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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
1 reference
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PubMed
PubMed ID
2105492
retrieved
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 ID
2105492
retrieved
31 January 2017
author
Tom Curran
object named as
T. Curran
series ordinal
5
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author name string
C. Abate
series ordinal
1
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PubMed
PubMed ID
2105492
retrieved
31 January 2017
D. Luk
series ordinal
2
1 reference
stated in
PubMed
PubMed ID
2105492
retrieved
31 January 2017
R. Gentz
series ordinal
3
1 reference
stated in
PubMed
PubMed ID
2105492
retrieved
31 January 2017
F. J. Rauscher
series ordinal
4
1 reference
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PubMed
PubMed ID
2105492
retrieved
31 January 2017
language of work or name
English
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publication date
1 February 1990
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PubMed
PubMed ID
2105492
retrieved
31 January 2017
published in
Proceedings of the National Academy of Sciences of the United States of America
1 reference
stated in
PubMed
PubMed ID
2105492
retrieved
31 January 2017
volume
87
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stated in
PubMed
PubMed ID
2105492
retrieved
31 January 2017
page(s)
1032–1036
1 reference
stated in
PubMed
PubMed ID
2105492
retrieved
31 January 2017
issue
3
1 reference
stated in
PubMed
PubMed ID
2105492
retrieved
31 January 2017
cites work
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Avian sarcoma virus 17 carries the jun oncogene
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The role of the leucine zipper in the fos-jun interaction
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PubMed Central
reference URL
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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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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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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
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
Dynamic alterations occur in the levels and composition of transcription factor AP-1 complexes after seizure
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
Nucleoprotein complexes that regulate gene expression in adipocyte differentiation: direct participation of c-fos
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
The Fos complex and Fos-related antigens recognize sequence elements that contain AP-1 binding sites
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
Common DNA binding site for Fos protein complexesand transcription factor AP-1
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
New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues
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
Identifiers
DOI
10.1073/PNAS.87.3.1032
0 references
ADS bibcode
1990PNAS...87.1032A
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PMCID
53404
0 references
PubMed ID
2105492
1 reference
stated in
PubMed
PubMed ID
2105492
retrieved
31 January 2017
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