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1 e C terminus of RAG2 contains a noncanonical PHD finger.
2 The ASH1 protein contains a SET domain and a PHD finger.
3 o RAG-1 are separable functions of the RAG-2 PHD finger.
4 that is dependent on histone binding by the PHD finger.
5 ylase activity, a property that requires the PHD fingers.
6 l role in determining the selectivity of the PHD fingers.
7 ne H3K4 and contain a set of uncharacterized PHD fingers.
8 of the histone and non-histone targeting by PHD fingers.
9 one 3 (H3K4me3) through a plant homeodomain (PHD) finger.
10 istones, by one of Aire's plant homeodomain (PHD) fingers.
13 -specific effect on expression of the double PHD fingers 3 (DPF3) of the BAF SWI/SNF complex as asses
14 ithin an intron of DPF3, encoding for Double PHD Fingers 3, a member of chromatin remodeling complexe
17 a conserved tryptophan residue in the RAG-2 PHD finger abolished binding to H3K4me3 and greatly impa
20 ough mutations in either the first or second PHD finger allow for Rpd3S complex formation, the assemb
21 dition of the PHD finger domain or the third PHD finger alone into MLL-ENL blocks the hematopoietic s
24 e, the first report that deregulation of the PHD finger, an 'effector' of specific histone modificati
25 s including a C-terminal SET domain, central PHD fingers, an N-terminal DNA-binding homology, and two
26 InsP-binding region of ING2 (consisting of a PHD finger and a polybasic region) revealed a number of
28 nteraction of KAP1 with HP1 and on an intact PHD finger and bromodomain of KAP1, suggesting that thes
32 stic three-pronged pocket of histone-binding PHD fingers and binds to methylated histone H3 tails.
33 ocalization signal (NLS), a SAND domain, two PHD fingers and four nuclear receptor targeting motifs.
34 ent domain that includes the CXXC domain and PHD fingers and is controlled by direct interactions wit
36 hy MLL translocation breakpoints exclude the PHD fingers and suggest a possible role for these domain
37 s consistently delete the plant homeodomain (PHD) fingers and more carboxyl terminal MLL sequences.
38 ative heterochromatin localization domain, a PHD finger, and a bromodomain, prevalent in factors invo
41 main (ASH1L(BD)), a plant homeodomain (ASH1L(PHD)) finger, and a bromo-adjacent homology (ASH1L(BAH))
45 noprecipitation experiments reveal that both PHD fingers are required for binding to H3K14ac in vivo
51 itate the functional characterization of new PHD fingers, as well as other protein families, solely b
54 of immunodeficiencies are located within the PHD finger, at either zinc-coordinating residues or resi
56 ectroscopic approaches to show that the Set3 PHD finger binds di- and trimethylated states of H3K4 wi
60 solution crystal structure of the mouse RAG2 PHD finger bound to H3K4me3 reveals the molecular basis
61 nsferase domain and the adjacent bromodomain/PHD finger (bromo/PHD) region of the transcriptional coa
62 a/TRIM33/Ectodermin and demonstrate that its PHD finger-bromodomain constitutes a multivalent histone
63 biquitinate its substrate Smad4 requires its PHD finger-bromodomain, as does its transcriptional repr
64 ribe a dual inhibitor of the bromodomain and PHD finger (BRPF) family member BRPF2 and the TATA box b
65 to increased H3K4me3 engagement by the BPTF PHD finger, but it is unknown if this mechanism has a br
68 allel alpha-helices and a plant homeodomain (PHD) finger, but their genetic role has not been previou
75 e provide evidence on the genomic scale that PHD fingers constitute a general class of effector modul
76 ining protein 24) and BRPF1 (bromodomain and PHD finger containing protein 1) are involved in the epi
77 URF was disabled by silencing of bromodomain PHD-finger containing transcription factor (BPTF), the l
78 ial readout for selective recruitment of the PHD finger-containing components of chromatin remodeling
79 he histone deacetylase HDAC1, Mrg15, and the PHD finger-containing Pf1 and show that this complex pla
85 ific functions of many of the over 100 human PHD finger-containing proteins are poorly understood.
86 volutionary conserved genes encoding nuclear PHD finger-containing proteins implicated in a variety o
92 s essential for viability and that the first PHD finger contributes to the preferred binding of PHD1-
94 rom PHF23, KDM5A and BPTF, suggests a common PHD finger-dependent mechanism that promotes leukemogene
95 ilarity to one another within the C-terminal PHD finger domain and also contain an additional N-termi
98 C (FLC), is critical for vernalization and a PHD finger domain protein, VERNALIZATION INSENSITIVE 3 (
99 cells is critically dependent on a conserved PHD finger domain, suggesting that Pcl2 might function t
101 se screens identified the plant homeodomain (PHD)-finger domain protein PHF5A as differentially requi
102 lt shows that the binding specificity of the PHD-finger domain of VIN3 plays a role in mediating a pr
103 alteration in the binding specificity of the PHD-finger domain of VIN3 results in a hypervernalizatio
105 subunit that contains the chromatin binding PHD finger domains attenuates enhancer functions, but un
111 H3 tail structure in complex with the double PHD finger (DPF) of the lysine acetyltransferase MOZ/MYS
112 ontaining C terminus of BRM binds to the CBP PHD finger, enhances PHD binding to histone H3, and enha
114 ventional PHD finger followed by an extended PHD finger exists in the mammalian AF10 protein, among a
115 A specific module containing a conventional PHD finger followed by an extended PHD finger exists in
117 on differences in binding affinities of the PHD fingers for H3K4me and the methylation state of the
118 y X-ray crystallography to show that the VEL PHD finger forms the central module of a larger compact
119 d protein that is homologous to the multiple PHD fingers found in the N-terminal regions of mammalian
121 3 ligases, reporting for the first time that PHD fingers from a nuclear protein exhibit E3 ubiquitin
122 analysis of the H3K4me3-binding sites of the PHD fingers from PHF23, KDM5A and BPTF, suggests a commo
123 l-characterized CBDs: the plant homeodomain (PHD) finger from ING2 and the chromodomain from heteroch
126 t correlation between the abilities of NUP98-PHD finger fusion chimeras to associate with H3K4me3-enr
127 rations to sites that differed from both the PHD finger fusion-directed and LEDGF-directed integratio
135 that contain one or more plant homeodomain (PHD) fingers have been implicated in the regulation of c
137 on as to how BCL9 co-factors binding to Pygo PHD fingers impact indirectly on their histone binding a
138 2.0 A resolution structure of the mouse ING2 PHD finger in complex with a histone H3 peptide trimethy
140 methylated at lysine 4 (H3K4me3) by the ING4 PHD finger in mediating ING4 gene expression and tumor s
143 talizing MLL fusion protein, the loss of the PHD fingers, in combination with the gain of the activat
144 d substitutions in either the bromodomain or PHD finger, including ones that mimic disease-causing mu
145 s to investigate the interaction of the ING3 PHD finger (ING3PHD) with the active transcription mark
146 e, expression of the fusion protein with the PHD finger insertion mediates the down-regulation of the
147 highlight the molecular mechanisms by which PHD fingers interact with ligands other than the amino t
150 a chimeric RAG-2 protein in which the mouse PHD finger is replaced by the corresponding domain from
152 t recognition of the histone H3 tails by the PHD fingers is required for repressive activity of the C
153 ur study suggests that a common function for PHD fingers is to transduce methyl-lysine events and she
154 ne 3 (H3)-tails by Aire's plant homeodomain (PHD) finger is essential for Aire function in cultured c
158 nal regulators, including plant homeodomain (PHD)-finger-like domains, and defines a plant-specific p
159 K4me2 recruits the Set3 complex via the Set3 PHD finger, localizing the Hos2 and Hst1 subunits to dea
161 MLL4, harboring its fourth, fifth and sixth PHD fingers (MLL4(PHD456)) forms an integrated module, m
162 y insertion" (L3MBTL1) and "surface groove" (PHD finger) modes of methyllysine recognition, a carboxy
164 rotein sequence shows strong homology to the PHD-finger motif found in known transcription factors fr
169 ), which bind methylated H3K4 (H3K4me3), the PHD finger of BHC80 binds unmethylated H3K4 (H3K4me0), a
171 d NMR structures of the bromodomain-proximal PHD finger of BPTF in free and H3(1-15)K4me3-bound state
175 This activity is conserved in the second PHD finger of MLL4, the closest homolog to MLL1 but not
177 ing PHD finger, such as the carboxy-terminal PHD finger of PHF23 or JARID1A (also known as KDM5A or R
178 one-binding activity is not conserved in the PHD finger of Set4 suggests different functions for the
179 ted screen for PI interactors identified the PHD finger of TAF3, a TATA box binding protein-associate
187 Our data support a critical role for the PHD fingers of NUP98-PHF23, and related NUP98-KDM5A and
193 the full-length protein reveals that the two PHD fingers of the dimer are chemically equivalent and i
194 (MBD5 and MBD6) that bind to the C-terminal PHD fingers of the large scaffold subunits ASXL1-3 and s
197 trimethylated at K4) by a plant homeodomain (PHD) finger of human BPTF (bromodomain and PHD domain tr
198 leoporin 98 and the third plant homeodomain (PHD) finger of JARID1A drives an oncogenic transcription
201 We recently found that plant homeodomain (PHD) finger of tumour suppressor ING2 (inhibitor of grow
202 a prime example of histone tail binding by a PHD finger (of Pygo) being modulated by a cofactor (BCL9
203 a unique chromatin regulator possessing two PHD fingers, one bromodomain and a PWWP domain for recog
204 Acf1 is a novel protein that contains two PHD fingers, one bromodomain, and two new conserved regi
208 at a cancer-associated mutation in the PHRF1 PHD finger (P221L) abolishes its histone interaction and
212 y express ATRX protein with mutations in the PHD finger (PHDmut) or helicase domains (K1584R), we exa
213 0, PFK, PHT1;4, PTR3, KUP2, GRAS, TCP, bHLH, PHD finger, PLATZ and genes involved in developmental, s
215 d long protein containing a SET domain, five PHD fingers, potential zinc fingers, and a very long run
216 istone methyl-lysine binding activity of the PHD fingers present within the Saccharomyces cerevisiae
218 as a quaternary complex with the bromodomain-PHD finger protein 1 (BRPF1), inhibitor of growth 5 (ING
219 We here report a PRC2-associated cofactor, PHD finger protein 19 (PHF19; also known as polycomb-lik
221 utative human homologs of Bye1, the proteins PHD finger protein 3 and death-inducer obliterator, whic
222 nds splicing factor 3B subunit 1 (SF3B1) and PHD finger protein 5A (PHF5A), the components of the hum
224 ls, forced expression of the testis-specific PHD finger protein 7 (PHF7) disrupts oogenesis, leading
225 logical processes and diseases revealed that PHD finger protein 8 (PHF8, KDM7B) was significantly ass
227 osophila identified pygopus, which encodes a PHD finger protein, as an additional nuclear component o
230 t of the BDP1/BDP2 complex and identified an PhD-finger protein (PHD 1, PF3D7_1008100) that could med
231 tified the co-chaperone SGT1b (EDM1) and the PHD-finger protein EDM2 as critical regulators of RPP7.
232 re we reveal that the ubiquitously expressed PHD-finger protein OBE3 forms a central module with the
235 ongs to a family of evolutionarily conserved PHD finger proteins thought to act as co-activators of W
238 mechanisms underlying this novel function of PHD fingers provides a basis for deciphering the role of
239 region consisting of a PHD finger-Zn knuckle-PHD finger (PZP) folds into a single module that recogni
243 itution within the aromatic cage of the BPTF PHD finger, resulting in a reversal of binding preferenc
244 ation of a novel transcript containing SNF2, PHD-finger, RING-finger, helicase, and linker histone do
249 ne H3 (H3K4me1) and seven plant homeodomain (PHD) fingers, six of which have not been structurally an
250 ing an H3K4-trimethylation (H3K4me3)-binding PHD finger, such as the carboxy-terminal PHD finger of P
252 s that the binding of Cyp33 to the MLL third PHD finger switches the MLL function from transactivatio
257 gene assembly--contains a plant homeodomain (PHD) finger that specifically recognizes histone H3 trim
258 LL protein contains three plant homeodomain (PHD) fingers that are well conserved between species but
260 putative double zinc-finger domain, called a PHD finger, that is present not only in the products of
261 BS69 contains regions of similarity to the PHD finger, the bromodomain, and the MYND domain, all of
262 KAP-1 contains a RING finger, B boxes, and a PHD finger; the RING-B1-B2 structure is required for KRA
266 erstand the path of allostery from the RAG-2 PHD finger to RAG-1, here we employed phylogenetic subst
267 crocyclic calixarenes can disrupt binding of PHD fingers to methylated lysine 4 of histone H3 in vitr
268 ochemical evidence for the utility of tandem PHD fingers to recruit protein complexes at targeted gen
270 tudy, we demonstrate the ability of the CHD5 PHD fingers to specifically recognize the unmodified N-t
273 ntrast to the PHD fingers of the bromodomain PHD finger transcription factor (BPTF) and inhibitor of
276 Here, we show that loss of BPTF (Bromodomain PHD Finger Transcription Factor), a core component of th
279 ging the polybasic regions between different PHD fingers we show that this region is a strong determi
280 the molecular basis of the integrated tandem PHD finger, which acts as one functional unit in the seq
281 antly, BP1 can directly bind DNA through its PHD finger, which might increase nucleosome residence an
283 ins four highly conserved plant homeodomain (PHD) fingers, which are invariably deleted in oncogenic
284 s preceded by a tandem of plant homeodomain (PHD) fingers whose biological roles and requirements for
285 rated a direct interaction of the chick Pcl2 PHD finger with EZH2, a component of the ESC/E(Z) repres
286 mechanism of multivalent association of the PHD fingers with chromatin and reveal their critical rol
287 raction of the C-terminal plant homeodomain (PHD) finger with histone H3 trimethylated at Lys4 (H3K4m
288 l beta-sheet formation on the surface of the PHD finger, with the long side chains of arginine 2 (R2)