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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0020792,
umls-concept:C0031689,
umls-concept:C0031715,
umls-concept:C0086418,
umls-concept:C0108555,
umls-concept:C0178539,
umls-concept:C0185117,
umls-concept:C0205145,
umls-concept:C0521009,
umls-concept:C0521026,
umls-concept:C0521346,
umls-concept:C2911684
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pubmed:issue |
1
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pubmed:dateCreated |
1994-12-6
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pubmed:abstractText |
The phosphoprotein P gene of human respiratory syncytial virus has been cloned and the protein expressed in Escherichia coli. The expressed protein was soluble, unphosphorylated, and constituted approximately 10% of the total bacterial protein. Electrophoretic and antigenic analyses demonstrated the identity of the recombinant protein with viral P protein and P protein synthesized in reticulocyte lysates. Purified recombinant P protein was efficiently phosphorylated in vitro by purified native as well as recombinant casein kinase II (CKII) or by the CKII activity in uninfected cell extracts. Through deletions and site-directed mutagenesis, the site of CKII phosphorylation was mapped to a single serine residue (Ser237) near the C-terminal end of the P protein.
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pubmed:grant |
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pubmed:commentsCorrections |
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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/Casein Kinase II,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/HN Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphates,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/attachment protein G
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0042-6822
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
205
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
93-103
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7975241-Amino Acid Sequence,
pubmed-meshheading:7975241-Base Sequence,
pubmed-meshheading:7975241-Casein Kinase II,
pubmed-meshheading:7975241-Catalysis,
pubmed-meshheading:7975241-Cloning, Molecular,
pubmed-meshheading:7975241-DNA Primers,
pubmed-meshheading:7975241-Escherichia coli,
pubmed-meshheading:7975241-HN Protein,
pubmed-meshheading:7975241-Humans,
pubmed-meshheading:7975241-Molecular Sequence Data,
pubmed-meshheading:7975241-Phosphates,
pubmed-meshheading:7975241-Phosphoric Monoester Hydrolases,
pubmed-meshheading:7975241-Phosphorylation,
pubmed-meshheading:7975241-Protein-Serine-Threonine Kinases,
pubmed-meshheading:7975241-Recombinant Proteins,
pubmed-meshheading:7975241-Respiratory Syncytial Viruses,
pubmed-meshheading:7975241-Serine,
pubmed-meshheading:7975241-Tumor Cells, Cultured,
pubmed-meshheading:7975241-Viral Envelope Proteins,
pubmed-meshheading:7975241-Viral Proteins
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pubmed:year |
1994
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pubmed:articleTitle |
Bacterial expression of human respiratory syncytial viral phosphoprotein P and identification of Ser237 as the site of phosphorylation by cellular casein kinase II.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, College of Medicine, University of South Alabama, Mobile 36688-0002.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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