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1 etylation of lysine residues is an important post-translational protein modification.
2 s levels, from transcriptional activation to post-translational protein modification.
3 zyme known to cleave a phosphodiester-linked post-translational protein modification.
4 urther broadened the horizon of this type of post-translational protein modification.
5 els, ranging from transcriptional control to post-translational protein modifications.
6 tives that can modulate protein function via post-translational protein modifications.
7 anti-inflammatory signaling actions through post-translational protein modifications.
8 n, messenger RNA processing, mRNA decay, and post-translational protein modifications.
9 d by two other lysosomal enzymes that remove post-translational protein modifications.
11 atalysis, the roles of these dioxygenases in post-translational protein modification and de-modificat
12 idues is the most common type of spontaneous post-translational protein modification and plays a vita
13 ic strains has led to the discovery of novel post-translational protein modifications and new underst
14 processes including cell-wall biosynthesis, post-translational protein modifications, and signaling.
15 and protein abundances; characterization of post-translational protein modifications; and instrument
19 mation describing the molecular mechanism of post-translational protein modifications catalysed by TP
20 Poly(ADP-ribosyl)ation (PARylation) is a post-translational protein modification effected by enzy
21 thin the phylum suggests that this system of post-translational protein modification evolved early, b
23 denosine diphosphate (ADP)-ribosylation is a post-translational protein modification implicated in th
32 amino acids (Pcombined = 1.57 x 10(-7)), and post-translational protein modification (Pcombined = 1.5
33 ll lumenal domain of Jaw1 represents a novel post-translational protein modification performed by the
34 in (TTR) is frequently affected by oxidative post-translational protein modifications (PTPMs) in vari
37 tions in vivo indicates that this reversible post-translational protein modification represents a new
38 proposition that this ubiquitous NO-derived post-translational protein modification serves as a majo
39 stress, intracellular lipid accumulation and post-translational protein modifications strongly argue
45 ein oligomerization (HTPO), a unique type of post-translational protein modification that may have cl
47 transduction generally involves cascades of post-translational protein modifications that rapidly ca
48 ne, which encodes a protein that catalyzes a post-translational protein modification, the attachment
49 ttempts to bypass normal immune tolerance, a post-translational protein modification was introduced i
50 cs after myocardial infarction by increasing post-translational protein modifications, which cause in
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