pubmed-article:9740790 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9740790 | lifeskim:mentions | umls-concept:C0318798 | lld:lifeskim |
pubmed-article:9740790 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
pubmed-article:9740790 | lifeskim:mentions | umls-concept:C0012940 | lld:lifeskim |
pubmed-article:9740790 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:9740790 | pubmed:dateCreated | 1998-10-13 | lld:pubmed |
pubmed-article:9740790 | pubmed:abstractText | The simian parainfluenza virus 5 (SV5) V/P gene encodes two proteins: V and the phosphoprotein P. The V and P proteins are amino coterminal for 164 residues, but they have unique carboxyl termini. The unique carboxyl terminus of V contains seven cysteine residues, resembles a zinc finger, and binds two atoms of zinc. In a glutathione-S-transferase (GST)-fusion protein selection of cell lysate assay, the GST-V protein was found to interact with the 127-kDa subunit (DDB1) of the damage-specific DNA binding protein (DDB) [also known as UV-damaged DNA binding protein (UV-DDB), xeroderma pigmentosum group E binding factor (XPE-BF), and the hepatitis B virus X-associated protein 1 (XAP-1)]. A reciprocal GST-DDB1 fusion protein selection assay of SV5-infected cell lysates showed that DDB1 and V interact, and it was found that V and DDB1 could be coimmunoprecipitated from SV5-infected cells or from cells expressing V and DDB1 using the vaccinia virus T7 expression system. The interaction of V and DDB1 involves the carboxyl-terminal domain of V in that either deletion of the V carboxyl-terminal domain or substitution of the cysteine residues (C189, C193, C205, C207, C210, C214, and C217) in the zinc-binding domain with alanine was able to disrupt binding to DDB1. The V proteins of the mumps virus, human parainfluenza virus 2 (hPIV2), and measles virus have also been found to interact with DDB1 in GST-fusion protein selection assays using in vitro transcribed and translated DDB1. | lld:pubmed |
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pubmed-article:9740790 | pubmed:language | eng | lld:pubmed |
pubmed-article:9740790 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9740790 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9740790 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9740790 | pubmed:month | Sep | lld:pubmed |
pubmed-article:9740790 | pubmed:issn | 0042-6822 | lld:pubmed |
pubmed-article:9740790 | pubmed:author | pubmed-author:LambR ARA | lld:pubmed |
pubmed-article:9740790 | pubmed:author | pubmed-author:RichardsonC... | lld:pubmed |
pubmed-article:9740790 | pubmed:author | pubmed-author:LinG YGY | lld:pubmed |
pubmed-article:9740790 | pubmed:author | pubmed-author:PatersonR GRG | lld:pubmed |
pubmed-article:9740790 | pubmed:copyrightInfo | Copyright 1998 Academic Press. | lld:pubmed |
pubmed-article:9740790 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9740790 | pubmed:day | 15 | lld:pubmed |
pubmed-article:9740790 | pubmed:volume | 249 | lld:pubmed |
pubmed-article:9740790 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9740790 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9740790 | pubmed:pagination | 189-200 | lld:pubmed |
pubmed-article:9740790 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:9740790 | pubmed:meshHeading | pubmed-meshheading:9740790-... | lld:pubmed |
pubmed-article:9740790 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9740790 | pubmed:articleTitle | The V protein of the paramyxovirus SV5 interacts with damage-specific DNA binding protein. | lld:pubmed |
pubmed-article:9740790 | pubmed:affiliation | Department of Biochemistry, Molecular Biology and Cell Biology, Howard Hughes Medical Institute, Northwestern University, 2153 North Campus Drive, Evanston, Illinois, 60208-3500, USA. | lld:pubmed |
pubmed-article:9740790 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9740790 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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