Crystal structure of a Legionella pneumophila ecto -triphosphate diphosphohydrolase, a structural and functional homolog of the eukaryotic NTPDases
about
Structural insight into activation mechanism of Toxoplasma gondii nucleoside triphosphate diphosphohydrolases by disulfide reductionThe ATP/ADP substrate specificity switch between Toxoplasma gondii NTPDase1 and NTPDase3 is caused by an altered mode of binding of the substrate baseThe biochemical properties of the Arabidopsis ecto-nucleoside triphosphate diphosphohydrolase AtAPY1 contradict a direct role in purinergic signalingUpdate on Legionnaires' disease: pathogenesis, epidemiology, detection and control.Molecular pathogenesis of infections caused by Legionella pneumophilaCellular function and molecular structure of ecto-nucleotidases.The GDA1_CD39 superfamily: NTPDases with diverse functions.Molecular Detection of Legionella: Moving on From mip.Fluorescence polarization immunoassays for monitoring nucleoside triphosphate diphosphohydrolase (NTPDase) activity.Extracellular nucleotide catabolism by the Group B Streptococcus ectonucleotidase NudP increases bacterial survival in blood.Schistosome tegumental ecto-apyrase (SmATPDase1) degrades exogenous pro-inflammatory and pro-thrombotic nucleotides.The role of the NTPDase enzyme family in parasites: what do we know, and where to from here?Therapeutic potentials of ecto-nucleoside triphosphate diphosphohydrolase, ecto-nucleotide pyrophosphatase/phosphodiesterase, ecto-5'-nucleotidase, and alkaline phosphatase inhibitors.Structures and kinetics for plant nucleoside triphosphate diphosphohydrolases support a domain motion catalytic mechanism.Inseparable tandem: evolution chooses ATP and Ca2+ to control life, death and cellular signalling.Multiple ecto-nucleoside triphosphate diphosphohydrolases facilitate intracellular replication of Legionella pneumophila.New crystal forms of NTPDase1 from the bacterium Legionella pneumophilaMutagenesis of apyrase conserved region 1 alters the nucleotide substrate specificity.Chaperones are necessary for the expression of catalytically active potato apyrases in prokaryotic cells.Biology of purinergic signalling: its ancient evolutionary roots, its omnipresence and its multiple functional significance.
P2860
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P2860
Crystal structure of a Legionella pneumophila ecto -triphosphate diphosphohydrolase, a structural and functional homolog of the eukaryotic NTPDases
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Crystal structure of a Legione ...... log of the eukaryotic NTPDases
@ast
Crystal structure of a Legione ...... log of the eukaryotic NTPDases
@en
Crystal structure of a Legione ...... log of the eukaryotic NTPDases
@nl
type
label
Crystal structure of a Legione ...... log of the eukaryotic NTPDases
@ast
Crystal structure of a Legione ...... log of the eukaryotic NTPDases
@en
Crystal structure of a Legione ...... log of the eukaryotic NTPDases
@nl
prefLabel
Crystal structure of a Legione ...... log of the eukaryotic NTPDases
@ast
Crystal structure of a Legione ...... log of the eukaryotic NTPDases
@en
Crystal structure of a Legione ...... log of the eukaryotic NTPDases
@nl
P2093
P50
P1433
P1476
Crystal structure of a Legione ...... log of the eukaryotic NTPDases
@en
P2093
Anthony J F d'Apice
Emma Byres
Fiona M Sansom
Jason W Schmidberger
Manisha Dias
Matthew C J Wilce
Patrice Riedmaier
P304
P356
10.1016/J.STR.2009.11.014
P50
P577
2010-02-10T00:00:00Z