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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2001-7-31
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pubmed:abstractText |
B144/LST1 is a gene encoded in the human major histocompatibility complex that produces multiple forms of alternatively spliced mRNA and encodes peptides fewer than 100 amino acids in length. B144/LST1 is strongly expressed in dendritic cells. Transfection of B144/LST1 into a variety of cells induces morphologic changes including the production of long, thin filopodia differing from those seen on transfection of a dominant active CDC42 gene. The structures are dynamically rearranging and sometimes connect one cell with another. The full effect of B144/LST1 protein on cell morphology requires the retention of at least one of the four cysteines of the peptide plus the presence of a hydrophobic segment in the protein, but requires only one of the two coding regions present in the terminal 3' exons.
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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/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/LST1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Lst1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha,
http://linkedlifedata.com/resource/pubmed/chemical/WASL protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Wasl protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Wiskott-Aldrich Syndrome Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/cdc42 GTP-Binding Protein
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0014-4827
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2001 Academic Press.
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
230-44
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11478849-Amino Acid Sequence,
pubmed-meshheading:11478849-Animals,
pubmed-meshheading:11478849-Blood Proteins,
pubmed-meshheading:11478849-COS Cells,
pubmed-meshheading:11478849-Cell Differentiation,
pubmed-meshheading:11478849-Cell Division,
pubmed-meshheading:11478849-Conserved Sequence,
pubmed-meshheading:11478849-Cytoplasmic Granules,
pubmed-meshheading:11478849-Dendritic Cells,
pubmed-meshheading:11478849-Evolution, Molecular,
pubmed-meshheading:11478849-Humans,
pubmed-meshheading:11478849-Immune System,
pubmed-meshheading:11478849-Major Histocompatibility Complex,
pubmed-meshheading:11478849-Membrane Proteins,
pubmed-meshheading:11478849-Mice,
pubmed-meshheading:11478849-Morphogenesis,
pubmed-meshheading:11478849-Multigene Family,
pubmed-meshheading:11478849-Nerve Tissue Proteins,
pubmed-meshheading:11478849-Pseudopodia,
pubmed-meshheading:11478849-Recombinant Proteins,
pubmed-meshheading:11478849-Tumor Necrosis Factor-alpha,
pubmed-meshheading:11478849-Wiskott-Aldrich Syndrome Protein, Neuronal,
pubmed-meshheading:11478849-cdc42 GTP-Binding Protein
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pubmed:year |
2001
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pubmed:articleTitle |
Functional analysis of B144/LST1: a gene in the tumor necrosis factor cluster that induces formation of long filopodia in eukaryotic cells.
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pubmed:affiliation |
Boyer Center for Molecular Medicine, Room 333, Department of Genetics, Yale School of Medicine, 295 Congress Avenue, New Haven, Connecticut 06536, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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