Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity - Wikidata - awgldk - TriplyDB

Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity

Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity

http://www.wikidata.org/entity/Q27644058

about

De novo mutations in moderate or severe intellectual disability Structure of Vps75 and implications for histone chaperone function Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75 Crystal Structure of Malaria Parasite Nucleosome Assembly Protein: DISTINCT MODES OF PROTEIN LOCALIZATION AND HISTONE RECOGNITION Structural Analysis of Rtt106p Reveals a DNA Binding Role Required for Heterochromatin Silencing Structure, localization and histone binding properties of nuclear-associated nucleosome assembly protein from Plasmodium falciparum Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face Two surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencing Histone chaperone specificity in Rtt109 activation.A DNA binding winged helix domain in CAF-1 functions with PCNA to stabilize CAF-1 at replication forks Ceramide induced mitophagy and tumor suppression Structural and functional analysis of novel human cytochrome C targets in apoptosis FTY720 induces apoptosis of M2 subtype acute myeloid leukemia cells by targeting sphingolipid metabolism and increasing endogenous ceramide levels 9q33.3q34.11 microdeletion: new contiguous gene syndrome encompassing STXBP1, LMX1B and ENG genes assessed using reverse phenotyping Interaction with the histone chaperone Vps75 promotes nuclear localization and HAT activity of Rtt109 in vivo.Identification of distinct SET/TAF-Ibeta domains required for core histone binding and quantitative characterisation of the interaction Histone chaperone activity of Arabidopsis thaliana NRP1 is blocked by cytochrome c The X-linked tumor suppressor TSPX interacts and promotes degradation of the hepatitis B viral protein HBx via the proteasome pathway.Cloning, purification, crystallization and preliminary X-ray crystallographic analysis of SET/TAF-Iß δN from Homo sapiens.Chaperone Nap1 shields histone surfaces used in a nucleosome and can put H2A-H2B in an unconventional tetrameric form.Phosphorylation of SET protein at Ser171 by protein kinase D2 diminishes its inhibitory effect on protein phosphatase 2A Molecular pathways undergoing dramatic transcriptomic changes during tumor development in the human colon.Histone chaperones in Arabidopsis and rice: genome-wide identification, phylogeny, architecture and transcriptional regulation.Histone chaperones, histone acetylation, and the fluidity of the chromogenome Roles of the Y chromosome genes in human cancers.Towards a mechanism for histone chaperones.Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochrome c.Eviction of linker histone H1 by NAP-family histone chaperones enhances activated transcription Promoter region-specific histone incorporation by the novel histone chaperone ANP32B and DNA-binding factor KLF5.Sphingosine analogue drug FTY720 targets I2PP2A/SET and mediates lung tumour suppression via activation of PP2A-RIPK1-dependent necroptosis.SET antagonist enhances the chemosensitivity of non-small cell lung cancer cells by reactivating protein phosphatase 2A B-cell acute lymphoblastic leukemia associated with SET-NUP214 rearrangement: A case report and review of the literature.Effect of leucine-to-methionine substitutions on the diffraction quality of histone chaperone SET/TAF-Ibeta/INHAT crystals Histone chaperones: an escort network regulating histone traffic.Direct interaction between the inhibitor 2 and ceramide via sphingolipid-protein binding is involved in the regulation of protein phosphatase 2A activity and signaling Histone chaperones in nucleosome eviction and histone exchange Expression of the Y-Encoded TSPY is Associated with Progression of Prostate Cancer.Histone chaperone networks shaping chromatin function.The histone shuffle: histone chaperones in an energetic dance.Sphingolipids and cancer: ceramide and sphingosine-1-phosphate in the regulation of cell death and drug resistance.

P2860

Q21144861-07919FAA-82C4-4CB2-8E73-92CC99CA0F14 Q27651775-DED62580-32C1-4B64-B7CB-5C1356CC8029 Q27653529-9A7CCF42-1B96-41D5-BE24-F637231DDA6B Q27653576-A571643D-78DA-472C-A8B5-3F0225A0197F Q27658650-AAFDCA2B-B5F7-423D-A708-07B69DFEA684 Q27660457-0F508E3F-9570-4E5F-AF20-A83C59214320 Q27664007-280F4DA3-D8C4-4D14-9FB4-0F80C43C1A30 Q27676464-AEF2A950-A242-4E73-ABB5-DCB515082439 Q27931083-A2BBDD02-B5E2-4E8E-8BDB-171F14054E64 Q28273583-20CF14F2-3C40-46DC-88EB-4A37260B8DDC Q28384389-BACDFBDF-B2C0-4F90-B2B7-5E12385E0D3F Q28387284-362F464C-D274-46A9-BD23-08F5353EB1D0 Q28541065-DC45B043-5F1D-4C5F-A82B-31BA52A3BA1A Q30355110-05968A98-A131-4305-A8B1-54DB36A7B46D Q30426269-2B0CC525-B13A-4A16-8396-56AEF4DAA08A Q33428755-FEC6E1B3-6BD7-49B0-A929-2CFD3FD1E748 Q33558339-DC41FE37-2672-4C37-858E-88FDD59870C3 Q33988130-09DB2894-47E8-45EF-9E03-4ABCBB25E59D Q34049166-55DCA7D0-8C5E-4E66-9E71-8C9A84A3B23B Q34366314-C39F6030-C579-4F2D-81E4-C7648CFADD38 Q34516277-36B74C61-B554-4D6B-83B2-51BDDE17F1D5 Q34518059-D01B1F29-B10F-4C94-B262-1C82343093B1 Q35169968-393FAB49-9617-472A-93C6-66A0FE0ABCC8 Q35253477-5874A97A-67B6-449B-8226-7ABCADE8C517 Q35604357-7F932ED0-C5CF-4157-B2D3-26BBB0D1BB14 Q35861914-9B3AB82F-ED25-47E1-ADF7-AF60014B1C5E Q35961467-6A56CCC3-9E61-4BD7-B01E-ECF951AAAE0F Q36022891-8F6197AB-B5F5-4D55-B057-46EFFD97763C Q36421370-F8411DD7-C9B9-478E-825F-6ADEFA068C45 Q36602177-E8EB050F-AA42-4E18-A4C4-7050CE124122 Q36729492-6A04931C-3031-4B36-A653-FA50842A113B Q36740935-ECE24A71-8117-415F-B6AE-6B9DF28268EB Q36930960-7A7BAF92-4592-4B58-9E05-45DD8CFDCB24 Q36994149-09684A49-76C5-456F-A49F-B4989F4E81C5 Q37123974-E2673088-9955-41BE-BFEB-EE224F43E6EB Q37183797-E53F7E35-EC92-4D76-8E81-0DC0E856436C Q37637012-D1084E97-C5DB-48F4-90DC-2FC22013B6D6 Q37656813-B0998435-FA22-4B69-902C-520BB3D5BF9E Q37731249-0DC58A6E-F8FF-4278-87DE-254FF7D2833E Q37808219-48133218-E779-4965-B34F-1D41A6B992A0

P2860

Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity

http://www.wikidata.org/entity/Q27644058

description

2007 nî lūn-bûn

@nan

2007 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի մարտին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity

@ast

Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity

@en

Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity

@nl

type

label

Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity

@ast

Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity

@en

Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity

@nl

prefLabel

Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity

@ast

Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity

@en

Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity

@nl

P1433

Q27644058-77235D83-6C18-431D-BF1F-A4688C1E93E3

P1476

Q27644058-2EE49897-A8C0-4247-85D9-F2405F921556

P2093

Q27644058-024C9E9C-0609-4700-B045-CC1B473B6C39

Q27644058-638B6B44-6AA2-4756-B621-96BEB89A7B9E

Q27644058-63A85638-7857-4F47-A1E1-1CB0835DDA34

Q27644058-7FF1AECF-7573-4723-8983-65E76F097721

Q27644058-BA1E1810-EB9E-4B89-AF9F-D89A93666FCE

Q27644058-C02DC47D-2FC6-4A6D-9560-E6C373D13D4A

Q27644058-C73CC3A3-75F3-4030-B929-6487DA12E661

Q27644058-F43949BC-8EE7-4303-BD83-59FB84519E32

P2860

Q27644058-070BC67A-A71B-4FE8-AA21-EF1FD1041F4C

Q27644058-0BDA1875-1C0A-453C-A0EF-6B8E60D60528

Q27644058-0C405CC0-C0C1-4ECC-A1AC-0D68F27A4248

Q27644058-0F416E26-1962-4D8A-B558-624FB63845E8

Q27644058-1498AF58-ACAD-419D-92D8-5C22E250206C

Q27644058-24DF6C7C-09CA-47FD-A0BA-2077A761373C

Q27644058-257B051B-1736-4D30-9EDA-A3F42D4B8C08

Q27644058-385CCB26-8139-42E8-BEFA-47F1B0AAE94C

Q27644058-3A79A01B-2619-47FE-A6DE-C634021E8BE6

Q27644058-44C663DB-A8BE-4FB6-A711-6F54C3BB824A

P304

Q27644058-D3F3F6CE-13E4-49EC-86F6-EB971EA31753

P31

Q27644058-8AAFCE1A-136D-4B9A-9C1C-54506867D333

P356

Q27644058-51E47B6D-BC7C-4372-B3C7-2FB4F22A0A8C

P407

Q27644058-E7784642-EEA4-4447-8A20-A62E1AC50D6F

P433

Q27644058-32254799-02CD-4881-B0F4-1711FB019387

P478

Q27644058-E65A7EB4-AB8B-48B1-B8F8-2FEEDBAED5C1

P577

Q27644058-C48CA161-B8CA-46DF-9565-4CED5613001C

P5875

Q27644058-2184AD91-C4B1-4EA5-B961-421F03C54D15

P698

Q27644058-72C88A25-05F4-4DAD-A9B8-C7CFB08C5C04

P921

Q27644058-A1DDF018-17AB-466B-ACD5-7B28334F5992

P932

Q27644058-EEB51691-924F-4498-99E7-E8D852753635

P356

PNAS.0603762104

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity

@en

P2093

Lui Sato

http://www.w3.org/2001/XMLSchema#string

Masami Horikoshi

http://www.w3.org/2001/XMLSchema#string

Miki Senda

http://www.w3.org/2001/XMLSchema#string

Ryozo Nagai

http://www.w3.org/2001/XMLSchema#string

Shinsuke Muto

http://www.w3.org/2001/XMLSchema#string

Toru Suzuki

http://www.w3.org/2001/XMLSchema#string

Toshiya Senda

http://www.w3.org/2001/XMLSchema#string

Yusuke Akai

http://www.w3.org/2001/XMLSchema#string

P2860

Requirement of RSF and FACT for transcription of chromatin templates in vitro

Translating the Histone Code

Crystal structure of the nucleosome core particle at 2.8 A resolution

Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks

Histone chaperones and nucleosome assembly

Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis

Structural basis for the interaction of Asf1 with histone H3 and its functional implications

Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3' half to different genes: characterization of the set gene

Recombinant human granzyme A binds to two putative HLA-associated proteins and cleaves one of them

Positive and negative regulation of the cardiovascular transcription factor KLF5 by p300 and the oncogenic regulator SET through interaction and acetylation on the DNA-binding domain

P304

4285-90

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1073/PNAS.0603762104

http://www.w3.org/2001/XMLSchema#string

P407

P433

11

http://www.w3.org/2001/XMLSchema#string

P478

104

http://www.w3.org/2001/XMLSchema#string

P577

2007-03-13T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

6445756

http://www.w3.org/2001/XMLSchema#string

P698

17360516

http://www.w3.org/2001/XMLSchema#string

P921

molecular chaperones

P932

1810507

http://www.w3.org/2001/XMLSchema#string