pubmed-article:9655330 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9655330 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:9655330 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:9655330 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
pubmed-article:9655330 | lifeskim:mentions | umls-concept:C1879748 | lld:lifeskim |
pubmed-article:9655330 | lifeskim:mentions | umls-concept:C1706853 | lld:lifeskim |
pubmed-article:9655330 | lifeskim:mentions | umls-concept:C1882348 | lld:lifeskim |
pubmed-article:9655330 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:9655330 | lifeskim:mentions | umls-concept:C0699032 | lld:lifeskim |
pubmed-article:9655330 | lifeskim:mentions | umls-concept:C1282913 | lld:lifeskim |
pubmed-article:9655330 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:9655330 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:9655330 | pubmed:dateCreated | 1998-9-1 | lld:pubmed |
pubmed-article:9655330 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9655330 | pubmed:abstractText | The betagamma-crystallins form a superfamily of eye lens proteins comprised of multiple Greek motifs that are symmetrically organized into domains and higher assemblies. In the betaB2-crystallin dimer each polypeptide folds into two similar domains that are related to monomeric gamma-crystallin by domain swapping. The crystal structure of the circularly permuted two-domain betaB2 polypeptide shows that permutation converts intermolecular domain pairing into intramolecular pairing. However, the dimeric permuted protein is, in fact, half a native tetramer. This result shows how the sequential order of domains in multi-domain proteins can affect quaternary domain assembly. | lld:pubmed |
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pubmed-article:9655330 | pubmed:language | eng | lld:pubmed |
pubmed-article:9655330 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9655330 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9655330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9655330 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9655330 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9655330 | pubmed:month | Jun | lld:pubmed |
pubmed-article:9655330 | pubmed:issn | 0961-8368 | lld:pubmed |
pubmed-article:9655330 | pubmed:author | pubmed-author:WrightGG | lld:pubmed |
pubmed-article:9655330 | pubmed:author | pubmed-author:SlingsbyCC | lld:pubmed |
pubmed-article:9655330 | pubmed:author | pubmed-author:BasakA KAK | lld:pubmed |
pubmed-article:9655330 | pubmed:author | pubmed-author:MaysE LEL | lld:pubmed |
pubmed-article:9655330 | pubmed:author | pubmed-author:WieligmannKK | lld:pubmed |
pubmed-article:9655330 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9655330 | pubmed:volume | 7 | lld:pubmed |
pubmed-article:9655330 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9655330 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9655330 | pubmed:pagination | 1280-5 | lld:pubmed |
pubmed-article:9655330 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:9655330 | pubmed:meshHeading | pubmed-meshheading:9655330-... | lld:pubmed |
pubmed-article:9655330 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9655330 | pubmed:articleTitle | Circular permutation of betaB2-crystallin changes the hierarchy of domain assembly. | lld:pubmed |
pubmed-article:9655330 | pubmed:affiliation | Birkbeck College, Department of Crystallography, London, United Kingdom. | lld:pubmed |
pubmed-article:9655330 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9655330 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:25422 | entrezgene:pubmed | pubmed-article:9655330 | lld:entrezgene |
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