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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:dateCreated |
1989-10-19
|
| pubmed:abstractText |
Glycation of proteins increases their negative charge and is a self-limiting process. Glycation also changes the recognition of proteins. The mammalian nephron can discriminate between glycated and unmodified albumin. Diabetes and ageing both modify this discrimination. Abnormalities in protein recognition may contribute to the pathological impact of glycation. The increase in negative charge may explain both the limit on glycation and its capacity to change protein recognition.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0361-7742
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
304
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
185-203
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:2675028-Aging,
pubmed-meshheading:2675028-Animals,
pubmed-meshheading:2675028-Diabetes Mellitus,
pubmed-meshheading:2675028-Glycosylation,
pubmed-meshheading:2675028-Humans,
pubmed-meshheading:2675028-Isoelectric Point,
pubmed-meshheading:2675028-Models, Biological,
pubmed-meshheading:2675028-Nephrons,
pubmed-meshheading:2675028-Serum Albumin
|
| pubmed:year |
1989
|
| pubmed:articleTitle |
Non-enzymatic glycation and protein recognition.
|
| pubmed:affiliation |
Life Sciences Division, Los Alamos National Laboratory, New Mexico 87545.
|
| pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
|