About: Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase

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scientific journal article

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rdf:type	Item
description	artículu científicu espublizáu en 2006 (ast) vědecký článek publikovaný v roce 2006 (cs) 2006 թվականի փետրվարին հրատարակված գիտական հոդված (hy) наукова стаття, опублікована в лютому 2006 (uk) 2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած (hyw) مقالة علمية (نشرت في فبراير 2006) (ar) vedecký článok (publikovaný 2006/02/01) (sk) wetenschappelijk artikel (gepubliceerd op 2006/02/01) (nl) scientific journal article (en) im Februar 2006 veröffentlichter wissenschaftlicher Artikel (de)
publication date	wds:Q28486499-8177A982-74C4-40C7-9099-03EA1B9283CE
publication date	2006-02-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q28486499-4E0DEE8B-09A8-428D-B813-D0731847770D
language of work or name	English
cites work	wds:Q28486499-0EF5E073-C453-4FD8-A9B9-C964A1D8DCFE wds:Q28486499-8062D6D3-3748-4A4A-9491-77A978857BEE wds:Q28486499-9D5BF5FA-CEC0-4DB4-A1ED-C0CBBFFF67A7 wds:Q28486499-AB6C0B52-0107-49E8-A6D7-C0F3C392AFE8 wds:Q28486499-C9DB9C92-2D65-4567-B74C-24CBF1B8594E
cites work	Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination Comparative study of purine and pyrimidine nucleoside analogues acting on the thymidylate kinases of Mycobacterium tuberculosis and of humans The control of synthesis of bacterial cell walls. Interaction in the synthesis of nucleotide precursors Nucleoside analogues as inhibitors of thymidylate kinases: possible therapeutic applications. Phosphorylation of ganciclovir phosphonate by cellular GMP kinase determines the stereoselectivity of anti-human cytomegalovirus activity
author name string	wds:Q28486499-77F81905-D0B9-4252-9372-BA9594B717B8 wds:Q28486499-A18EE888-CF45-43C7-AAE4-9994768CB840 wds:Q28486499-A5A46E01-CA6E-4CE1-8E9A-6413C0B636F7 wds:Q28486499-C7DB0F66-7736-4EF2-A077-7B2310B99E24 wds:Q28486499-D4ABE4C2-D675-4378-BA83-A3A411FC14AD wds:Q28486499-F48B31B8-8265-462D-8D88-76683E636DEA
author name string	Petya Christova Andrew Thompson Louis Renault Jacqueline Cherfils Edward Seclaman Guillaume Hible
rdfs:label	Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase (en) Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase (nl) Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase (ast)
skos:prefLabel	Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase (en) Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase (nl) Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase (ast)
name	Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase (en) Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase (nl) Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase (ast)
author	wds:Q28486499-281CD401-1008-45C9-B590-2FA258F1D3B6 wds:Q28486499-2ABC1271-196A-41DC-B0C1-AF5DC31A9F85
author	Hélène Munier-Lehmann Eric Girard
title	wds:Q28486499-0EA5F735-E46D-4283-9EF1-3ADFEB83BBA3
title	Unique GMP-binding site in Mycobacterium tuberculosis guanosine monophosphate kinase (en)
page(s)	wds:Q28486499-C9CE545E-95C3-4C91-BE63-62A2584FFAD8
page(s)	489–500
instance of	wds:Q28486499-87FE0F1B-E892-4AD2-A6A8-E335A5B3EF4A
instance of	scholarly article
main subject	wds:Q28486499-0C0668D8-93CC-4E62-A438-05D109B9B32C wds:Q28486499-4743A542-C6A2-4287-8EB9-CB0A07662287
main subject	Mycobacterium tuberculosis tuberculosis
PubMed ID	wds:Q28486499-D4D8494D-599E-4DCB-B36D-45AFECC0C794
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16288457
PubMed ID	16288457
published in	wds:Q28486499-F68A217B-7086-4364-BC42-122A6AF0EE31
published in	Proteins
issue	wds:Q28486499-589754E2-01E8-451E-A431-890CD1B918B8
volume	wds:Q28486499-D0B4A4F1-8EB4-4381-8A42-E5CBD5832B78
issue	2
volume	62
DOI	wds:Q28486499-B918DCAE-AFB0-41D0-8E41-0045B1E910E5
DOI	http://dx.doi.org/10.1002/PROT.20662
DOI	10.1002/PROT.20662
ResearchGate publication ID	wds:Q28486499-6BEFE2B5-EFD7-4EF9-9AAD-FE72D0A94DBB
ResearchGate publication ID	7480921
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q28486499
is cites work of	Structural and functional characterization of the Mycobacterium tuberculosis uridine monophosphate kinase: insights into the allosteric regulation Structural and functional consequences of single amino acid substitutions in the pyrimidine base binding pocket of Escherichia coli CMP kinase (1)H, (13)C and (15)N resonance assignment of human guanylate kinase Structure of Staphylococcus aureus guanylate monophosphate kinase. Strain analysis of protein structures and low dimensionality of mechanical allosteric couplings. Eukaryotic-type serine/threonine kinase mediated phosphorylation at Thr169 perturbs mycobacterial guanylate kinase activity. Binding dynamics and energetic insight into the molecular forces driving nucleotide binding by guanylate kinase Enzyme closure and nucleotide binding structurally lock guanylate kinase. Functional modes and residue flexibility control the anisotropic response of guanylate kinase to mechanical stress Development of an HPLC-based guanosine monophosphate kinase assay and application to Plasmodium vivax guanylate kinase Structural studies of a hyperthermophilic thymidylate kinase enzyme reveal conformational substates along the reaction coordinate Purification and characterization of guanylate kinase, a nucleoside monophosphate kinase of Brugia malayi.
is cites work of	wds:Q40061681-FC06C879-7162-4A8D-B25C-13FC4DCCA696 wds:Q92822364-81EC09AB-4FC5-4A66-8D96-11FC9B8A2037 wds:Q39777395-12C8983B-20DF-48FF-B5F0-E206F7ED3C42 wds:Q35224003-187D9CE3-83C1-42B5-BD20-66CD267E5454 wds:Q38719901-23FC4494-4AE0-496E-A67E-D6A137526C03 wds:Q54335111-16005F9A-913D-41F4-99B4-529C56F2C197 wds:Q27666341-30C97458-DD1A-40C3-9FB7-BFF8AFD8FB32 wds:Q27645128-BFAC1E3A-59FD-4EA0-B4E4-2AE1FC1F4E1E wds:Q45714068-A034C727-1D3F-4740-BF12-30BA18E5437E wds:Q41916667-EF379A2A-B49B-4D5B-89BA-DDA79B2B7574 wds:Q41786350-B0F046CE-98A7-44BB-8A69-9122F9A5CD74 wds:Q37322944-E19A9939-44BD-42E8-BF63-1D5F99885D9D

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