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1 homology to MBD2 and MBD3, but it lacks the methyl-CpG binding domain.
2 MBD3 and 38% identical to MBD2 but lacks the methyl-CpG binding domain.
3 eins (MBD2, MBD3, and MBD4) that contain the methyl-CpG binding domain.
4 homology to MBD2 and MBD3, but it lacks the methyl-CpG-binding domain.
5 are closely related proteins with consensus methyl-CpG binding domains.
8 RNA expression of brain and liver Dnmt3a and methyl CpG-binding domain 2 (Mbd2) protein as well as ce
10 sine-binding protein complex 1 that contains methyl-CpG-binding domain 2 protein (MBD2) in electropho
11 We demonstrate a key role for the protein methyl-CpG-binding domain-2 (Mbd2), which links DNA meth
12 Suppressor of Mek null (Smek) interact with methyl-CpG-binding domain 3 (Mbd3) and the complex plays
15 ermore, analyses of incorporated FdUrd using methyl-CpG-binding domain 4 glycosylase indicated that t
18 action sites for partner macromolecules: the methyl-CpG binding domain and the NCoR/SMRT interaction
19 are transcriptional repressors that contain methyl-CpG binding domains and are components of a CpG-m
20 MBD2 and MBD3 are two proteins that contain methyl-CpG binding domains and have a transcriptional re
21 unrelated mammalian protein that contains a methyl-CpG binding domain, can also efficiently remove t
24 tastasis-associated protein 1, MTA2, and the methyl-CpG-binding domain-containing protein, MBD3, were
26 isordered MeCP2 protein is restricted to the methyl-CpG binding domain; however, at least four region
28 MeCP2 binds to chromocentric DNA through its methyl CpG-binding domain (MBD) to regulate gene express
29 s two DNA binding domains, an amino-proximal methyl-CpG binding domain (MBD) and a C-terminal mismatc
30 NA interactions is that only proteins with a methyl-CpG binding domain (MBD) can interact with methyl
33 syndrome mutations at known sites within the methyl-CpG binding domain (MBD) impair binding to methyl
34 odifications were assayed for binding to the methyl-CpG binding domain (MBD) of one member of the MBP
36 ng with a RTT-causing mutation in either the methyl-CpG binding domain (MBD) or the transcriptional r
41 The gene for MeCP2 has been cloned and a methyl-CpG binding domain (MBD) within it has been defin
46 Transfection of a MED1 mutant lacking the methyl-CpG-binding domain (MBD) is associated with micro
51 stable gene repression, mediated in part by methyl-CpG-binding domain (MBD) proteins that recruit co
52 e defined as: DNA methyltransferases (DNMT), methyl-CpG-binding domain (MBD) proteins, histone acetyl
56 , although a family of proteins containing a methyl-CpG-binding domain (MBD), of which MeCP2 is the b
59 he number and variety of proteins containing methyl-CpG binding domains (MBDs) that are encoded in an
61 ected an association with a highly conserved methyl-CpG-binding domain missense variant, p.79Gly>Glu
62 homology domain of Dnmt3a interacts with the methyl CpG binding domain of Mbd3 and with both bromo an
64 The MBD1-CAF-1 p150 interaction requires the methyl-CpG binding domain of MBD1, and the association o
65 ecipitation of methylated DNA by recombinant methyl-CpG binding domain of MBD2 protein and sequencing
69 issense mutations were located either in the methyl-CpG-binding domain or in the transcription repres
74 G modification and capable of binding to the methyl-CpG binding domain protein 4 (MBD4) are able to i
76 Within the nucleus, FADD interacted with the methyl-CpG binding domain protein 4 (MBD4), which excise
78 h-specific thymine-DNA glycosylase (Tdg) and methyl-CpG binding domain protein 4 can both excise urac
81 target a specific sequence of dsDNA, while a methyl-CpG binding domain protein attached to the comple
82 LN promoter hypermethylation and reduces the methyl-CpG binding domain protein binding to RELN and GA
84 ylation of the CpG island and the binding of methyl-CpG-binding domain protein 2 (MBD2) and DNA methy
87 NA methyl-transferases (DNMTs) 3a and 3b and methyl-CpG-binding domain protein 2 (MBD2) to the Ankrd2
88 cing event is regulated by overexpression of methyl-CpG-binding domain protein 2 (MBD2), a key mediat
90 chromosomal region 2q23.1 that disrupt MBD5 (methyl-CpG-binding domain protein 5) contribute to a spe
93 ylated one in UOK181, is associated with the methyl CpG binding domain proteins (MBDs), MBD2 and MeCP
94 tionally repressive complexes, which include methyl-CpG binding domain proteins (MBDs) and histone de
95 tment to methylated cytosines of a family of methyl-CpG binding domain proteins (MBDs), which are dir
98 of novel DNA methyltransferase (SmDnmt2) and methyl-CpG-binding domain proteins mirrors the detection
99 family (MeCP2, MBD1, MBD2 and MBD4) share a methyl-CpG-binding domain that has a specific affinity f
100 r acting at CpG sites depends largely on its methyl-CpG-binding domain, which binds preferably to G.T
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