Exchange of associated factors directs a switch in HBO1 acetyltransferase histone tail specificity. - Test2 - elhamkhani - TriplyDB

Exchange of associated factors directs a switch in HBO1 acetyltransferase histone tail specificity.

Exchange of associated factors directs a switch in HBO1 acetyltransferase histone tail specificity.

http://www.wikidata.org/entity/Q34373248

about

Studying epigenetic complexes and their inhibitors with the proteomics toolbox Keep-ING balance: tumor suppression by epigenetic regulation A PWWP domain-containing protein targets the NuA3 acetyltransferase complex via histone H3 lysine 36 trimethylation to coordinate transcriptional elongation at coding regions.Regulation of KAT6 Acetyltransferases and Their Roles in Cell Cycle Progression, Stem Cell Maintenance, and Human Disease Mutations in the Chromatin Regulator Gene BRPF1 Cause Syndromic Intellectual Disability and Deficient Histone Acetylation Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2 Expression atlas of the multivalent epigenetic regulator Brpf1 and its requirement for survival of mouse embryos.The MOZ histone acetyltransferase in epigenetic signaling and disease.Deficiency of the chromatin regulator BRPF1 causes abnormal brain development.The lysine acetyltransferase activator Brpf1 governs dentate gyrus development through neural stem cells and progenitors.The chromatin regulator Brpf1 regulates embryo development and cell proliferation The novel function of JADE1S in cytokinesis of epithelial cells.Bivalent interaction of the PZP domain of BRPF1 with the nucleosome impacts chromatin dynamics and acetylation.The Chromatin Regulator BRPF3 Preferentially Activates the HBO1 Acetyltransferase but Is Dispensable for Mouse Development and Survival.The TIP60 Complex Regulates Bivalent Chromatin Recognition by 53BP1 through Direct H4K20me Binding and H2AK15 Acetylation.SCF(JFK) is a bona fide E3 ligase for ING4 and a potent promoter of the angiogenesis and metastasis of breast cancer.ING5 is phosphorylated by CDK2 and controls cell proliferation independently of p53 BRPF3-HBO1 regulates replication origin activation and histone H3K14 acetylation The Enok acetyltransferase complex interacts with Elg1 and negatively regulates PCNA unloading to promote the G1/S transition BRPF1 is essential for development of fetal hematopoietic stem cells Crosstalk between epigenetic readers regulates the MOZ/MORF HAT complexes.Histone target selection within chromatin: an exemplary case of teamwork.Myst2/Kat7 histone acetyltransferase interaction proteomics reveals tumour-suppressor Niam as a novel binding partner in embryonic stem cells Histone H3K4 trimethylation: dynamic interplay with pre-mRNA splicing.Selective targeting of Bromodomains of the Bromodomain-PHD Fingers family impairs osteoclast differentiation.Biological function and histone recognition of family IV bromodomain-containing proteins.Structure, function and regulation of jade family PHD finger 1 (JADE1).The PZP Domain of AF10 Senses Unmodified H3K27 to Regulate DOT1L-Mediated Methylation of H3K79.KATapulting toward Pluripotency and Cancer.Widespread colocalization of the Drosophila histone acetyltransferase homolog MYST5 with DREF and insulator proteins at active genes.Phosphorylated HBO1 at UV irradiated sites is essential for nucleotide excision repair.The histone acetyltransferase Myst2 regulates Nanog expression, and is involved in maintaining pluripotency and self-renewal of embryonic stem cells.Combined Action of Histone Reader Modules Regulates NuA4 Local Acetyltransferase Function but Not Its Recruitment on the Genome.1,3-Dimethyl Benzimidazolones Are Potent, Selective Inhibitors of the BRPF1 Bromodomain.UV Damage-Induced Phosphorylation of HBO1 Triggers CRL4DDB2-Mediated Degradation To Regulate Cell Proliferation.Critical genomic regulation mediated by Enhancer of Polycomb.Chromatin Regulation by the NuA4 Acetyltransferase Complex Is Mediated by Essential Interactions Between Enhancer of Polycomb (Epl1) and Esa1.The scaffolding protein JADE1 physically links the acetyltransferase subunit HBO1 with its histone H3/H4 substrate.Histone acetyltransferase 7 (KAT7)-dependent intragenic histone acetylation regulates endothelial cell gene regulation.Histone H3K4 and H3K36 Methylation Independently Recruit the NuA3 Histone Acetyltransferase in Saccharomyces cerevisiae.

P2860

Q26738885-F4D375A4-E1F5-43DF-84CA-BD63876463E2 Q26859017-4676327A-7819-491F-B6BF-FDB7567306E0 Q27935497-55698E38-0F3B-43C8-B43E-93946012A023 Q28079704-A5FF04E3-39EF-4E2E-8A97-10BCA08C288A Q29144895-E8BA9DF8-9DD3-4B6B-AD8B-59CCE8409534 Q33741122-B91FB8AF-F99E-4480-A9B5-0DBC6DB8A870 Q33784606-42D8688A-BB5D-4F95-8AEC-44B3BBF6B27A Q34410314-938EEEF2-F2F6-400A-AE10-9D8109E777A0 Q34457162-A3A3595A-334B-4838-A1AD-AE7D5738B0D7 Q34466505-E159AFCC-1B87-4F50-A9C9-7B76AC75E75B Q34467243-CB7139DE-7753-4127-9AA8-C5583436CD8E Q34483855-71A2BC8B-0EEF-4814-B8E3-12BD4F7CD181 Q34503700-D47D3EFA-39BC-4F71-8254-B33FF5FDBDA7 Q34505489-6EA0C1A4-7D2E-4DC3-8225-DA7F092ADE18 Q34525512-486015E6-B6C7-4F31-8870-362922E4F818 Q35228761-CF22FA3E-B7FC-4490-AEE8-6539788824F4 Q35599241-2B80255A-0A7A-461D-AF21-EB17465A18D0 Q35856245-AD4BE91F-D9D3-4DC4-B24A-AD2D0DD3EEE4 Q36955946-A6C3F1B0-39DF-4F41-880E-A0863E18DC7B Q37217478-B6A3177B-6A56-4E3F-AD1C-A908F3AC77D2 Q37655824-6D144C45-A56C-45A9-A632-8D10F0565446 Q38212003-D6BF8A04-0743-4279-B277-358527C37D49 Q38372140-0BBB2570-CA33-4C36-9760-E166BFC92095 Q38583533-386D8409-12D2-42BF-ABB3-54B791E6D804 Q38604141-DE0A9C6F-0A9E-48F9-ABDE-10A8F3D0EE08 Q38788315-72F6A5CF-763C-4E74-BB26-019ACF6971A5 Q38828242-8DFAEEF9-7F64-48AC-9FA4-CE4A87A82353 Q38830100-4655EAE1-CC02-46B0-9416-8BF93F1196F8 Q38976614-3AC08A7E-E8E4-4F10-BBCC-09C00868EB78 Q39984220-5F87CBE6-5B92-41F9-91D6-63A271A4FDBB Q41078209-9739D9CF-A514-4CF7-A728-9D12B4F68692 Q41287212-BFB1E4FB-4FBD-4EF3-AC31-628C3091DA8F Q41619794-7BC0FDFC-BEFF-4D97-B0ED-9B1D993ED822 Q42198254-FEDC73EB-C194-4DE4-A0BD-000403B0F806 Q43078967-D7D5AD40-4911-4849-ACC6-435601B53B21 Q46700411-72E11067-44E6-45B9-9D8F-D57B380AAF62 Q46751466-DEDBA23D-3DAF-497B-ABB1-CC2AA832DE1B Q49571760-185B7844-8EC8-441D-A08B-11F5640046C4 Q50134108-5B9333CE-23ED-47BB-B889-3FF8A7480A02 Q51177029-4A51F607-7702-4765-A96B-81DC7E8FA67F

P2860

Exchange of associated factors directs a switch in HBO1 acetyltransferase histone tail specificity.

http://www.wikidata.org/entity/Q34373248

description

2013 nî lūn-bûn

@nan

2013 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Exchange of associated factors ...... rase histone tail specificity.

@ast

Exchange of associated factors ...... rase histone tail specificity.

@en

Exchange of associated factors ...... rase histone tail specificity.

@nl

type

label

Exchange of associated factors ...... rase histone tail specificity.

@ast

Exchange of associated factors ...... rase histone tail specificity.

@en

Exchange of associated factors ...... rase histone tail specificity.

@nl

prefLabel

Exchange of associated factors ...... rase histone tail specificity.

@ast

Exchange of associated factors ...... rase histone tail specificity.

@en

Exchange of associated factors ...... rase histone tail specificity.

@nl

P1433

Q34373248-979AB3B2-2E06-450B-A775-8C45C6A7E339

P1476

Q34373248-435948A4-1E17-4033-945B-2B12311EBBBF

P2093

Q34373248-11AAE807-F903-475D-86AB-72B4C53F5CEE

Q34373248-1FE54326-2A8F-4EBD-88F6-5D2DE72BA8D3

Q34373248-413C7F73-3F6B-4D97-BD00-039D4F82BB35

Q34373248-444AC03A-D6BB-4014-A634-422B7756DFF1

Q34373248-6293CD1B-4F8C-4EDB-8627-D90C3DEDE4D7

Q34373248-73AC50C3-250B-4522-B3BC-6968E4604AC8

Q34373248-776F5852-7F7F-42DA-8814-48E9CE267D40

Q34373248-97CF9E1B-D751-4D0E-9C98-7C204A50178B

Q34373248-983D1B9D-971E-49F9-B21B-568458503E4F

Q34373248-A39532D7-E515-4EA1-BC61-81206E737C9C

P2860

Q34373248-0200C7CC-7053-4DBB-B053-6CED5655DC92

Q34373248-07172718-A841-4C28-8726-FCE4F1B5A480

Q34373248-19ADBA53-A687-4FED-BD16-FA3592A4E2D2

Q34373248-1BA9B5DA-ACBB-4183-A015-9F0F3A64C336

Q34373248-21F87372-6067-4E32-9FB4-6BBD86CB4F8D

Q34373248-25F32034-5219-479C-BBC5-31788D512A59

Q34373248-27B10225-61A1-4240-89B9-011869B05C11

Q34373248-2F9F67FD-8C3F-4CDD-8150-FB021E4023E9

Q34373248-33B6085F-11EA-492B-AD75-9635CEBD6C1A

Q34373248-3A43A726-B3DB-438D-B739-91145BFBA7C1

P304

Q34373248-EE4929D7-5F41-46D6-9A68-3EAB51B2E9F0

P31

Q34373248-9C2BBC55-258F-414C-9462-9BB19BEFD723

P356

Q34373248-ABB62E66-214B-410E-A6BD-847767769B9F

P433

Q34373248-8ECF2D76-A02D-4982-8900-29589DD4E0DE

P478

Q34373248-4CF944C2-5722-4875-9AC6-5BBC4247F6E3

P50

Q34373248-030C2263-988B-4FEA-A20F-E7C065411E43

Q34373248-382C99D1-0F4B-42B6-BB60-D192A5796111

Q34373248-5075E499-FF89-4A95-B6E3-C5DB25D0F9C9

Q34373248-B7E27A00-3CA7-45E1-985E-FAE7E8717E89

P577

Q34373248-6FB31A43-B673-4EED-807A-924995F00D47

P698

Q34373248-D15398B2-F307-45E1-9401-0941F360DB00

P921

Q34373248-13624F26-62D8-4FDA-A6D2-6BA5F95770F4

Q34373248-F60D970E-70FF-4E18-9754-DDC25197E5B9

Q34373248-FA29C010-24A8-4B95-8D86-FF2C3278AA30

Q34373248-FCFA6A6E-6E71-431E-9D8A-647D6B75C50D

P932

Q34373248-D67B8AEF-C684-4FB6-A499-5D78AD707DFE

P356

P1433

Genes & Development

P1476

Exchange of associated factors ...... erase histone tail specificity

@en

P2093

Brianna J Klein

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

Eric Paquet

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

France-Hélène Joncas

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

Kezhi Yan

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

Marie-Eve Lalonde

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

Michael Holliday

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

Nikita Avvakumov

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

Qiong Tong

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

Song Tan

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

Xiang-Jiao Yang

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

P2860

ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation

Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans

Histone recognition and large-scale structural analysis of the human bromodomain family

Molecular architecture of quartet MOZ/MORF histone acetyltransferase complexes

TRIM24 links a non-canonical histone signature to breast cancer

Recognition of unmodified histone H3 by the first PHD finger of bromodomain-PHD finger protein 2 provides insights into the regulation of histone acetyltransferases monocytic leukemic zinc-finger protein (MOZ) and MOZ-related factor (MORF)

ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression

Regulation of replication licensing by acetyltransferase Hbo1.

MOZ and MORF, two large MYSTic HATs in normal and cancer stem cells

The crystal structure of the ING5 PHD finger in complex with an H3K4me3 histone peptide

P304

2009-2024

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

P31

scholarly article

P356

10.1101/GAD.223396.113

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

P433

18

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

P478

27

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

P50

Tatiana G Kutateladze

P577

2013-09-01T00:00:00Z

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

P698

24065767

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

P921

Lysine acetyltransferase 7

histone H3-K14 acetylation

Inhibitor of growth family member 5

Bromodomain and PHD finger containing 1

P932

3792477

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