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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2009-9-17
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pubmed:abstractText |
Mutations resulting in the disruption of protein function are the underlying causes of many genetic diseases. Some mutations affect the number of expressed proteins while others alter the activity on a per-molecule basis. Single amino acid substitutions as caused by non-synonymous Single Nucleotide Polymorphisms (nsSNPs) often disrupt function by altering protein structure and/or stability, but can also wreak havoc by directly impacting functional binding sites. Given the experimental three-dimensional (3D) structure of a protein, we can try to differentiate between the "effect on structure/stability" and the "effect on binding". However, experimental 3D structures are available for only 1% of all known proteins; the magnitude of stability change caused by a given mutation is more widely available.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-10592178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-10820007,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-11242096,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-11295823,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-12079393,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-12202775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-12824425,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-12957544,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-15608251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-15879453,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-15980516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-15987780,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-16074985,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-16551372,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-16760466,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-16824020,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-17526529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-17881006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-18172930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-18245393,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-18287689,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-18654622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-2231712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-238787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-2694933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-8073043,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-9051733,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19758472-9847227
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1471-2105
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
10 Suppl 8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
S8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:19758472-Amino Acid Substitution,
pubmed-meshheading:19758472-Computational Biology,
pubmed-meshheading:19758472-Databases, Protein,
pubmed-meshheading:19758472-Information Storage and Retrieval,
pubmed-meshheading:19758472-Polymorphism, Single Nucleotide,
pubmed-meshheading:19758472-Protein Stability,
pubmed-meshheading:19758472-Proteins,
pubmed-meshheading:19758472-Sequence Alignment,
pubmed-meshheading:19758472-Structure-Activity Relationship
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pubmed:year |
2009
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pubmed:articleTitle |
Correlating protein function and stability through the analysis of single amino acid substitutions.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA. bromberg@rostlab.org
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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