| pubmed-article:2169648 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2169648 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:2169648 | lifeskim:mentions | umls-concept:C0085431 | lld:lifeskim |
| pubmed-article:2169648 | lifeskim:mentions | umls-concept:C0205390 | lld:lifeskim |
| pubmed-article:2169648 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:2169648 | lifeskim:mentions | umls-concept:C0279380 | lld:lifeskim |
| pubmed-article:2169648 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:2169648 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
| pubmed-article:2169648 | pubmed:issue | 4975 | lld:pubmed |
| pubmed-article:2169648 | pubmed:dateCreated | 1990-10-26 | lld:pubmed |
| pubmed-article:2169648 | pubmed:abstractText | Ribonuclease H digests the RNA strand of duplex RNA.DNA hybrids into oligonucleotides. This activity is indispensable for retroviral infection and is involved in bacterial replication. The ribonuclease H from Escherichia coli is homologous with the retroviral proteins. The crystal structure of the E. coli enzyme reveals a distinctive alpha-beta tertiary fold. Analysis of the molecular model implicates a carboxyl triad in the catalytic mechanism and suggests a likely mode for the binding of RNA.DNA substrates. The structure was determined by the method of multiwavelength anomalous diffraction (MAD) with the use of synchrotron data from a crystal of the recombinant selenomethionyl protein. | lld:pubmed |
| pubmed-article:2169648 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2169648 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2169648 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2169648 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2169648 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2169648 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:2169648 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:2169648 | pubmed:author | pubmed-author:HendricksonW... | lld:pubmed |
| pubmed-article:2169648 | pubmed:author | pubmed-author:SatowYY | lld:pubmed |
| pubmed-article:2169648 | pubmed:author | pubmed-author:YangWW | lld:pubmed |
| pubmed-article:2169648 | pubmed:author | pubmed-author:CrouchR JRJ | lld:pubmed |
| pubmed-article:2169648 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2169648 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:2169648 | pubmed:volume | 249 | lld:pubmed |
| pubmed-article:2169648 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2169648 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2169648 | pubmed:pagination | 1398-405 | lld:pubmed |
| pubmed-article:2169648 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:2169648 | pubmed:meshHeading | pubmed-meshheading:2169648-... | lld:pubmed |
| pubmed-article:2169648 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2169648 | pubmed:articleTitle | Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein. | lld:pubmed |
| pubmed-article:2169648 | pubmed:affiliation | Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032. | lld:pubmed |
| pubmed-article:2169648 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2169648 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2169648 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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