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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
2002-10-17
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pubmed:abstractText |
Differences in protein solubility appear to play an important role in lumenal protein trafficking through Golgi/post-Golgi compartments. Recent advances indicate that multimeric protein assembly is one of the factors regulating the efficiency of protein storage within secretory granules, by mechanisms that, with slight modification, might be considered to represent the culmination of a process of Golgi cisternal maturation.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
|
|
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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|
pubmed:issn |
0955-0674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
448-53
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12383795-Animals,
pubmed-meshheading:12383795-Carrier Proteins,
pubmed-meshheading:12383795-Cell Compartmentation,
pubmed-meshheading:12383795-Cytoplasmic Granules,
pubmed-meshheading:12383795-Golgi Apparatus,
pubmed-meshheading:12383795-Humans,
pubmed-meshheading:12383795-Intracellular Membranes,
pubmed-meshheading:12383795-Models, Biological,
pubmed-meshheading:12383795-Protein Precursors,
pubmed-meshheading:12383795-Protein Processing, Post-Translational,
pubmed-meshheading:12383795-Protein Transport,
pubmed-meshheading:12383795-Proteins,
pubmed-meshheading:12383795-Solubility,
pubmed-meshheading:12383795-trans-Golgi Network
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pubmed:year |
2002
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pubmed:articleTitle |
Lumenal protein multimerization in the distal secretory pathway/secretory granules.
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pubmed:affiliation |
Division of Endocrinology/Diabetes Center, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA. arvan@aecom.yu.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
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