pubmed-article:9873052 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9873052 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:9873052 | lifeskim:mentions | umls-concept:C1136027 | lld:lifeskim |
pubmed-article:9873052 | lifeskim:mentions | umls-concept:C1148673 | lld:lifeskim |
pubmed-article:9873052 | lifeskim:mentions | umls-concept:C0069139 | lld:lifeskim |
pubmed-article:9873052 | lifeskim:mentions | umls-concept:C1512667 | lld:lifeskim |
pubmed-article:9873052 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
pubmed-article:9873052 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:9873052 | pubmed:dateCreated | 1999-2-5 | lld:pubmed |
pubmed-article:9873052 | pubmed:abstractText | The immunoglobulin heavy chain switch regions contain multiple runs of guanines on the top (nontemplate) DNA strand. Here we show that LR1, a B cell-specific, duplex DNA binding factor, binds tightly and specifically to synthetic oligonucleotides containing G-G base pairs (KD </= 0.25 nM). LR1 also binds to single-stranded G-rich sequences (KD approximately 10 nM). The two subunits of LR1, nucleolin and hnRNP D, bind with high affinity to G4 DNA (KD = 0.4 and 0.5 nM, respectively). LR1 therefore contains two independent G4 DNA binding domains. We propose that LR1 binds with G-G-paired structures that form during the transcription of the S regions that is prerequisite to recombination in vivo. Interactions of donor and acceptor S regions with subunits of the LR1 could then juxtapose the switch regions for recombination. | lld:pubmed |
pubmed-article:9873052 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873052 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873052 | pubmed:language | eng | lld:pubmed |
pubmed-article:9873052 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873052 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9873052 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873052 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873052 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873052 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873052 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873052 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873052 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873052 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873052 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873052 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873052 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873052 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9873052 | pubmed:month | Jan | lld:pubmed |
pubmed-article:9873052 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:9873052 | pubmed:author | pubmed-author:SuhBB | lld:pubmed |
pubmed-article:9873052 | pubmed:author | pubmed-author:MaizelsNN | lld:pubmed |
pubmed-article:9873052 | pubmed:author | pubmed-author:DempseyL ALA | lld:pubmed |
pubmed-article:9873052 | pubmed:author | pubmed-author:HanakahiL ALA | lld:pubmed |
pubmed-article:9873052 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9873052 | pubmed:day | 8 | lld:pubmed |
pubmed-article:9873052 | pubmed:volume | 274 | lld:pubmed |
pubmed-article:9873052 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9873052 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9873052 | pubmed:pagination | 1066-71 | lld:pubmed |
pubmed-article:9873052 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:9873052 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:9873052 | pubmed:articleTitle | G4 DNA binding by LR1 and its subunits, nucleolin and hnRNP D, A role for G-G pairing in immunoglobulin switch recombination. | lld:pubmed |
pubmed-article:9873052 | pubmed:affiliation | Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114, USA. | lld:pubmed |
pubmed-article:9873052 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9873052 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9873052 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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