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1 NatA co-translationally acetylates the N termini of a wi
2 rprisingly, this enzyme is able to acetylate NatA and NatE substrates and is believed to represent an
4 , and the three N(alpha)-acetyltransferases, NatA, NatB, and NatC, which collectively modify approxim
5 pes of N(alpha)-terminal acetyltransferases, NatA, NatB, and NatC, with each having a different catal
6 ases significantly after drought stress, and NatA abundance is rapidly downregulated by the phytohorm
7 t each other's NAT activity in vitro Because NatA and Naa50 exhibit distinct substrate specificity, w
8 tress and that imprinting of the proteome by NatA is an important switch for the control of metabolis
9 N-terminal acetyl transferases (NATs), i.e., NatA, NatB, and NatC, which require as few as two specif
10 molecular dynamics simulations of the human NatA and its S37P mutant highlight differences in region
12 f three N-terminal acetyltransferases (NAT), NatA, NatB, and NatC, which contain Ard1p, Nat3p and Mak
14 the Arg/N-end rule pathway in the absence of NatA, and showed that a number of Hsp90 clients are prev
15 plex and reveal evolutionary conservation of NatA biochemical properties in higher eukaryotes and unc
17 Accordingly, transgenic downregulation of NatA induces the drought stress response and results in
18 uncover specific and essential functions of NatA for development, biosynthetic pathways and stress r
19 ealed a decreased acetylation of a subset of NatA and NatE substrates in Ogden syndrome cells, suppor
20 arding reduced Nt-acetylation of a subset of NatA/NatE-type substrates as one etiology for Ogden synd
21 ene encoding Naa10, the catalytic subunit of NatA, the major human NAT involved in the co-translation
23 Despite this change in phenotype, [PSI(+)] NatA mutants continue to propagate heritable Sup35([PSI+
31 equired for N-terminal acetylation, i.e. the NatA, NatB, and NatC substrates, were evaluated by consi
32 impaired in naa10Delta cells, which lack the NatA N(alpha)-terminal acetylase (Nt-acetylase) and ther
34 ive site of ssNAT represents a hybrid of the NatA and NatE active sites, and we highlight features of
36 ld be overridden not only by ablation of the NatA Nt-acetylase but also by overexpression of the Arg/
37 h a small fraction of San interacts with the NatA complex, San appears to mediate cohesion independen
38 minal-acetylated, and 24 of these (80%) were NatA substrates, unacetylated in solely the ard1-Delta m
39 ve been structurally characterized, of which NatA will acetylate the alpha-amino group of a number of
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