about
Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactionsATRX-mediated chromatin association of histone variant macroH2A1 regulates α-globin expressionWSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activityPro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repressionMolecular basis underlying histone H3 lysine-arginine methylation pattern readout by Spin/Ssty repeats of Spindlin1ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppressionMolecular basis for CPAP-tubulin interaction in controlling centriolar and ciliary lengthYng1 PHD Finger Binding to H3 Trimethylated at K4 Promotes NuA3 HAT Activity at K14 of H3 and Transcription at a Subset of Targeted ORFsStructure of an argonaute silencing complex with a seed-containing guide DNA and target RNA duplex.Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD fingerNucleation, propagation and cleavage of target RNAs in Ago silencing complexes.Structural and functional insights into 5′-ppp RNA pattern recognition by the innate immune receptor RIG-IATRX ADD domain links an atypical histone methylation recognition mechanism to human mental-retardation syndromeMolecular basis for histone N-terminal methylation by NRMT1Multivalent engagement of chromatin modifications by linked binding modulesATRX tolerates activity-dependent histone H3 methyl/phos switching to maintain repetitive element silencing in neuronsJMJD5 (Jumonji Domain-containing 5) Associates with Spindle Microtubules and Is Required for Proper Mitosis.Divergent lncRNAs Regulate Gene Expression and Lineage Differentiation in Pluripotent Cells.Histone H3 recognition and presentation by the WDR5 module of the MLL1 complexChemical basis for the recognition of trimethyllysine by epigenetic reader proteins.Developing Spindlin1 small-molecule inhibitors by using protein microarrays.Reading between the Lines: "ADD"-ing Histone and DNA Methylation Marks toward a New Epigenetic "Sum".Multifaceted Histone H3 Methylation and Phosphorylation Readout by the Plant Homeodomain Finger of Human Nuclear Antigen Sp100C.PRMT5-mediated methylation of histone H4R3 recruits DNMT3A, coupling histone and DNA methylation in gene silencing.Conserved TCP domain of Sas-4/CPAP is essential for pericentriolar material tethering during centrosome biogenesis.Targeting epigenetic regulators for cancer therapy.Kinetic and high-throughput profiling of epigenetic interactions by 3D-carbene chip-based surface plasmon resonance imaging technology.Structural and biochemical characterization of DAXX-ATRX interaction.The BAH domain of BAHD1 is a histone H3K27me3 reader.Berberine binds RXRα to suppress β-catenin signaling in colon cancer cells.pH-profile crystal structure studies of C-terminal despentapeptide nitrite reductase from Achromobacter cycloclastes.Systematic Profiling of Histone Readers in Arabidopsis thaliana.Molecular basis for histidine N1 position-specific methylation by CARNMT1.Identification of a Mycothiol-Dependent Nitroreductase from Mycobacterium tuberculosis.Crystal structure of C-terminal desundecapeptide nitrite reductase from Achromobacter cycloclastes.Expanding RNA binding specificity and affinity of engineered PUF domains.Design, synthesis, structure-activity relationships study and X-ray crystallography of 3-substituted-indolin-2-one-5-carboxamide derivatives as PAK4 inhibitors.Gas41 links histone acetylation to H2A.Z deposition and maintenance of embryonic stem cell identity.Cancer-driving H3G34V/R/D mutations block H3K36 methylation and H3K36me3-MutSα interactionPreliminary crystallographic studies of two C-terminally truncated copper-containing nitrite reductases from Achromobacter cycloclastes: changed crystallizing behaviors caused by residue deletion
P50
Q24303887-E4166A2A-8E72-4FE8-A8A2-3A39A28B8A38Q24306749-956D53A7-C387-4071-9EB2-4F964CB8982CQ24309061-2E157D39-9BA2-4C3A-B6F0-48407E43D6AFQ24319024-5F3CA046-DD56-4541-8F27-8AB774E9E167Q24338569-CA081939-68CF-4A67-860C-97649DDFBA05Q24338606-B9EA1878-3C4E-483B-A7AD-461C0F8A4EABQ27313261-6ED6476C-6DF0-446E-A528-587B2D922ECFQ27640447-3185784F-2DF3-4008-9494-8A7EC4A3AE2BQ27653175-86E0FEA2-DA2C-4495-B028-383EB1AE63C7Q27655436-C9CDDE82-5F69-420B-8B39-6284D1449CACQ27657724-062E4232-8FB7-44AD-8584-9E4A58360CBBQ27662820-62FE49C4-FC14-49A2-A511-F66B0028A21AQ27670417-92C5587D-77EE-42DF-BDC5-CFE89DEFD048Q28116097-1E325636-C1F6-424F-8060-5F1FFCFBD0B5Q29617236-EDFAEBEF-D1EE-451A-A6C0-21E3519ACD22Q30653780-FE4A70CF-BB8C-4F08-B247-A4E8084AB0D1Q30734435-DA892468-6CBD-42FF-9EB4-CF364617013FQ34519073-B2ECD4B9-5779-4D22-9A46-7C3A622D0C5CQ34546055-4A7ABD49-BB6D-41CE-8DBC-DCCDA6547DA5Q36358096-C7D16F91-52BF-4742-BCFA-4A6ECCC373C4Q36371775-D649FC85-E4EF-46C3-80F1-D27069CFBB43Q36703430-DF8E7A0E-0F78-4D41-A187-B9F4E16ED091Q37066533-134C2AA6-B21E-410D-A5D0-1B4A2DFCCEB4Q37432768-D53903C1-9553-4F0B-AD17-40F963F2A708Q37519676-CAC4A58B-9516-48E5-81B9-F15FB3C92F78Q38191266-0A8A1CFE-D279-497E-BFEE-7B93CAC61700Q41614015-6F42A0C9-0C36-4F2B-9316-807FB6115162Q42704634-51ED311C-5E3C-41A0-90CC-0535023FD461Q42954790-27C959BD-9BDA-4094-B039-EAD290F87C7CQ47152429-191B697D-9667-4BE4-BEEA-C2C2CECB550BQ47994580-61CA3A55-B596-4FEA-AAD6-4301FB953668Q49547159-7303AD69-93E7-4C43-A37D-F73482B00E95Q49789002-38BB70A4-A4A1-4EB5-8BA8-200B3892670CQ52375535-F63419E1-AC92-46D9-B38D-246EF4CDA427Q52567240-C75CC4C7-45EE-4DDF-A45C-8622AAF5CCDEQ52681299-D0ECC399-BBC6-4792-9D2A-5E9468D65383Q54976615-A275F169-CCBF-4CF8-B948-502956EBFA2FQ55100850-B005B1D8-E655-46AA-BC90-D977DFDCA89BQ57978722-B37A5C22-6E0C-458E-9394-2117EB013A8BQ57978753-76F6033D-E5A0-41B8-9B4E-D8B38342B71F
P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Haitao Li
@ast
Haitao Li
@en
Haitao Li
@es
Haitao Li
@fr
Haitao Li
@nl
Haitao Li
@sl
type
label
Haitao Li
@ast
Haitao Li
@en
Haitao Li
@es
Haitao Li
@fr
Haitao Li
@nl
Haitao Li
@sl
altLabel
Hai-Tao Li
@en
prefLabel
Haitao Li
@ast
Haitao Li
@en
Haitao Li
@es
Haitao Li
@fr
Haitao Li
@nl
Haitao Li
@sl
P1053
B-2668-2012
P106
P1153
39861627900
P31
P3829
P496
0000-0001-6741-293X