| pubmed-article:2354165 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2354165 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:2354165 | lifeskim:mentions | umls-concept:C1707455 | lld:lifeskim |
| pubmed-article:2354165 | lifeskim:mentions | umls-concept:C1149302 | lld:lifeskim |
| pubmed-article:2354165 | lifeskim:mentions | umls-concept:C0037633 | lld:lifeskim |
| pubmed-article:2354165 | lifeskim:mentions | umls-concept:C0450442 | lld:lifeskim |
| pubmed-article:2354165 | lifeskim:mentions | umls-concept:C1707391 | lld:lifeskim |
| pubmed-article:2354165 | lifeskim:mentions | umls-concept:C1382100 | lld:lifeskim |
| pubmed-article:2354165 | lifeskim:mentions | umls-concept:C1516451 | lld:lifeskim |
| pubmed-article:2354165 | lifeskim:mentions | umls-concept:C1514623 | lld:lifeskim |
| pubmed-article:2354165 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:2354165 | pubmed:dateCreated | 1990-7-20 | lld:pubmed |
| pubmed-article:2354165 | pubmed:abstractText | This paper details comprehensive binding studies (solution and X-ray) of human hemoglobin A with a group of halogenated carboxylic acids that were investigated as potential antisickling agents. It is, to our knowledge, the first study to compare solution and crystal binding for a series of compounds under similar high-salt conditions used for cocrystallization. The compounds include [(3,4-dichlorobenzyl)oxy]acetic acid, [(p-bromobenzyl)oxy]acetic acid, clofibric acid, and bezafibrate. The location and stereochemistry of binding sites have been established by X-ray crystallography, while the number of binding sites and affinity constants were measured by using equilibrium dialysis. The solution binding studies were conducted with deoxygenated hemoglobin and carbonmonoxyhemoglobin with low (50 mM) and high (2 M) salt concentrations. It was concluded that the observed crystal structures are consistent with the binding observed in solution and that the number of binding sites is independent of salt concentration, while the binding constant increases with increasing salt concentration. The studies also reveal that relatively small changes in the chemical structure of a drug molecule can result in entirely different binding sites on the protein. Moreover, the X-ray studies provide a possible explanation for the multiplicity in function exhibited by these compounds as allosteric modulators and/or antisickling agents. Finally, the studies that these compounds bind differently to the R and T states of hemoglobin, an observation of special significance to the original design of these agents. | lld:pubmed |
| pubmed-article:2354165 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2354165 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2354165 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2354165 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2354165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2354165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2354165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2354165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2354165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2354165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2354165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2354165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2354165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2354165 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2354165 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2354165 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:2354165 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:2354165 | pubmed:author | pubmed-author:AbrahamD JDJ | lld:pubmed |
| pubmed-article:2354165 | pubmed:author | pubmed-author:MehannaA SAS | lld:pubmed |
| pubmed-article:2354165 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2354165 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:2354165 | pubmed:volume | 29 | lld:pubmed |
| pubmed-article:2354165 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2354165 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2354165 | pubmed:pagination | 3944-52 | lld:pubmed |
| pubmed-article:2354165 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:2354165 | pubmed:meshHeading | pubmed-meshheading:2354165-... | lld:pubmed |
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| pubmed-article:2354165 | pubmed:meshHeading | pubmed-meshheading:2354165-... | lld:pubmed |
| pubmed-article:2354165 | pubmed:meshHeading | pubmed-meshheading:2354165-... | lld:pubmed |
| pubmed-article:2354165 | pubmed:meshHeading | pubmed-meshheading:2354165-... | lld:pubmed |
| pubmed-article:2354165 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2354165 | pubmed:articleTitle | Comparison of crystal and solution hemoglobin binding of selected antigelling agents and allosteric modifiers. | lld:pubmed |
| pubmed-article:2354165 | pubmed:affiliation | Department of Medicinal Chemistry, School of Pharmacy, Medical College of Virginia, Virginia Commonwealth University, Richmond 23298. | lld:pubmed |
| pubmed-article:2354165 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2354165 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2354165 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2354165 | lld:pubmed |
