| pubmed-article:16563025 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16563025 | lifeskim:mentions | umls-concept:C0304925 | lld:lifeskim |
| pubmed-article:16563025 | lifeskim:mentions | umls-concept:C0001117 | lld:lifeskim |
| pubmed-article:16563025 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:16563025 | lifeskim:mentions | umls-concept:C0043031 | lld:lifeskim |
| pubmed-article:16563025 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:16563025 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:16563025 | pubmed:dateCreated | 2007-4-10 | lld:pubmed |
| pubmed-article:16563025 | pubmed:abstractText | Sudlow Site I of human serum albumin (HSA) is located in subdomain IIA of the protein and serves as a binding cavity for a variety of ligands. In this study, the binding of warfarin (W) is examined using computational techniques and isothermal titration calorimetry (ITC). The structure of the docked warfarin anion (W-) to Site I is similar to that revealed by X-ray crystallography, with a calculated binding constant of 5.8 x 10(5) M(-1). ITC experiments (pH 7.13 and I = 0.1) carried out in three different buffers (MOPs, phosphate and Tris) reveal binding of W- is accompanied by uptake of 0.30+/-0.02 protons from the solvent. This measurement suggests that the binding of W- is stabilized by an ion-pair interaction between protonated H242 and the phenoxide group of W-. | lld:pubmed |
| pubmed-article:16563025 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16563025 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16563025 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16563025 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16563025 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16563025 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16563025 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16563025 | pubmed:issn | 0031-8655 | lld:pubmed |
| pubmed-article:16563025 | pubmed:author | pubmed-author:TooneEric JEJ | lld:pubmed |
| pubmed-article:16563025 | pubmed:author | pubmed-author:SimonJohn DJD | lld:pubmed |
| pubmed-article:16563025 | pubmed:author | pubmed-author:BeratanDavid... | lld:pubmed |
| pubmed-article:16563025 | pubmed:author | pubmed-author:PerryJennifer... | lld:pubmed |
| pubmed-article:16563025 | pubmed:author | pubmed-author:ChristensenTr... | lld:pubmed |
| pubmed-article:16563025 | pubmed:author | pubmed-author:RadackKyle... | lld:pubmed |
| pubmed-article:16563025 | pubmed:author | pubmed-author:GoldsmithMich... | lld:pubmed |
| pubmed-article:16563025 | pubmed:author | pubmed-author:GorhamJustinJ | lld:pubmed |
| pubmed-article:16563025 | pubmed:author | pubmed-author:WilliamsT... | lld:pubmed |
| pubmed-article:16563025 | pubmed:author | pubmed-author:PasquinelliMe... | lld:pubmed |
| pubmed-article:16563025 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16563025 | pubmed:volume | 82 | lld:pubmed |
| pubmed-article:16563025 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16563025 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16563025 | pubmed:pagination | 1365-9 | lld:pubmed |
| pubmed-article:16563025 | pubmed:dateRevised | 2007-12-3 | lld:pubmed |
| pubmed-article:16563025 | pubmed:meshHeading | pubmed-meshheading:16563025... | lld:pubmed |
| pubmed-article:16563025 | pubmed:meshHeading | pubmed-meshheading:16563025... | lld:pubmed |
| pubmed-article:16563025 | pubmed:meshHeading | pubmed-meshheading:16563025... | lld:pubmed |
| pubmed-article:16563025 | pubmed:meshHeading | pubmed-meshheading:16563025... | lld:pubmed |
| pubmed-article:16563025 | pubmed:meshHeading | pubmed-meshheading:16563025... | lld:pubmed |
| pubmed-article:16563025 | pubmed:meshHeading | pubmed-meshheading:16563025... | lld:pubmed |
| pubmed-article:16563025 | pubmed:meshHeading | pubmed-meshheading:16563025... | lld:pubmed |
| pubmed-article:16563025 | pubmed:meshHeading | pubmed-meshheading:16563025... | lld:pubmed |
| pubmed-article:16563025 | pubmed:meshHeading | pubmed-meshheading:16563025... | lld:pubmed |
| pubmed-article:16563025 | pubmed:articleTitle | Binding of warfarin influences the acid-base equilibrium of H242 in sudlow site I of human serum albumin. | lld:pubmed |
| pubmed-article:16563025 | pubmed:affiliation | Laboratory of Pharmacology and Chemistry, National Institute of Environmental Health Sciences, Research Triangle Park, NC, USA. | lld:pubmed |
| pubmed-article:16563025 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16563025 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16563025 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
