Source:http://linkedlifedata.com/resource/pubmed/id/20967265
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2010-10-22
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pubmed:abstractText |
Coat protein complex I (COPI) vesicles, coated by seven coatomer subunits, are mainly responsible for Golgi-to-ER transport. Silkworm posterior silkgland (PSG), a highly differentiated secretory tissue, secretes fibroin for silk production, but many physiological processes in the PSG cells await further investigation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
1932-6203
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
e13252
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pubmed:meshHeading |
pubmed-meshheading:20967265-Animals,
pubmed-meshheading:20967265-Bombyx,
pubmed-meshheading:20967265-Cloning, Molecular,
pubmed-meshheading:20967265-Insect Proteins,
pubmed-meshheading:20967265-Phylogeny,
pubmed-meshheading:20967265-Polymerase Chain Reaction,
pubmed-meshheading:20967265-RNA, Messenger,
pubmed-meshheading:20967265-Subcellular Fractions
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pubmed:year |
2010
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pubmed:articleTitle |
Silkworm coatomers and their role in tube expansion of posterior silkgland.
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pubmed:affiliation |
The Key Laboratory of Cell Proliferation and Differentiation of Ministry of Education, College of Life Sciences, Peking University, Beijing, China.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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