| pubmed-article:19234474 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19234474 | lifeskim:mentions | umls-concept:C0034865 | lld:lifeskim |
| pubmed-article:19234474 | lifeskim:mentions | umls-concept:C1708726 | lld:lifeskim |
| pubmed-article:19234474 | lifeskim:mentions | umls-concept:C0010531 | lld:lifeskim |
| pubmed-article:19234474 | lifeskim:mentions | umls-concept:C0021027 | lld:lifeskim |
| pubmed-article:19234474 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
| pubmed-article:19234474 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:19234474 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:19234474 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:19234474 | pubmed:dateCreated | 2009-3-19 | lld:pubmed |
| pubmed-article:19234474 | pubmed:abstractText | Immunoglobulin class-switch recombination (CSR) requires activation-induced cytidine deaminase (AID). Deamination of DNA by AID in transcribed switch (S) regions leads to double-stranded breaks in DNA that serve as obligatory CSR intermediates. Here we demonstrate that the catalytic and regulatory subunits of protein kinase A (PKA) were specifically recruited to S regions to promote the localized phosphorylation of AID, which led to binding of replication protein A and subsequent propagation of the CSR cascade. Accordingly, inactivation of PKA resulted in considerable disruption of CSR because of decreased AID phosphorylation and recruitment of replication protein A to S regions. We propose that PKA nucleates the formation of active AID complexes specifically on S regions to generate the high density of DNA lesions required for CSR. | lld:pubmed |
| pubmed-article:19234474 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19234474 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19234474 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19234474 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19234474 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19234474 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19234474 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19234474 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19234474 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19234474 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19234474 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19234474 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:19234474 | pubmed:issn | 1529-2916 | lld:pubmed |
| pubmed-article:19234474 | pubmed:author | pubmed-author:VuongBao QBQ | lld:pubmed |
| pubmed-article:19234474 | pubmed:author | pubmed-author:McKnightG... | lld:pubmed |
| pubmed-article:19234474 | pubmed:author | pubmed-author:ChaudhuriJaya... | lld:pubmed |
| pubmed-article:19234474 | pubmed:author | pubmed-author:LeeMieunM | lld:pubmed |
| pubmed-article:19234474 | pubmed:author | pubmed-author:KabirShaheenS | lld:pubmed |
| pubmed-article:19234474 | pubmed:author | pubmed-author:IrimiaCristin... | lld:pubmed |
| pubmed-article:19234474 | pubmed:author | pubmed-author:MacchiaruloSt... | lld:pubmed |
| pubmed-article:19234474 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19234474 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:19234474 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19234474 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19234474 | pubmed:pagination | 420-6 | lld:pubmed |
| pubmed-article:19234474 | pubmed:dateRevised | 2011-5-10 | lld:pubmed |
| pubmed-article:19234474 | pubmed:meshHeading | pubmed-meshheading:19234474... | lld:pubmed |
| pubmed-article:19234474 | pubmed:meshHeading | pubmed-meshheading:19234474... | lld:pubmed |
| pubmed-article:19234474 | pubmed:meshHeading | pubmed-meshheading:19234474... | lld:pubmed |
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| pubmed-article:19234474 | pubmed:meshHeading | pubmed-meshheading:19234474... | lld:pubmed |
| pubmed-article:19234474 | pubmed:meshHeading | pubmed-meshheading:19234474... | lld:pubmed |
| pubmed-article:19234474 | pubmed:meshHeading | pubmed-meshheading:19234474... | lld:pubmed |
| pubmed-article:19234474 | pubmed:meshHeading | pubmed-meshheading:19234474... | lld:pubmed |
| pubmed-article:19234474 | pubmed:meshHeading | pubmed-meshheading:19234474... | lld:pubmed |
| pubmed-article:19234474 | pubmed:meshHeading | pubmed-meshheading:19234474... | lld:pubmed |
| pubmed-article:19234474 | pubmed:meshHeading | pubmed-meshheading:19234474... | lld:pubmed |
| pubmed-article:19234474 | pubmed:meshHeading | pubmed-meshheading:19234474... | lld:pubmed |
| pubmed-article:19234474 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19234474 | pubmed:articleTitle | Specific recruitment of protein kinase A to the immunoglobulin locus regulates class-switch recombination. | lld:pubmed |
| pubmed-article:19234474 | pubmed:affiliation | Memorial Sloan-Kettering Cancer Center, New York, New York, USA. | lld:pubmed |
| pubmed-article:19234474 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19234474 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:19234474 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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