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Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP
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instance of
scholarly article
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title
Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP
(English)
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main subject
Escherichia coli
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author name string
D L Ollis
series ordinal
1
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P Brick
series ordinal
2
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R Hamlin
series ordinal
3
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N G Xuong
series ordinal
4
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T A Steitz
series ordinal
5
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language of work or name
English
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published in
Nature
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volume
313
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issue
6005
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page(s)
762-6
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cites work
polA6, a mutation affecting the DNA binding capacity of DNA polymerase I
1 reference
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reference URL
https://api.crossref.org/works/10.1038%2F313762A0
retrieved
21 January 2018
Selective Elimination of the Exonuclease Activity of the Deoxyribonucleic Acid Polymerase from Escherichia coli B by Limited Proteolysis
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7 January 2021
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An active fragment of DNA polymerase produced by proteolytic cleavage
1 reference
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https://api.crossref.org/works/10.1038%2F313762A0
retrieved
7 January 2021
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A fully active DNA polymerase I from Escherichia coli lacking stoichiometric zinc
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Mechanism of selective inhibition of 3' to 5' exonuclease activity of Escherichia coli DNA polymerase I by nucleoside 5'-monophosphates
1 reference
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7 January 2021
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Construction of a plasmid that overproduces the large proteolytic fragment (Klenow fragment) of DNA polymerase I of Escherichia coli
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Crystallization and 7 Å resolution electron density map of the large fragment of Escherichia coli DNA polymerase I
1 reference
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Crossref
reference URL
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retrieved
7 January 2021
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Crystallographic studies of protein-nucleic acid interaction: catabolite gene activator protein and the large fragment of DNA polymerase I.
1 reference
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A graphics model building and refinement system for macromolecules
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Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution
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High resolution x-ray structure of yeast hexokinase, an allosteric protein exhibiting a non-symmetric arrangement of subunits
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Staphylococcal nuclease: Proposed mechanism of action based on structure of enzyme—thymidine 3′,5′-bisphosphate—calcium ion complex at 1.5-Å resolution
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Structural similarity in the DNA-binding domains of catabolite gene activator and cro repressor proteins
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Structure of the cro repressor from bacteriophage lambda and its interaction with DNA.
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The operator-binding domain of lambda repressor: structure and DNA recognition
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On the processivity of DNA replication
1 reference
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7 January 2021
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inferred from DOI database lookup
Glucose-induced conformational change in yeast hexokinase
1 reference
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Crossref
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inferred from DOI database lookup
The interpretation of protein structures: Estimation of static accessibility
1 reference
stated in
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reference URL
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Identifiers
DOI
10.1038/313762A0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1235094
Dimensions Publication ID
1045780752
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OpenCitations bibliographic resource ID
1235094
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1235094
PubMed publication ID
3883192
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1235094
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