rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1990-3-15
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pubmed:abstractText |
Several investigations have demonstrated the ability of synthetic peptides homologous to the nuclear transport signal of simian virus 40 large T antigen to induce the nuclear transport of nonnuclear carrier proteins. To determine the generality of peptide-induced transport, six peptides with sequences derived from four previously identified nuclear transport signals were synthesized and examined for their ability to induce the transport of mouse immunoglobulin G following microinjection into the cytoplasm of mammalian cells. Peptides containing transport signals from simian virus 40 T antigen, Xenopus nucleoplasmin, and adenovirus E1A proteins were highly efficient at peptide-induced transport, while a peptide homologous to yeast MAT alpha 2 protein was incapable of inducing transport. A short nucleoplasmin peptide that contained only the basic amino acid domain was capable of inducing transport but yielded a much slower rate of transport than a long nucleoplasmin peptide encompassing the previously identified minimal transport signal. The short nucleoplasmin signal exhibited a greater capacity for transport than a peptide homologous to the cytoplasmic mutant T antigen signal when conjugates with a low number of signals coupled per carrier protein were examined. However, the short nucleoplasmin peptide was only marginally more effective than the T antigen mutant peptide when conjugates with a high number of signals coupled per carrier protein were examined.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adenovirus Early Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Polyomavirus Transforming,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Homeodomain Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleoplasmins,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0014-4827
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
186
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
32-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:2137089-Adenovirus Early Proteins,
pubmed-meshheading:2137089-Amino Acid Sequence,
pubmed-meshheading:2137089-Antigens, Polyomavirus Transforming,
pubmed-meshheading:2137089-Biological Transport,
pubmed-meshheading:2137089-Carrier Proteins,
pubmed-meshheading:2137089-Cell Nucleus,
pubmed-meshheading:2137089-Fungal Proteins,
pubmed-meshheading:2137089-Homeodomain Proteins,
pubmed-meshheading:2137089-Microinjections,
pubmed-meshheading:2137089-Molecular Sequence Data,
pubmed-meshheading:2137089-Nuclear Proteins,
pubmed-meshheading:2137089-Nucleoplasmins,
pubmed-meshheading:2137089-Oncogene Proteins, Viral,
pubmed-meshheading:2137089-Peptides,
pubmed-meshheading:2137089-Phosphoproteins,
pubmed-meshheading:2137089-Protein Sorting Signals,
pubmed-meshheading:2137089-Repressor Proteins,
pubmed-meshheading:2137089-Signal Transduction
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pubmed:year |
1990
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pubmed:articleTitle |
Comparison of diverse transport signals in synthetic peptide-induced nuclear transport.
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pubmed:affiliation |
Department of Virology and Immunology, Southwest Foundation for Biomedical Research, San Antonio, Texas 78284.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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