protein-dependent lipid transfer to nascent very low density lipoprotein

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Inhibition of secretion of truncated apolipoproteins B by monomethylethanolamine is independent of the length of the apolipoprotein.

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

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Monoclonal antibody MB19 detects genetic polymorphism in human apolipoprotein B

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The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins

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Molecular chaperones involved in protein degradation in the endoplasmic reticulum: quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum

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Interactions between microsomal triglyceride transfer protein and apolipoprotein B within the endoplasmic reticulum in a heterologous expression system.

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

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Posttranslational folding of vesicular stomatitis virus G protein in the ER: involvement of noncovalent and covalent complexes

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The enzymatic and non-enzymatic roles of protein-disulfide isomerase in apolipoprotein B secretion

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apoB-100 has a pentapartite structure composed of three amphipathic alpha-helical domains alternating with two amphipathic beta-strand domains. Detection by the computer program LOCATE.

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Apolipoprotein B sequence requirements for hepatic very low density lipoprotein assembly. Evidence that hydrophobic sequences within apolipoprotein B48 mediate lipid recruitment

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Normal activity of microsomal triglyceride transfer protein is required for the oleate-induced secretion of very low density lipoproteins containing apolipoprotein B from McA-RH7777 cells

21 January 2018

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Ubiquitin-proteasome pathway mediates intracellular degradation of apolipoprotein B

21 January 2018

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The degradation of apolipoprotein B100 is mediated by the ubiquitin-proteasome pathway and involves heat shock protein 70

21 January 2018

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Protein disulfide isomerase and newly synthesized procollagen chains form higher-order structures in the lumen of the endoplasmic reticulum

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.13.7244

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2 May 2018

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2 May 2018