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1 NatA co-translationally acetylates the N termini of a wi
2 NatA is bound to Huntingtin-interacting protein K (HYPK)
3 Among them, N-terminal acetyltransferase A (NatA) acetylates the N terminus of ~40% of the eukaryoti
7 rprisingly, this enzyme is able to acetylate NatA and NatE substrates and is believed to represent an
11 , and the three N(alpha)-acetyltransferases, NatA, NatB, and NatC, which collectively modify approxim
12 pes of N(alpha)-terminal acetyltransferases, NatA, NatB, and NatC, with each having a different catal
13 two-hybrid protein K(4,5) (HYPK) to activate NatA on the ribosome, enforcing cotranslational N-termin
15 embles a multienzyme complex with MetAP1 and NatA early during translation and pre-positions the acti
16 tionship between ADO-catalysed oxidation and NatA-catalysed acetylation of a broad range of protein s
17 ases significantly after drought stress, and NatA abundance is rapidly downregulated by the phytohorm
18 t each other's NAT activity in vitro Because NatA and Naa50 exhibit distinct substrate specificity, w
19 tress and that imprinting of the proteome by NatA is an important switch for the control of metabolis
20 -terminal acetyltransferase (NAT) complexes (NatA-NatC), which co-translationally acetylate the N-ter
22 yeast (Saccharomyces cerevisiae), this core NatA complex interacts with NAA50 to form the NatE compl
23 N-terminal acetyl transferases (NATs), i.e., NatA, NatB, and NatC, which require as few as two specif
27 molecular dynamics simulations of the human NatA and its S37P mutant highlight differences in region
28 al analyses of variants as part of the human NatA complex, as well as enzymatic analyses with and wit
29 unctionally important differences with human NatA and Candida albicans NatB, resolves key hNatB prote
30 f a neurodegenerative disease and implicates NatA-mediated Htt acetylation as a new potential therape
31 interacting protein K (HYPK), which inhibits NatA activity in vitro but enhances function in vivo.
32 at) in Arabidopsis (Arabidopsis thaliana) is NatA, which cotranslationally catalyzes acetylation of ~
33 NAA50 expression did not affect NTA of known NatA substrates and caused the accumulation of proteins
35 f three N-terminal acetyltransferases (NAT), NatA, NatB, and NatC, which contain Ard1p, Nat3p and Mak
38 the Arg/N-end rule pathway in the absence of NatA, and showed that a number of Hsp90 clients are prev
39 plex and reveal evolutionary conservation of NatA biochemical properties in higher eukaryotes and unc
41 Accordingly, transgenic downregulation of NatA induces the drought stress response and results in
42 uncover specific and essential functions of NatA for development, biosynthetic pathways and stress r
43 Based on our data, we propose the name of NatA (N-acyltransferase A) in lieu of YiaC to reflect th
44 ealed a decreased acetylation of a subset of NatA and NatE substrates in Ogden syndrome cells, suppor
45 arding reduced Nt-acetylation of a subset of NatA/NatE-type substrates as one etiology for Ogden synd
46 ene encoding Naa10, the catalytic subunit of NatA, the major human NAT involved in the co-translation
49 HYPK, hyper-tight ribosome binding prevents NatA from accessing additional ribosomes following each
50 Despite this change in phenotype, [PSI(+)] NatA mutants continue to propagate heritable Sup35([PSI+
58 equired for N-terminal acetylation, i.e. the NatA, NatB, and NatC substrates, were evaluated by consi
59 N-terminus is an in vitro substrate for the NatA N-terminal acetyltransferase and show that N-termin
60 eleases the inhibitory interactions from the NatA regulatory protein huntingtin yeast two-hybrid prot
61 impaired in naa10Delta cells, which lack the NatA N(alpha)-terminal acetylase (Nt-acetylase) and ther
63 ive site of ssNAT represents a hybrid of the NatA and NatE active sites, and we highlight features of
64 The auxiliary and regulatory subunits of the NatA complex are NAA15 and Huntington-interacting protei
66 ld be overridden not only by ablation of the NatA Nt-acetylase but also by overexpression of the Arg/
67 h a small fraction of San interacts with the NatA complex, San appears to mediate cohesion independen
68 minal-acetylated, and 24 of these (80%) were NatA substrates, unacetylated in solely the ard1-Delta m
69 ve been structurally characterized, of which NatA will acetylate the alpha-amino group of a number of