Structural basis for ELL2 and AFF4 activation of HIV-1 proviral transcription

about

Crystal structure of the tricellulin C-terminal coiled-coil domain reveals a unique mode of dimerization.Aberrant activation of non-coding RNA targets of transcriptional elongation complexes contributes to TDP-43 toxicity

P2860

Q50917009-7A16234C-6EBC-47CF-9918-468A647A0D97 Q57798875-2F5C9FAF-4A70-4666-9044-8E4C606646F1

P2860

Structural basis for ELL2 and AFF4 activation of HIV-1 proviral transcription

Item

http://www.wikidata.org/entity/Q37622516

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 30 January 2017

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Structural basis for ELL2 and AFF4 activation of HIV-1 proviral transcription

@en

Structural basis for ELL2 and AFF4 activation of HIV-1 proviral transcription.

@nl

type

Item

label

Structural basis for ELL2 and AFF4 activation of HIV-1 proviral transcription

@en

Structural basis for ELL2 and AFF4 activation of HIV-1 proviral transcription.

@nl

prefLabel

Structural basis for ELL2 and AFF4 activation of HIV-1 proviral transcription

@en

Structural basis for ELL2 and AFF4 activation of HIV-1 proviral transcription.

@nl

P1476

Structural basis for ELL2 and AFF4 activation of HIV-1 proviral transcription

@en

P2093

Goran Stjepanovic

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

James H Hurley

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

Qiang Zhou

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

Shiqian Qi

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

Zichong Li

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

P2860

A higher-order complex containing AF4 and ENL family proteins with P-TEFb facilitates oncogenic and physiologic MLL-dependent transcription

Selective inhibition of BET bromodomains

Crystal structure of HIV-1 Tat complexed with human P-TEFb

Transcriptional control of HIV latency: cellular signaling pathways, epigenetics, happenstance and the hope for a cure

Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding.

The AFF4 scaffold binds human P-TEFb adjacent to HIV Tat

Crystal structure of HIV-1 Tat complexed with human P-TEFb and AFF4

P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II

Latency reversal and viral clearance to cure HIV-1.

AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia.

P2888

ncomms14076

P304

14076

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

P31

scholarly article

P356

10.1038/NCOMMS14076

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

P407

English

P478

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

P50

Ursula Schulze-Gahmen

P577

2017-01-30T00:00:00Z

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

P698

28134250

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

P932

5290273

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

Structural basis for ELL2 and AFF4 activation of HIV-1 proviral transcription

about

P2860

P2860

Structural basis for ELL2 and AFF4 activation of HIV-1 proviral transcription

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P478

P50

P577

P698

P932