| pubmed-article:20235194 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20235194 | lifeskim:mentions | umls-concept:C0029434 | lld:lifeskim |
| pubmed-article:20235194 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:20235194 | lifeskim:mentions | umls-concept:C0009325 | lld:lifeskim |
| pubmed-article:20235194 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:20235194 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:20235194 | lifeskim:mentions | umls-concept:C0001721 | lld:lifeskim |
| pubmed-article:20235194 | lifeskim:mentions | umls-concept:C0014406 | lld:lifeskim |
| pubmed-article:20235194 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:20235194 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:20235194 | lifeskim:mentions | umls-concept:C0185026 | lld:lifeskim |
| pubmed-article:20235194 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:20235194 | pubmed:dateCreated | 2011-4-21 | lld:pubmed |
| pubmed-article:20235194 | pubmed:abstractText | Osteogenesis imperfecta (OI), a disorder characterized by fragile bones, is often a consequence of missense mutations in type I collagen, which change one Gly in the repeating (Gly-Xaa-Yaa)(n) sequence to a larger amino acid. The impact of local environment and the identity of the residue replacing Gly were investigated using two sets of triple-helical peptides. Gly mutations in the highly stable (Pro-Hyp-Gly)(10) system are compared with mutations in T1-865 peptides where the mutation is located within a less stable natural collagen sequence. Replacement of a Gly residue by Ala, Ser, or Arg leads to significant triple-helical destabilization in both peptide systems. The loss of stability (?T(m) ) due to a Gly to Ala or Gly to Ser change was greater in the more rigid (Pro-Hyp-Gly)(10) peptides than in the T1-865 set, as expected. But the final T(m) values, which may be the more biologically meaningful parameters, were higher for the (Pro-Hyp-Gly)(10) mutation peptides than for the corresponding T1-865 mutation peptides. In both peptide environments, a Gly to Arg replacement prevented the formation of a fully folded triple-helix. Monitoring of folding by differential scanning calorimetry showed a lower stability species as well as the fully folded triple-helical molecules for T1-865 peptides with Gly to Ala or Ser replacements, and this lower stability species disappears as a function of time. The difficulty in propagation through a mutation site in T1-865 peptides may relate to the delayed folding seen in OI collagens and indicates a dependence of folding mechanism on the local sequence environment. | lld:pubmed |
| pubmed-article:20235194 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20235194 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20235194 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20235194 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20235194 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20235194 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20235194 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20235194 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20235194 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20235194 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20235194 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20235194 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20235194 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20235194 | pubmed:issn | 0006-3525 | lld:pubmed |
| pubmed-article:20235194 | pubmed:author | pubmed-author:BrodskyBarbar... | lld:pubmed |
| pubmed-article:20235194 | pubmed:author | pubmed-author:BryanMichael... | lld:pubmed |
| pubmed-article:20235194 | pubmed:author | pubmed-author:ChengHaimingH | lld:pubmed |
| pubmed-article:20235194 | pubmed:copyrightInfo | Copyright © 2010 Wiley Periodicals, Inc. | lld:pubmed |
| pubmed-article:20235194 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:20235194 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:20235194 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20235194 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20235194 | pubmed:pagination | 4-13 | lld:pubmed |
| pubmed-article:20235194 | pubmed:dateRevised | 2011-8-1 | lld:pubmed |
| pubmed-article:20235194 | pubmed:meshHeading | pubmed-meshheading:20235194... | lld:pubmed |
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| pubmed-article:20235194 | pubmed:meshHeading | pubmed-meshheading:20235194... | lld:pubmed |
| pubmed-article:20235194 | pubmed:meshHeading | pubmed-meshheading:20235194... | lld:pubmed |
| pubmed-article:20235194 | pubmed:meshHeading | pubmed-meshheading:20235194... | lld:pubmed |
| pubmed-article:20235194 | pubmed:meshHeading | pubmed-meshheading:20235194... | lld:pubmed |
| pubmed-article:20235194 | pubmed:meshHeading | pubmed-meshheading:20235194... | lld:pubmed |
| pubmed-article:20235194 | pubmed:meshHeading | pubmed-meshheading:20235194... | lld:pubmed |
| pubmed-article:20235194 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:20235194 | pubmed:articleTitle | Sequence environment of mutation affects stability and folding in collagen model peptides of osteogenesis imperfecta. | lld:pubmed |
| pubmed-article:20235194 | pubmed:affiliation | Department of Biochemistry, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA. | lld:pubmed |
| pubmed-article:20235194 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20235194 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:20235194 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
| entrez-gene:1277 | entrezgene:pubmed | pubmed-article:20235194 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20235194 | lld:entrezgene |
