| pubmed-article:8925838 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8925838 | lifeskim:mentions | umls-concept:C0439660 | lld:lifeskim |
| pubmed-article:8925838 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:8925838 | lifeskim:mentions | umls-concept:C0002520 | lld:lifeskim |
| pubmed-article:8925838 | lifeskim:mentions | umls-concept:C0032191 | lld:lifeskim |
| pubmed-article:8925838 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:8925838 | lifeskim:mentions | umls-concept:C0733755 | lld:lifeskim |
| pubmed-article:8925838 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:8925838 | lifeskim:mentions | umls-concept:C1416485 | lld:lifeskim |
| pubmed-article:8925838 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
| pubmed-article:8925838 | lifeskim:mentions | umls-concept:C1523815 | lld:lifeskim |
| pubmed-article:8925838 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:8925838 | lifeskim:mentions | umls-concept:C0337112 | lld:lifeskim |
| pubmed-article:8925838 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8925838 | pubmed:dateCreated | 1996-11-4 | lld:pubmed |
| pubmed-article:8925838 | pubmed:abstractText | To examine the effects of naturally occurring inherited mutations on the ability of the integrin alpha-subunit, also termed glycoprotein IIb (GPIIb), to bind metal ions, we prepared small synthetic peptides that encompassed individual cation-binding domains, and recombinant GPIIb poly peptides that encompassed all four Ca(2+)-binding domains, and examined their interactions with divalent cations by means of Tb3+-luminescence spectroscopy. Replacement of the highly conserved Gly418 residue, located within the flanking region of the fourth Ca(2+)-binding domain of GPIIb, with a negatively charged Asp residue resulted in marked reduction in the ability to bind divalent cations. A variant form of GPIIb with a deletion of two amino acids at the -1 and X positions of the fourth Ca(2+)-binding domain of GPIIb also failed to bind metal ions in a normal manner. In contrast, a Glanzmann mutation at the -1 position of the first Ca(2+)-binding domain of GPIIb had no effect on divalent-cation-binding ability with either synthetic peptides or recombinant GPIIb polypeptides. These data support the hypothesis that the highly conserved Gly normally found 7-8 residues N-terminal to integrin metal-binding domains plays a critical role in the maintenance of the conformation or orientation of surrounding EF-hand structures so that they can effectively interact with and bind divalent cations. Furthermore, inherited mutations at or near the divalent-cation-binding domains of GPIIb do not necessarily exert their biochemical effects by disruption of cation binding, but can interfere with integrin biogenesis in a Ca(2+)-independent manner. | lld:pubmed |
| pubmed-article:8925838 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8925838 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8925838 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8925838 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8925838 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8925838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8925838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8925838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8925838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8925838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8925838 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8925838 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8925838 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:8925838 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:8925838 | pubmed:author | pubmed-author:NewmanP JPJ | lld:pubmed |
| pubmed-article:8925838 | pubmed:author | pubmed-author:JacksonD EDE | lld:pubmed |
| pubmed-article:8925838 | pubmed:author | pubmed-author:PonczMM | lld:pubmed |
| pubmed-article:8925838 | pubmed:author | pubmed-author:HolystM TMT | lld:pubmed |
| pubmed-article:8925838 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8925838 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8925838 | pubmed:volume | 240 | lld:pubmed |
| pubmed-article:8925838 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8925838 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8925838 | pubmed:pagination | 280-7 | lld:pubmed |
| pubmed-article:8925838 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:8925838 | pubmed:meshHeading | pubmed-meshheading:8925838-... | lld:pubmed |
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| pubmed-article:8925838 | pubmed:meshHeading | pubmed-meshheading:8925838-... | lld:pubmed |
| pubmed-article:8925838 | pubmed:meshHeading | pubmed-meshheading:8925838-... | lld:pubmed |
| pubmed-article:8925838 | pubmed:meshHeading | pubmed-meshheading:8925838-... | lld:pubmed |
| pubmed-article:8925838 | pubmed:meshHeading | pubmed-meshheading:8925838-... | lld:pubmed |
| pubmed-article:8925838 | pubmed:meshHeading | pubmed-meshheading:8925838-... | lld:pubmed |
| pubmed-article:8925838 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8925838 | pubmed:articleTitle | Inherited mutations within the calcium-binding sites of the integrin alpha IIb subunit (platelet glycoprotein IIb). Effects of the amino acid side chain and the amino acid position on cation binding. | lld:pubmed |
| pubmed-article:8925838 | pubmed:affiliation | Blood Research Institute, Blood Center of Southeastern Wisconsin, Milwauke 53233-2194, USA. | lld:pubmed |
| pubmed-article:8925838 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8925838 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8925838 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8925838 | lld:pubmed |
