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Q35939782-EA6D6BFB-85BC-4021-A299-AB5380A15EE6
Q35939782-EA6D6BFB-85BC-4021-A299-AB5380A15EE6
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http://www.wikidata.org/entity/statement/Q35939782-EA6D6BFB-85BC-4021-A299-AB5380A15EE6
System-wide studies of N-lysine acetylation in Rhodopseudomonas palustris reveal substrate specificity of protein acetyltransferases.
P2860
Q35939782-EA6D6BFB-85BC-4021-A299-AB5380A15EE6
BestRank
Statement
http://www.wikidata.org/entity/statement/Q35939782-EA6D6BFB-85BC-4021-A299-AB5380A15EE6
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wasDerivedFrom
096fbf8ddcb44e8c9e62b6c360da0833c70d399f
P2860
Control of acetyl-coenzyme A synthetase (AcsA) activity by acetylation/deacetylation without NAD(+) involvement in Bacillus subtilis