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Q45305618-B976E455-9CDA-4E8A-A35B-FABB275CFAD1
Q45305618-B976E455-9CDA-4E8A-A35B-FABB275CFAD1
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http://www.wikidata.org/entity/statement/Q45305618-B976E455-9CDA-4E8A-A35B-FABB275CFAD1
Phosphorylation of huntingtin at residue T3 is decreased in Huntington's disease and modulates mutant huntingtin protein conformation.
P2860
Q45305618-B976E455-9CDA-4E8A-A35B-FABB275CFAD1
BestRank
Statement
http://www.wikidata.org/entity/statement/Q45305618-B976E455-9CDA-4E8A-A35B-FABB275CFAD1
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wasDerivedFrom
38b8db36d10722ad81bb06836db72722b33ef097
P2860
Comparative study of naturally occurring huntingtin fragments in Drosophila points to exon 1 as the most pathogenic species in Huntington's disease