Source:http://linkedlifedata.com/resource/pubmed/id/11208111
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2001-3-6
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pubmed:abstractText |
In order to determine if the sequence patterns known to specify internalization represent the majority of possible internalization signals, we identified random sequences capable of causing a reporter protein to be internalized at least several-fold faster than the rate of non-selective internalization of membrane by clathrin-coated pits. A library of influenza hemagglutinin (HA) proteins, bearing short random sequences in place of the wild-type cytoplasmic domain, was prepared in recombinant SV40 virus. The library was expressed and screened for HAs that could internalize anti-HA antibody from the medium. The cytoplasmic sequences of the selected proteins were determined. From a small sample of sequences we detected several that did not resemble those previously identified. The known internalization signals must represent only a subset of the sequences that can serve as internalization signals.
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pubmed:grant | |
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:month |
Mar
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pubmed:issn |
1398-9219
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
282-90
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11208111-Amino Acid Motifs,
pubmed-meshheading:11208111-Amino Acid Sequence,
pubmed-meshheading:11208111-Amino Acid Substitution,
pubmed-meshheading:11208111-Animals,
pubmed-meshheading:11208111-Cell Line,
pubmed-meshheading:11208111-Cercopithecus aethiops,
pubmed-meshheading:11208111-Clathrin-Coated Vesicles,
pubmed-meshheading:11208111-Codon,
pubmed-meshheading:11208111-Endocytosis,
pubmed-meshheading:11208111-Endosomes,
pubmed-meshheading:11208111-Fibroblasts,
pubmed-meshheading:11208111-Gene Library,
pubmed-meshheading:11208111-Genes, Reporter,
pubmed-meshheading:11208111-Hemagglutinin Glycoproteins, Influenza Virus,
pubmed-meshheading:11208111-Influenza A virus,
pubmed-meshheading:11208111-Molecular Sequence Data,
pubmed-meshheading:11208111-Mutagenesis, Site-Directed,
pubmed-meshheading:11208111-Protein Structure, Tertiary,
pubmed-meshheading:11208111-Protein Transport,
pubmed-meshheading:11208111-Random Allocation,
pubmed-meshheading:11208111-Recombinant Fusion Proteins
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pubmed:year |
2000
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pubmed:articleTitle |
A screen of random sequences for those that alter the trafficking of the influenza virus hemagglutinin in vivo.
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pubmed:affiliation |
Department of Biochemistry, University of Texas Southwestern Medical Center at Dallas, Dallas, TX 75235-9038, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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