pubmed-article:3844012 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3844012 | lifeskim:mentions | umls-concept:C0035711 | lld:lifeskim |
pubmed-article:3844012 | lifeskim:mentions | umls-concept:C1537998 | lld:lifeskim |
pubmed-article:3844012 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:3844012 | lifeskim:mentions | umls-concept:C2346927 | lld:lifeskim |
pubmed-article:3844012 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:3844012 | pubmed:dateCreated | 1985-3-6 | lld:pubmed |
pubmed-article:3844012 | pubmed:abstractText | The Pb2+-catalyzed cleavage of tRNAPhe has been used to probe the effect of Na+ and Mg2+ binding to tRNA. Na+ is a noncompetitive inhibitor of the Pb2+-catalyzed cleavage. Millimolar Mg2+ is also a noncompetitive inhibitor. Analysis of the Mg2+ data show that at least two sites are involved in binding and that there is an interaction between the sites (cooperativity). Low-affinity Mg2+ binding is thus different from "weak" and "strong" Mg2+ binding to tRNA characterized previously. We postulate that the alterations induced by low-affinity Mg2+ binding in tRNA mimic to some extent those brought about in RNA by the interaction with a protein factor and that at appropriate [Mg2+] the whole structure of tRNA is able to respond in a concerted way to a signal from the environment such as aminoacylation or codon binding. | lld:pubmed |
pubmed-article:3844012 | pubmed:language | eng | lld:pubmed |
pubmed-article:3844012 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3844012 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3844012 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3844012 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3844012 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3844012 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3844012 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3844012 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3844012 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3844012 | pubmed:month | Jan | lld:pubmed |
pubmed-article:3844012 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:3844012 | pubmed:author | pubmed-author:LabudaDD | lld:pubmed |
pubmed-article:3844012 | pubmed:author | pubmed-author:CedergrenRR | lld:pubmed |
pubmed-article:3844012 | pubmed:author | pubmed-author:NicoghosianKK | lld:pubmed |
pubmed-article:3844012 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3844012 | pubmed:day | 25 | lld:pubmed |
pubmed-article:3844012 | pubmed:volume | 260 | lld:pubmed |
pubmed-article:3844012 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3844012 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3844012 | pubmed:pagination | 1103-7 | lld:pubmed |
pubmed-article:3844012 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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pubmed-article:3844012 | pubmed:year | 1985 | lld:pubmed |
pubmed-article:3844012 | pubmed:articleTitle | Cooperativity in low-affinity Mg2+ binding to tRNA. | lld:pubmed |
pubmed-article:3844012 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3844012 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |