Expression and purification of the leucine zipper and DNA-binding domains of Fos and Jun: both Fos and Jun contact DNA directly (Q28580048)

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English	Expression and purification of the leucine zipper and DNA-binding domains of Fos and Jun: both Fos and Jun contact DNA directly	scientific journal article

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scholarly article

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PubMed publication ID

2105492

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31 January 2017

title

Expression and purification of the leucine zipper and DNA-binding domains of Fos and Jun: both Fos and Jun contact DNA directly (English)

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PubMed

PubMed publication ID

2105492

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31 January 2017

author

Tom Curran

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T. Curran

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5

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C. Abate

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1

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PubMed publication ID

2105492

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31 January 2017

D. Luk

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2

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PubMed publication ID

2105492

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31 January 2017

R. Gentz

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3

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PubMed publication ID

2105492

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31 January 2017

F. J. Rauscher

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4

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2105492

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31 January 2017

language of work or name

English

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publication date

1 February 1990

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PubMed publication ID

2105492

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31 January 2017

published in

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

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2105492

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31 January 2017

volume

87

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2105492

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issue

3

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PubMed

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2105492

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page(s)

1032–1036

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PubMed

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2105492

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31 January 2017

cites work

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Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated trans-acting factor

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Avian sarcoma virus 17 carries the jun oncogene

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17 March 2017

The role of the leucine zipper in the fos-jun interaction

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PubMed Central

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17 March 2017

Preferential heterodimer formation by isolated leucine zippers from fos and jun

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Candidate product of the FBJ murine osteosarcoma virus oncogene: characterization of a 55,000-dalton phosphoprotein

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Viral and cellular fos proteins are complexed with a 39,000-dalton cellular protein

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Fos and Jun: the AP-1 connection

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Codon usage patterns in Escherichia coli, Bacillus subtilis, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Drosophila melanogaster and Homo sapiens; a review of the considerable within-species diversity

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Fos-associated protein p39 is the product of the jun proto-oncogene

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Bioassay for trans-activation using purified human immunodeficiency virus tat-encoded protein: trans-activation requires mRNA synthesis

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The carboxy terminus of the viral Jun oncoprotein is required for complex formation with the cellular Fos protein

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Fos and Jun bind cooperatively to the AP-1 site: reconstitution in vitro

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FBR murine osteosarcoma virus. I. Molecular analysis and characterization of a 75,000-Da gag-fos fusion product

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Two distinct transcription factors bind to the HSV thymidine kinase promoter in vitro

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Leucine repeats and an adjacent DNA binding domain mediate the formation of functional cFos-cJun heterodimers

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The fos gene product undergoes extensive post-translational modification in eukaryotic but not in prokaryotic cells.

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Viral and cellular fos proteins: A comparative analysis

1 reference

stated in

PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2105492

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Parallel association of Fos and Jun leucine zippers juxtaposes DNA binding domains

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2105492

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Dynamic alterations occur in the levels and composition of transcription factor AP-1 complexes after seizure

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2105492

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Nucleoprotein complexes that regulate gene expression in adipocyte differentiation: direct participation of c-fos

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2105492

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The Fos complex and Fos-related antigens recognize sequence elements that contain AP-1 binding sites

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2105492

retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Common DNA binding site for Fos protein complexesand transcription factor AP-1

1 reference

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2105492

retrieved

12 December 2020

based on heuristic

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New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/2105492

retrieved

12 December 2020

based on heuristic

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Identifiers

DOI

10.1073/PNAS.87.3.1032

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ADS bibcode

1990PNAS...87.1032A

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PMC publication ID

53404

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PubMed publication ID

2105492

1 reference

stated in

PubMed

PubMed publication ID

2105492

retrieved

31 January 2017

 

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