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Biophysical analysis of Thermus aquaticus single-stranded DNA binding protein.
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scholarly article
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Europe PubMed Central
PMC publication ID
2257892
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18065449%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 December 2019
title
Biophysical analysis of Thermus aquaticus single-stranded DNA binding protein
(English)
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stated in
Europe PubMed Central
PMC publication ID
2257892
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18065449%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 December 2019
main subject
Thermus aquaticus
object named as
Thermus aquaticus
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inferred from title
author
Gregor Witte
series ordinal
1
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Europe PubMed Central
PMC publication ID
2257892
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18065449%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 December 2019
Ute Curth
series ordinal
3
object named as
Ute Curth
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stated in
Europe PubMed Central
PMC publication ID
2257892
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18065449%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 December 2019
author name string
Roman Fedorov
series ordinal
2
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stated in
Europe PubMed Central
PMC publication ID
2257892
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18065449%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 December 2019
language of work or name
English
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publication date
7 December 2007
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Europe PubMed Central
PMC publication ID
2257892
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18065449%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 December 2019
number of pages
11
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published in
Biophysical Journal
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stated in
Europe PubMed Central
PMC publication ID
2257892
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18065449%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 December 2019
volume
94
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stated in
Europe PubMed Central
PMC publication ID
2257892
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18065449%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 December 2019
issue
6
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stated in
Europe PubMed Central
PMC publication ID
2257892
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18065449%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 December 2019
page(s)
2269-2279
1 reference
stated in
Europe PubMed Central
PMC publication ID
2257892
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18065449%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 December 2019
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3D structure of Thermus aquaticus single-stranded DNA-binding protein gives insight into the functioning of SSB proteins
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Structure of the single-stranded DNA-binding protein SSB from Thermus aquaticus
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DNA polymerase III chi subunit ties single-stranded DNA binding protein to the bacterial replication machinery
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Identification and characterization of single-stranded-DNA-binding proteins from Thermus thermophilus and Thermus aquaticus - new arrangement of binding domains
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Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling
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Role of single-stranded DNA regions and Y-box proteins in transcriptional regulation of viral and cellular genes
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Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme contacts SSB to promote processive elongation and sliding clamp assembly
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29 May 2018
Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice.
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29 May 2018
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29 May 2018
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29 May 2018
Complexes of the single-stranded DNA-binding protein from Escherichia coli (Eco SSB) with poly(dT). An investigation of their structure and internal dynamics by means of electron microscopy and NMR.
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29 May 2018
Large-scale overproduction and rapid purification of the Escherichia coli ssb gene product. Expression of the ssb gene under lambda PL control.
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29 May 2018
Kinetics of binding of single-stranded DNA binding protein from Escherichia coli to single-stranded nuclei acids.
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29 May 2018
Amino acid 55 plays a central role in tetramerization and function of Escherichia coli single-stranded DNA binding protein.
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29 May 2018
Polar destabilization of DNA duplexes with single-stranded overhangs by the Deinococcus radiodurans SSB protein.
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17 August 2018
Sedimentation velocity method in the analytical ultracentrifuge for the study of protein-protein interactions.
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17 August 2018
Chimeras between single-stranded DNA-binding proteins from Escherichia coli and Mycobacterium tuberculosis reveal that their C-terminal domains interact with uracil DNA glycosylases
1 reference
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17 August 2018
Multiple binding modes of the single-stranded DNA binding protein from Escherichia coli as detected by tryptophan fluorescence and site-directed mutagenesis.
1 reference
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17 August 2018
A general method of analysis of ligand-macromolecule equilibria using a spectroscopic signal from the ligand to monitor binding. Application to Escherichia coli single-strand binding protein-nucleic acid interactions.
1 reference
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17 August 2018
Common fold, common function, common origin?
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18065449
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Interaction of E. coli single-stranded DNA binding protein (SSB) with exonuclease I. The carboxy-terminus of SSB is the recognition site for the nuclease
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18065449
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Characterization of the Escherichia coli SSB-113 mutant single-stranded DNA-binding protein. Cloning of the gene, DNA and protein sequence analysis, high pressure liquid chromatography peptide mapping, and DNA-binding studies
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18065449
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Modulation of the affinity of the single-stranded DNA-binding protein of Escherichia coli (E. coli SSB) to poly(dT) by site-directed mutagenesis
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18065449
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1529/BIOPHYSJ.107.121533
1 reference
stated in
Europe PubMed Central
PMC publication ID
2257892
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18065449%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 December 2019
PMC publication ID
2257892
1 reference
stated in
Europe PubMed Central
PMC publication ID
2257892
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18065449%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 December 2019
PubMed publication ID
18065449
1 reference
stated in
Europe PubMed Central
PMC publication ID
2257892
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:18065449%20AND%20SRC:MED&resulttype=core&format=json
retrieved
29 December 2019
ResearchGate publication ID
5783777
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