Source:http://linkedlifedata.com/resource/pubmed/id/10322122
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1999-6-22
|
| pubmed:abstractText |
Normally, gelsolin functions in plasma as part of the actin-scavenging system to assemble and disassemble actin filaments. The Asp 187-->Asn (D187N) Asp 187-->Tyr (D187Y) gelsolin mutations facilitate two proteolytic cuts in the parent protein generating a 71-residue fragment that forms amyloid fibrils in humans, putatively causing Finnish type familial amyloidosis (FAF). We investigated the role of the D187N mutation in amyloidogenicity using biophysical studies in vitro.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
1074-5521
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
6
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
293-304
|
| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:10322122-Amyloidosis,
pubmed-meshheading:10322122-Gelsolin,
pubmed-meshheading:10322122-Humans,
pubmed-meshheading:10322122-Hydrogen-Ion Concentration,
pubmed-meshheading:10322122-Peptide Fragments,
pubmed-meshheading:10322122-Peptide Hydrolases,
pubmed-meshheading:10322122-Point Mutation,
pubmed-meshheading:10322122-Protein Conformation,
pubmed-meshheading:10322122-Recombinant Proteins
|
| pubmed:year |
1999
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| pubmed:articleTitle |
The amyloidogenicity of gelsolin is controlled by proteolysis and pH.
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| pubmed:affiliation |
Department of Chemistry, Skaggs Institute for Chemical Biology, The Scripps Research Institute 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|