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1 in the long C-terminal region of yeast Dcp2 decapping enzyme.
2 all substrates tested, Dcp2 was the primary decapping enzyme.
3 ication of a previously uncharacterized mRNA decapping enzyme.
4 rus family shown to encode a Nudix hydrolase-decapping enzyme.
5 Here, we report that TDT encodes the mRNA-decapping enzyme.
6 ne expression and is carried out by the Dcp2 decapping enzyme.
7 er suppressor of a conditional allele in the decapping enzyme.
8 compensate for decreases in activity of the decapping enzyme.
9 ing in vivo and for the production of active decapping enzyme.
10 d for the production of enzymatically active decapping enzyme.
11 capping differ in their requirements for the decapping enzyme.
12 apping, thereby indicating that Dcp1p is the decapping enzyme.
13 rotects the 5' cap from attack by Dcp1p, the decapping enzyme.
14 cytoplasmic granules that co-localized with decapping enzyme 1 (DCP1), a marker of P-bodies; sites o
15 e processing body (PB) markers, such as mRNA-decapping enzyme 1A (DCP1a), and thus may not represent
17 eneral mRNA decapping requires the Dcp1/Dcp2 decapping enzyme and a set of decapping activators, incl
18 ta define a new role for the Dcs1p scavenger decapping enzyme and demonstrate a novel mechanism where
19 his review, we discuss the properties of the decapping enzyme and how its activity is regulated to gi
20 This observation confirmed that Dcp1p is the decapping enzyme and indicated that Dcp2p functions to a
21 cp2p also coimmunoprecipitates with the DCP1 decapping enzyme and is required for the production of e
25 hich enhances the coimmunoprecipitation of a decapping enzyme complex (Dcp1p and Dcp2p) with the mRNA
26 sic ligases, is highly effective as a DNA 3' decapping enzyme, converting DNAppG to DNA3'p and GMP.
29 le to stimulate the activity of the purified decapping enzyme Dcp1 in an in vitro decapping assay.
31 proteins co-immunoprecipitate with the mRNA decapping enzyme (Dcp1), a decapping activator (Pat1/Mrt
32 he Upf1-like group of helicases, but not the decapping enzymes DCP1a and DCP2, leads to potent inhibi
33 on of nonsense-containing mRNAs requires the decapping enzyme Dcp1p, the 5'-to-3' exoribonuclease Xrn
36 ex responsible for decapping consists of the decapping enzyme Dcp2 in association with decapping enha
40 pf1, Upf2, and Upf3X coimmunopurify with the decapping enzyme Dcp2, the putative 5'-->3' exonuclease
41 e is principally removed by the Nudix family decapping enzyme Dcp2, yielding a 5'-monophosphorylated
46 methylated caps in contrast to the canonical decapping enzyme, Dcp2, which targets mRNAs with a methy
51 mologue of the yeast Dcp2 protein is an mRNA decapping enzyme demonstrated to contain intrinsic decap
52 e mammalian and fungal noncanonical DXO/Rai1 decapping enzymes efficiently remove NAD(+) caps, and co
55 d Mohr (2015) describe how two poxvirus mRNA decapping enzymes hijack a host 5'-to-3'-exoribonuclease
57 pm2p interacts with Dcp2p, a subunit of mRNA decapping enzyme in the two-hybrid assay, and is enriche
58 strate mammalian cells possess multiple mRNA decapping enzymes, including Nudt16 to regulate mRNA tur
60 unstable and stable mRNAs in yeast when the decapping enzyme is compromised by temperature-sensitive
62 nized during development, with two different decapping enzymes localized in distinct cytoplasmic doma
64 cells infected with a vaccinia virus (VACV) decapping enzyme mutant and by wild-type virus colocaliz
65 mic viral factories in cells infected with a decapping enzyme mutant as well as with wild-type VACV a
66 phorylation earlier and more strongly than a decapping enzyme mutant even though less dsRNA was made,
68 t cause by inactivation of Xrn1, whereas the decapping enzyme mutant still exhibited defects in gene
70 t, the previously reported Xenopus nucleolar decapping enzyme, Nudt16, is an ubiquitous cytoplasmic d
72 subsequent work was demonstrated to encode a decapping enzyme or a necessary component of a decapping
73 a yeast gene, termed DCP1, that encodes the decapping enzyme, or an essential component of a decappi
75 p2p is required for the production of active decapping enzyme, perhaps in a process requiring the hyd
76 urrently believed to be the only cytoplasmic decapping enzyme responsible for decapping of all mRNAs.
77 hree proteins that exist in complex with the decapping enzyme subunits hDcp2 and hDcp1: hEdc3, Rck/p5
79 tely affected mRNA decapping in vivo yielded decapping enzymes that had at least the same specific ac
80 ination of alleles within this group yielded decapping enzymes that showed a strong loss of function
82 cay of many yeast mRNAs; the activity of the decapping enzyme therefore plays a significant role in d
83 box protein Dhh1 regulates the access of the decapping enzyme to the m(7)G cap by modulating the stru
87 fy proteins that control the activity of the decapping enzyme, which is encoded by the DCP1 gene, we
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