About: Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP

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rdf:type	Item
description	artikull shkencor (sq) artículu científicu (ast) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) наукова стаття (uk) article scientifique (fr) գիտական հոդված (hy) գիտական յօդուած (hyw) scientific article (en) מאמר אקדמי (he)
language of work or name	wds:Q27728960-86F7915F-EB06-4552-A184-7C1B35EF55ED
language of work or name	English
cites work	wds:Q27728960-0BC0018B-33ED-4EE4-990A-CC0B630DF33C wds:Q27728960-0BF7E967-506C-4CA3-A071-0C2EA046B7A2 wds:Q27728960-2F1950AC-92A8-4EE3-B4FF-57568AD16F43 wds:Q27728960-628DB128-A4AA-4F85-AE38-3E7D1ADEB3C6 wds:Q27728960-65EA2023-2F54-40E7-8595-17B238B72887 wds:Q27728960-6DB6A520-D165-4557-8D4E-16DFF04D8059 wds:Q27728960-6F18B1FE-6076-4456-B7FE-7CFE3EBE6613 wds:Q27728960-720385BE-110B-45B9-B4BB-9C8BBA907AFA wds:Q27728960-74F51490-EC87-401B-A807-01669E214624 wds:Q27728960-792FB9E0-D6F4-413B-922D-6D240BB89875 wds:Q27728960-7F215370-A866-4390-99BE-6E854E58A645 wds:Q27728960-94A8DE7F-9C38-45FB-9962-0F64A5CA86B4 wds:Q27728960-9A2394CE-4082-498F-9AAC-63CF2388C945 wds:Q27728960-D6A77985-E605-4C4E-863B-11CB617E86F9 wds:Q27728960-EB64FF0B-CEAC-47DF-B7EE-2A4D53C0AFD5 wds:Q27728960-EFD9E2D4-9434-4AAD-BF2F-A8C0F2D540A3 wds:Q27728960-F0022D01-23BD-493B-AAC7-E59DB7667C66 wds:Q27728960-FE50B1C4-7CB0-4452-BBC6-9ABD5E2844B8
cites work	The interpretation of protein structures: Estimation of static accessibility Construction of a plasmid that overproduces the large proteolytic fragment (Klenow fragment) of DNA polymerase I of Escherichia coli Structure of the cro repressor from bacteriophage lambda and its interaction with DNA. Selective Elimination of the Exonuclease Activity of the Deoxyribonucleic Acid Polymerase from Escherichia coli B by Limited Proteolysis Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 A resolution A graphics model building and refinement system for macromolecules Glucose-induced conformational change in yeast hexokinase Staphylococcal nuclease: Proposed mechanism of action based on structure of enzyme—thymidine 3′,5′-bisphosphate—calcium ion complex at 1.5-Å resolution polA6, a mutation affecting the DNA binding capacity of DNA polymerase I Mechanism of selective inhibition of 3' to 5' exonuclease activity of Escherichia coli DNA polymerase I by nucleoside 5'-monophosphates Crystallographic studies of protein-nucleic acid interaction: catabolite gene activator protein and the large fragment of DNA polymerase I. High resolution x-ray structure of yeast hexokinase, an allosteric protein exhibiting a non-symmetric arrangement of subunits Crystallization and 7 Å resolution electron density map of the large fragment of Escherichia coli DNA polymerase I On the processivity of DNA replication A fully active DNA polymerase I from Escherichia coli lacking stoichiometric zinc An active fragment of DNA polymerase produced by proteolytic cleavage Structural similarity in the DNA-binding domains of catabolite gene activator and cro repressor proteins The operator-binding domain of lambda repressor: structure and DNA recognition
author name string	wds:Q27728960-00158146-5B02-44CB-A5B8-7313AD47EEFC wds:Q27728960-15AA326E-E5B0-4C74-9B1B-B69928DCA8A1 wds:Q27728960-7AC003E0-2207-4F0C-98BF-88E376352846 wds:Q27728960-CC102D96-F830-40E3-B9E5-4C508FB6C85D wds:Q27728960-D78C823D-5EAD-43A5-AC4D-5856C9E3C106
OpenCitations bibliographic resource ID	wds:Q27728960-743AC684-DFBB-42A2-9B67-30C3E5FA6901
OpenCitations bibliographic resource ID	https://w3id.org/oc/corpus/br/1235094
author name string	D L Ollis N G Xuong P Brick R Hamlin T A Steitz
OpenCitations bibliographic resource ID	1235094
rdfs:label	Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP (en) Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP (nl) Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP (ast)
skos:prefLabel	Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP (en) Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP (nl) Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP (ast)
name	Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP (en) Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP (nl) Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP (ast)
title	wds:Q27728960-E62B1027-D56D-4DCA-8C65-B9D290D1F462
title	Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP (en)
page(s)	wds:Q27728960-0FD686D5-A945-4154-81FA-0443BA188031
page(s)	762-6
instance of	wds:Q27728960-2E01E0DF-BEA8-41C4-AF3A-C65C92C034F8
instance of	scholarly article
main subject	wds:Q27728960-5E91DEA0-3FD7-43C1-8D7F-F4118C6486EB
main subject	Escherichia coli
PubMed ID	wds:Q27728960-3959480C-777F-4409-873B-90871C3F8D8C
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/3883192
PubMed ID	3883192
published in	wds:Q27728960-FABC2268-4E16-43E7-A394-6244DF723AE6
published in	Nature
issue	wds:Q27728960-13096DA0-AF0E-4106-9B60-43FE3E33994D
volume	wds:Q27728960-46586E6A-A1A4-4E26-9C1D-9A126F86F465
issue	6005
volume	313
DOI	wds:Q27728960-16CADA8C-4AAE-4F03-9465-E209D7CBF981
DOI	http://dx.doi.org/10.1038/313762A0
DOI	10.1038/313762A0
Springer Nature article ID	wds:Q27728960-1999D4D4-DDA1-4DF6-9698-69F2BB3F7C59
Dimensions Publication ID	wds:Q27728960-E93262D1-075A-43FA-934E-8AF808F51A45
Springer Nature article ID	10.1038/313762a0
Dimensions Publication ID	1045780752
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q27728960
is cites work of	Crystal structure of Thermus aquaticus DNA polymerase Structural basis for the 3'-5' exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism The 3'-5' exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction Primer-terminus stabilization at the 3'-5' exonuclease active site of phi29 DNA polymerase. Involvement of two amino acid residues highly conserved in proofreading DNA polymerases

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