Source:http://linkedlifedata.com/resource/pubmed/id/21738521
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
2011-7-8
|
pubmed:abstractText |
Pin 1 is an enzyme that specifically catalyzes the cis-trans isomerization of phosphorylated serine/threonine-proline (pSer/Thr-Pro) motif in its substrate proteins. Recent studies demonstrate that stability of several viral proteins is regulated by phosphorylation-dependent prolyl-isomerization by a host factor Pin1. Pin1 is now positioned as an important modulator of the molecular crosstalk between virus and host cells and could be a unique target for anti-virus therapy. This new type of post-translational modification by Pin1 might be involved in the regulation of other viral proteins.
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/21738521-12571275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21738521-17383430,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21738521-17876319,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21738521-17878917,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21738521-19158244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21738521-19338781,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21738521-20173753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21738521-7834742
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:status |
PubMed-not-MEDLINE
|
pubmed:issn |
1664-302X
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:volume |
1
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
107
|
pubmed:dateRevised |
2011-8-1
|
pubmed:year |
2010
|
pubmed:articleTitle |
Pinning down viral proteins: a new prototype for virus-host cell interaction.
|
pubmed:affiliation |
Department of Microbiology, Yokohama City University School of Medicine Yokohama, Kanagawa, Japan.
|
pubmed:publicationType |
Journal Article
|