about
Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphataseGradual deregulation and loss of PCPH expression in the progression of human laryngeal neoplasiaN-linked oligosaccharides affect the enzymatic activity of CD39: diverse interactions between seven N-linked glycosylation sitesDistribution of NTPDase5 and NTPDase6 and the regulation of P2Y receptor signalling in the rat cochlea.Characterization of an alternative splice variant of human nucleoside triphosphate diphosphohydrolase 3 (NTPDase3): a possible modulator of nucleotidase activity and purinergic signaling.Cellular function and molecular structure of ecto-nucleotidases.Requirement of Cys399 for processing of the human ecto-ATPase (NTPDase2) and its implications for determination of the activities of splice variants of the enzyme.The GDA1_CD39 superfamily: NTPDases with diverse functions.The ENTPD5/mt-PCPH oncoprotein is a catalytically inactive member of the ectonucleoside triphosphate diphosphohydrolase family.NTPDase5/PCPH as a new target in highly aggressive tumors: a systematic reviewNucleotidase cascades are catalyzed by secreted proteins of the parasitic nematode Trichinella spiralisIdentification of a tyrosine residue responsible for N-acetylimidazole-induced increase of activity of ecto-nucleoside triphosphate diphosphohydrolase 3.Identification of cysteine residues responsible for oxidative cross-linking and chemical inhibition of human nucleoside-triphosphate diphosphohydrolase 3.Various N-glycoforms differentially upregulate E-NTPDase activity of the NTPDase3/CD39L3 ecto-enzymatic domain.NTPDase5 hydrolyzes nucleoside diphosphatesAtAPY1 and AtAPY2 function as Golgi-localized nucleoside diphosphatases in Arabidopsis thaliana.
P2860
Q28217160-F1A3114C-F3AB-4DFC-9F0F-5EB1A231EDE2Q28218233-B19E00B0-56D5-4D56-A612-2D1C4597EF95Q28571719-87BFD83E-3EE6-416B-9072-743E7264F27CQ30479858-7674BA63-F12A-426A-B6EE-86C3F92D6F1AQ33264628-5F711364-0C80-4A90-8296-3A0FEC930086Q34031794-96C82905-0EA8-486A-88CE-CF16FDE5F885Q34218222-8F5EB1F7-0CC4-4E63-8930-2ADB870CC94CQ34868468-1C6D02B3-A2F5-4DF5-B936-069A2F372F4AQ37313396-D06F41A8-875E-4DA7-AF3B-B9742A743B7CQ38232084-F720EC34-4CE5-4485-8799-C717AC134FC1Q39656271-BD79D937-7EC4-4169-B540-416AB16C0703Q40722921-B651C08A-E327-4EDC-B5FF-9C6B2FF7D39AQ43826785-96AFE186-E65A-44D1-B230-768366590E6FQ47732889-536AED44-3B66-44FE-86EF-4B34E06555C7Q50294695-D0F15CA0-5EAF-43E7-9828-CE5AF924BB51Q50489707-9A2D2F9A-E3FB-4FD4-9FF5-DBA6A1E664F6
P2860
description
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2000
@ast
im Oktober 2000 veröffentlicher wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2000/10/24)
@sk
vědecký článek publikovaný v roce 2000
@cs
wetenschappelijk artikel (gepubliceerd op 2000/10/24)
@nl
наукова стаття, опублікована в жовтні 2000
@uk
مقالة علمية (نشرت في 24-10-2000)
@ar
name
Biochemical characterization of CD39L4
@ast
Biochemical characterization of CD39L4
@en
Biochemical characterization of CD39L4
@nl
type
label
Biochemical characterization of CD39L4
@ast
Biochemical characterization of CD39L4
@en
Biochemical characterization of CD39L4
@nl
prefLabel
Biochemical characterization of CD39L4
@ast
Biochemical characterization of CD39L4
@en
Biochemical characterization of CD39L4
@nl
P2093
P356
P1433
P1476
Biochemical characterization of CD39L4
@en
P2093
D. W. McGowan
J. E. Ford
J. J. Mulero
J. M. Bright
S. T. Nelken
P304
12924–12928
P356
10.1021/BI000960Y
P407
P577
2000-10-24T00:00:00Z