Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo - Test2 - elhamkhani - TriplyDB

Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo

Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo

http://www.wikidata.org/entity/Q42551223

about

Histone ubiquitylation and its roles in transcription and DNA damage response Direct screening for chromatin status on DNA barcodes in yeast delineates the regulome of H3K79 methylation by Dot1 DOT1L safeguards cartilage homeostasis and protects against osteoarthritis.Identification of a functional hotspot on ubiquitin required for stimulation of methyltransferase activity on chromatin.Chemical tagging and customizing of cellular chromatin states using ultrafast trans-splicing inteins Dot1 histone methyltransferases share a distributive mechanism but have highly diverged catalytic properties.Evidence that ubiquitylated H2B corrals hDot1L on the nucleosomal surface to induce H3K79 methylation.The upstreams and downstreams of H3K79 methylation by DOT1L.The interplay of histone H2B ubiquitination with budding and fission yeast heterochromatin.The ribosome: A hot spot for the identification of new types of protein methyltransferases.Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome

P2860

Q28081194-81B30F34-997B-45C3-A54D-5E703266CCFB Q28818751-DC606A16-01B6-4533-9844-23B7475AEE34 Q33827165-ED249F5A-9AF1-4633-A6B6-1747093C0981 Q35990073-A8D16360-FDD2-4C06-8BB0-54708667B7E3 Q36198433-969FCC5E-CEB1-4267-94A7-74267798C1EC Q36293950-D7777F4F-8B38-4295-AC18-745DCEA3C55F Q36542574-AF8D8686-68CF-465B-AE72-8EDFD7E225A1 Q38686217-7EDFB013-1F3E-47BE-AFAD-60384167C5EB Q49723158-26C2A1A7-7B32-433E-B17F-8CDFEE36FB77 Q55511922-DCD4256F-D377-4633-836C-EED0A9F05CAF Q56530225-491230FF-D79D-44D7-98BC-9FB0C4C04866

P2860

Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo

http://www.wikidata.org/entity/Q42551223

description

2014 nî lūn-bûn

@nan

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

2014年论文

@zh

2014年论文

@zh-cn

name

Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo

@en

Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo

@nl

type

label

Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo

@en

Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo

@nl

prefLabel

Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo

@en

Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo

@nl

P1433

Q42551223-993C7008-0F82-4B42-A6A9-421D60F278FA

P1476

Q42551223-48500DD4-3A35-471F-9F9B-C894E80A3F2D

P2093

Q42551223-63E264D1-92F7-4F8C-8C36-C59A373B59BC

Q42551223-F14342F8-41BD-487D-B4E1-62BF2BBB6B67

P2860

Q42551223-0016C6CA-9455-486A-B142-DE76758FE224

Q42551223-04ECF6C6-005B-4534-B1BE-F84DF43D433B

Q42551223-084385E2-FFED-47BC-9052-DC5999FE29E3

Q42551223-0E1B5ED0-E88F-4994-B01A-2A63DBBD1754

Q42551223-0E9F761B-FDCA-4488-8F69-1E4058312D0B

Q42551223-1A1A15AC-D078-42F4-9757-478E4AA1ED54

Q42551223-1B6F8EDF-77A0-4E50-84CB-04D034918246

Q42551223-1FB000D0-20C2-4F60-B930-674126068AA4

Q42551223-3F664BCB-87D1-4654-BCDD-1ADFFF9BAF8C

Q42551223-432A7E03-B3A3-4798-A63E-75A2054463A4

P304

Q42551223-2D8B378A-D0C0-4E79-9852-3CF67AF349C8

P31

Q42551223-C7D2BA84-B4AB-44DD-9CE3-728AC6BA35F9

P356

Q42551223-CFF75336-FA61-46A9-A971-929D2097F1F5

P433

Q42551223-BE6FD2FF-6432-4898-9F13-57525D539FE1

P478

Q42551223-464EA6B2-D5E5-4040-8B8A-665B82C6A745

P50

Q42551223-67C3B0F7-BC66-4665-A4BD-9EBF02AF89B1

Q42551223-6A22D324-2B03-4C01-BFE8-CE69E3342EBA

Q42551223-7DE30F91-69D8-4AF0-A83A-BF5B571B88CD

Q42551223-82A46DB5-ED8A-4D48-A2EB-06E7020D47C5

Q42551223-C7E3626D-8DA6-46FB-9001-08264E8BBDB7

Q42551223-D856E280-ABC4-4570-B312-799282AEFC8F

P577

Q42551223-8C5EF71F-5F31-4856-B1C8-ECF40C5545D0

P5875

Q42551223-C22281EB-98E0-4A3D-B377-4E73076ABF38

P698

Q42551223-8AFE7DCD-BAB7-40E8-8F4E-EEDEA233E570

P921

Q42551223-756AC773-C3FC-4F4E-8918-1C50F1DF2F11

P932

Q42551223-3FADFDE2-DD36-4CD4-9EC0-67E3D19688AA

P356

P1433

P1476

Flexibility in crosstalk between H2B ubiquitination and H3 methylation in vivo

@en

P2093

Pedro A San-Segundo

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

Tibor van Welsem

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

P2860

Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation

RNF168 ubiquitinates K13-15 on H2A/H2AX to drive DNA damage signaling

Histone H2A deubiquitinase activity of the Polycomb repressive complex PR-DUB

Structure of monoubiquitinated PCNA and implications for translesion synthesis and DNA polymerase exchange

Interplay of chromatin modifiers on a short basic patch of histone H4 tail defines the boundary of telomeric heterochromatin

Transcriptional activation via sequential histone H2B ubiquitylation and deubiquitylation, mediated by SAGA-associated Ubp8.

The DNA damage checkpoint response requires histone H2B ubiquitination by Rad6-Bre1 and H3 methylation by Dot1.

Context dependency of Set1/COMPASS-mediated histone H3 Lys4 trimethylation.

MLL-AF9-induced leukemogenesis requires coexpression of the wild-type Mll allele.

Ubp10/Dot4p regulates the persistence of ubiquitinated histone H2B: distinct roles in telomeric silencing and general chromatin.

P304

1077-1084

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

P31

scholarly article

P356

10.15252/EMBR.201438793

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

P433

10

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

P478

15

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

P50

Albert J.R. Heck

Fred van Leeuwen

Maarten Altelaar

Erik L de Graaf

Hanneke Vlaming

P577

2014-08-20T00:00:00Z

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

P5875

264900714

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

P698

25141862

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

P921

protein ubiquitination

P932

4253848

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