(Q45764450)

English

Hepatitis B virus X protein is a transcriptional modulator that communicates with transcription factor IIB and the RNA polymerase II subunit 5.

scientific article published in March 1997

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Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

Hepatitis B virus X protein is a transcriptional modulator that communicates with transcription factor IIB and the RNA polymerase II subunit 5. (English)

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

Hepatitis B virus

1 reference

based on heuristic

inferred from title

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based on heuristic

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author name string

Lin Y

1

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

Nomura T

2

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

Cheong J

3

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

Dorjsuren D

4

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

Iida K

5

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

Murakami S

6

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

language of work or name

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publication date

1 March 1997

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Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

number of pages

8

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Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

272

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Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

11

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Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

7132-7139

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

Hepatitis B virus HBx protein activates Ras-GTP complex formation and establishes a Ras, Raf, MAP kinase signaling cascade

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Multiple simian virus 40 enhancer elements mediate the trans-activating function of the X protein of hepatitis B virus

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Trans-activation of the human immunodeficiency virus long terminal repeat by the hepatitis B virus X protein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Transactivation by the hepatitis B virus X protein depends on AP-2 and other transcription factors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Hepatitis B virus X gene activates kappa B-like enhancer sequences in the long terminal repeat of human immunodeficiency virus 1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Trans-activation of HLA-DR gene by hepatitis B virus X gene product

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

HBx gene of hepatitis B virus induces liver cancer in transgenic mice

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Expression of the hepatitis B virus X gene in mammalian cells

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Hepatitis B virus transactivator protein X interacts with the TATA-binding protein.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

HBV X protein alters the DNA binding specificity of CREB and ATF-2 by protein-protein interactions

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

HBx protein of hepatitis B virus interacts with the C-terminal portion of a novel human proteasome alpha-subunit

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Hepatitis B virus X protein inhibits p53 sequence-specific DNA binding, transcriptional activity, and association with transcription factor ERCC3

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Transactivation by hepatitis B virus X protein is promiscuous and dependent on mitogen-activated cellular serine/threonine kinases.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Hepatitis B virus transactivator HBx uses a tumour promoter signalling pathway

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Transactivation of human hepatitis B virus X protein, HBx, operates through a mechanism distinct from protein kinase C and okadaic acid activation pathways

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Induction of the DNA-binding activity of c-jun/c-fos heterodimers by the hepatitis B virus transactivator pX

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Functional and structural similarity between the X protein of hepatitis B virus and nucleoside diphosphate kinases

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

The X protein of hepatitis B virus coactivates potent activation domains

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Highly conserved core domain and unique N terminus with presumptive regulatory motifs in a human TATA factor (TFIID).

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Sequence of general transcription factor TFIIB and relationships to other initiation factors

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Purification, cloning, and characterization of a human coactivator, PC4, that mediates transcriptional activation of class II genes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Activator-induced conformational change in general transcription factor TFIIB.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

A suppressor of TBP mutations encodes an RNA polymerase III transcription factor with homology to TFIIB.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Multiple functional domains of human transcription factor IIB: distinct interactions with two general transcription factors and RNA polymerase II.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

TFIIB, an evolutionary link between the transcription machineries of archaebacteria and eukaryotes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

The yeast SUA7 gene encodes a homolog of human transcription factor TFIIB and is required for normal start site selection in vivo.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Interaction between a transcriptional activator and transcription factor IIB in vivo.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

A direct interaction between a glutamine-rich activator and the N terminus of TFIIB can mediate transcriptional activation in vivo

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

TATA-binding protein residues implicated in a functional interplay between negative cofactor NC2 (Dr1) and general factors TFIIA and TFIIB.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Nuclear protein CBP is a coactivator for the transcription factor CREB

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Molecular cloning and expression of the 32-kDa subunit of human TFIID reveals interactions with VP16 and TFIIB that mediate transcriptional activation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Drosophila TAFII40 interacts with both a VP16 activation domain and the basal transcription factor TFIIB.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Delineation of two functional regions of transcription factor TFIIB.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Identification of the gene (SSU71/TFG1) encoding the largest subunit of transcription factor TFIIF as a suppressor of a TFIIB mutation in Saccharomyces cerevisiae

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Five intermediate complexes in transcription initiation by RNA polymerase II

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

An RNA polymerase II holoenzyme responsive to activators

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

A multiprotein mediator of transcriptional activation and its interaction with the C-terminal repeat domain of RNA polymerase II.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Association of an activator with an RNA polymerase II holoenzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Recycling of the general transcription factors during RNA polymerase II transcription

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

RNA polymerase II initiation factor interactions and transcription start site selection

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Model for binding of transcription factor TFIIB to the TBP-DNA complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Contact with a component of the polymerase II holoenzyme suffices for gene activation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.272.11.7132

21 January 2018

Identifiers

10.1074/JBC.272.11.7132

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

15 December 2017

http://europepmc.org/abstract/MED/9054408

ResearchGate publication ID

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