| pubmed-article:12054555 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12054555 | lifeskim:mentions | umls-concept:C0023317 | lld:lifeskim |
| pubmed-article:12054555 | lifeskim:mentions | umls-concept:C0002202 | lld:lifeskim |
| pubmed-article:12054555 | lifeskim:mentions | umls-concept:C0205216 | lld:lifeskim |
| pubmed-article:12054555 | lifeskim:mentions | umls-concept:C0678640 | lld:lifeskim |
| pubmed-article:12054555 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:12054555 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:12054555 | pubmed:dateCreated | 2002-6-10 | lld:pubmed |
| pubmed-article:12054555 | pubmed:abstractText | alpha A-Crystallin high-molecular-weight (HMW) aggregates were prepared by preheating at 80-90 degrees C and studied using spectroscopic measurements. Conformational differences were suggested based on data of increased bis-ANS (4,4(')-dianilino-1,1(')-binaphthalene-5,5(')-disulfonic acid) and ThT (thioflavin T) fluorescence as well as increased far-UV and decreased near-UV circular dichroism (CD). These results indicated that HMW aggregated alpha-crystallin was more hydrophobic than the native alpha-crystallin, possibly resulting from partial unfolding of alpha-crystallin. The two cysteines in alpha A-crystallin were mostly oxidized in HMW aggregates. The effects of HMW aggregation on the dynamic structure were studied with fluorescence resonance energy transfer; subunit exchange became slower. These results strongly suggest that HMW alpha A-crystallin aggregates result from exposure of buried beta-pleated sheets and increased hydrophobic interaction. | lld:pubmed |
| pubmed-article:12054555 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12054555 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12054555 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12054555 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12054555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12054555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12054555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12054555 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12054555 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12054555 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:12054555 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:12054555 | pubmed:author | pubmed-author:NoelG JGJ | lld:pubmed |
| pubmed-article:12054555 | pubmed:author | pubmed-author:LiangJack... | lld:pubmed |
| pubmed-article:12054555 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12054555 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:12054555 | pubmed:volume | 293 | lld:pubmed |
| pubmed-article:12054555 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12054555 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12054555 | pubmed:pagination | 7-12 | lld:pubmed |
| pubmed-article:12054555 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:12054555 | pubmed:meshHeading | pubmed-meshheading:12054555... | lld:pubmed |
| pubmed-article:12054555 | pubmed:meshHeading | pubmed-meshheading:12054555... | lld:pubmed |
| pubmed-article:12054555 | pubmed:meshHeading | pubmed-meshheading:12054555... | lld:pubmed |
| pubmed-article:12054555 | pubmed:meshHeading | pubmed-meshheading:12054555... | lld:pubmed |
| pubmed-article:12054555 | pubmed:meshHeading | pubmed-meshheading:12054555... | lld:pubmed |
| pubmed-article:12054555 | pubmed:meshHeading | pubmed-meshheading:12054555... | lld:pubmed |
| pubmed-article:12054555 | pubmed:meshHeading | pubmed-meshheading:12054555... | lld:pubmed |
| pubmed-article:12054555 | pubmed:meshHeading | pubmed-meshheading:12054555... | lld:pubmed |
| pubmed-article:12054555 | pubmed:meshHeading | pubmed-meshheading:12054555... | lld:pubmed |
| pubmed-article:12054555 | pubmed:meshHeading | pubmed-meshheading:12054555... | lld:pubmed |
| pubmed-article:12054555 | pubmed:meshHeading | pubmed-meshheading:12054555... | lld:pubmed |
| pubmed-article:12054555 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12054555 | pubmed:articleTitle | Decreased subunit exchange of heat-treated lens alpha A-crystallin. | lld:pubmed |
| pubmed-article:12054555 | pubmed:affiliation | Department of Ophthalmology, Center for Ophthalmic Research, Brigham and Women's Hospital, Harvard Medical School, 221 Longwood Avenue, Boston, MA 02115, USA. jliang@rics.bwh.harvard.edu | lld:pubmed |
| pubmed-article:12054555 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12054555 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12054555 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12054555 | lld:pubmed |
