| pubmed-article:11173483 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11173483 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:11173483 | lifeskim:mentions | umls-concept:C0042373 | lld:lifeskim |
| pubmed-article:11173483 | lifeskim:mentions | umls-concept:C0010641 | lld:lifeskim |
| pubmed-article:11173483 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:11173483 | lifeskim:mentions | umls-concept:C0444669 | lld:lifeskim |
| pubmed-article:11173483 | lifeskim:mentions | umls-concept:C0010423 | lld:lifeskim |
| pubmed-article:11173483 | lifeskim:mentions | umls-concept:C0043301 | lld:lifeskim |
| pubmed-article:11173483 | lifeskim:mentions | umls-concept:C0765250 | lld:lifeskim |
| pubmed-article:11173483 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:11173483 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:11173483 | lifeskim:mentions | umls-concept:C0439611 | lld:lifeskim |
| pubmed-article:11173483 | pubmed:issue | Pt 2 | lld:pubmed |
| pubmed-article:11173483 | pubmed:dateCreated | 2001-2-22 | lld:pubmed |
| pubmed-article:11173483 | pubmed:abstractText | Cystathionine beta-synthase (CBS) is a unique heme enzyme that catalyzes a PLP-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an autosomal recessively inherited disease of sulfur metabolism. A truncated form of CBS in which the C-terminal amino-acid residues have been deleted has been prepared. The truncated CBS subunits form a dimer, in contrast to the full-length subunits which form tetramers and higher oligomers. The truncated CBS yielded crystals diffracting to 2.6 A which belong to space group P3(1) or P3(2). This is the first comprehensive structural investigation of a PLP and heme-containing enzyme. | lld:pubmed |
| pubmed-article:11173483 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11173483 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11173483 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11173483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11173483 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11173483 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11173483 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:11173483 | pubmed:issn | 0907-4449 | lld:pubmed |
| pubmed-article:11173483 | pubmed:author | pubmed-author:MeierMM | lld:pubmed |
| pubmed-article:11173483 | pubmed:author | pubmed-author:Janosik MM | lld:pubmed |
| pubmed-article:11173483 | pubmed:author | pubmed-author:Kery VV | lld:pubmed |
| pubmed-article:11173483 | pubmed:author | pubmed-author:OliveriusovaJ... | lld:pubmed |
| pubmed-article:11173483 | pubmed:author | pubmed-author:Burkhard PP | lld:pubmed |
| pubmed-article:11173483 | pubmed:author | pubmed-author:Kraus J PJP | lld:pubmed |
| pubmed-article:11173483 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11173483 | pubmed:volume | 57 | lld:pubmed |
| pubmed-article:11173483 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11173483 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11173483 | pubmed:pagination | 289-91 | lld:pubmed |
| pubmed-article:11173483 | pubmed:dateRevised | 2007-7-24 | lld:pubmed |
| pubmed-article:11173483 | pubmed:meshHeading | pubmed-meshheading:11173483... | lld:pubmed |
| pubmed-article:11173483 | pubmed:meshHeading | pubmed-meshheading:11173483... | lld:pubmed |
| pubmed-article:11173483 | pubmed:meshHeading | pubmed-meshheading:11173483... | lld:pubmed |
| pubmed-article:11173483 | pubmed:meshHeading | pubmed-meshheading:11173483... | lld:pubmed |
| pubmed-article:11173483 | pubmed:meshHeading | pubmed-meshheading:11173483... | lld:pubmed |
| pubmed-article:11173483 | pubmed:meshHeading | pubmed-meshheading:11173483... | lld:pubmed |
| pubmed-article:11173483 | pubmed:meshHeading | pubmed-meshheading:11173483... | lld:pubmed |
| pubmed-article:11173483 | pubmed:meshHeading | pubmed-meshheading:11173483... | lld:pubmed |
| pubmed-article:11173483 | pubmed:meshHeading | pubmed-meshheading:11173483... | lld:pubmed |
| pubmed-article:11173483 | pubmed:meshHeading | pubmed-meshheading:11173483... | lld:pubmed |
| pubmed-article:11173483 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11173483 | pubmed:articleTitle | Crystallization and preliminary X-ray diffraction analysis of the active core of human recombinant cystathionine beta-synthase: an enzyme involved in vascular disease. | lld:pubmed |
| pubmed-article:11173483 | pubmed:affiliation | Department of Pediatrics, University of Colorado School of Medicine, Denver, CO 80262, USA. | lld:pubmed |
| pubmed-article:11173483 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:875 | entrezgene:pubmed | pubmed-article:11173483 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:11173483 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11173483 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:11173483 | lld:pubmed |
