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Cited by 460

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Complexity in the Secretory Pathway: The Assembly and Secretion of Apolipoprotein B-containing Lipoproteins

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Fisher, Edward A., Ginsberg, Henry N.·2002·Journal of Biological Chemistry

Abstract

Apolipoprotein B100 (apoB100) is expressed primarily in mammalian liver. It has 4536 amino acids, 25 cysteines (16 of which are in intramolecular disulfide bonds), and 20 N-linked glycosylation sites. A smaller form, apoB48, is expressed in mammalian intestine and in the livers of some non-human mammals. ApoB48 results from a post-transcriptional modification of the apoB mRNA at codon 2153 that converts a glutamine codon to a stop codon at ∼48% of the full-length coding sequence. Both forms of apoB have a complex structure that includes a globular amphipathic NH2 domain spanning the first 15–20% (using B100 as a standard length) of the polypeptide followed by an extended hydrophobic β-sheet domain from about 20 to 48%.

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Metadata

Authors
Fisher, E. A., & Ginsberg, H. N.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2002-05
Volume
277
Issue
20
Pages
17377-17380
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2080508595
Cited by
460
References
2
FWCI
25.71
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Complexity in the Secretory Pathway: The Assembly and Secretion of Apolipoprotein B-containing Lipoproteins. https://app.cochat.ai/papers/10.1074/jbc.r100068200
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Fisher, E. A., & Ginsberg, H. N. (2002). Complexity in the Secretory Pathway: The Assembly and Secretion of Apolipoprotein B-containing Lipoproteins. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.r100068200

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.