Crystal structure of a mammalian purple acid phosphatase
about
Crystal structures of a purple acid phosphatase, representing different steps of this enzyme's catalytic cycleTartrate-resistant purple acid phosphatase is synthesized as a latent proenzyme and activated by cysteine proteinasesIdentification of purple acid phosphatase inhibitors by fragment-based screening: promising new leads for osteoporosis therapeuticsThe structure of a purple acid phosphatase involved in plant growth and pathogen defence exhibits a novel immunoglobulin-like foldProteolytic excision of a repressive loop domain in tartrate-resistant acid phosphatase by cathepsin K in osteoclastsExpression and distribution of tartrate-resistant purple acid phosphatase in the rat nervous system.Phosphate forms an unusual tripodal complex with the Fe-Mn center of sweet potato purple acid phosphatase.Biology of tartrate-resistant acid phosphatase.Tartrate-resistant acid phosphatase (TRAP/ACP5) promotes metastasis-related properties via TGFβ2/TβR and CD44 in MDA-MB-231 breast cancer cells.A model of the acid sphingomyelinase phosphoesterase domain based on its remote structural homolog purple acid phosphatase.A Potent Tartrate Resistant Acid Phosphatase Inhibitor to Study the Function of TRAP in Alveolar Macrophages.Mutagenesis of putative catalytic and regulatory residues of Streptomyces chromofuscus phospholipase D differentially modifies phosphatase and phosphodiesterase activities.Metal binding Asp-120 in metallo-beta-lactamase L1 from Stenotrophomonas maltophilia plays a crucial role in catalysis.Theoretical studies on the reaction mechanism of PP1 and the effects of different oxidation states of the Mn-Mn center on the mechanism.Contribution of the two domains of E. coli 5'-nucleotidase to substrate specificity and catalysis.Properties and expression of human tartrate-resistant acid phosphatase isoform 5a by monocyte-derived cells.3',5' Cyclic nucleotide phosphodiesterases class III: members, structure, and catalytic mechanism.Purple acid phosphatases of Arabidopsis thaliana. Comparative analysis and differential regulation by phosphate deprivation.Characterization of an evolutionarily conserved metallophosphoesterase that is expressed in the fetal brain and associated with the WAGR syndrome.Theoretical studies on the mechanism of activation of phosphoprotein phosphatases and purple acid phosphatases suggest an evolutionary strategy to survive in acidic environments.
P2860
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P2860
Crystal structure of a mammalian purple acid phosphatase
description
1999 nî lūn-bûn
@nan
1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Crystal structure of a mammalian purple acid phosphatase
@ast
Crystal structure of a mammalian purple acid phosphatase
@en
Crystal structure of a mammalian purple acid phosphatase
@nl
type
label
Crystal structure of a mammalian purple acid phosphatase
@ast
Crystal structure of a mammalian purple acid phosphatase
@en
Crystal structure of a mammalian purple acid phosphatase
@nl
prefLabel
Crystal structure of a mammalian purple acid phosphatase
@ast
Crystal structure of a mammalian purple acid phosphatase
@en
Crystal structure of a mammalian purple acid phosphatase
@nl
P2093
P356
P1476
Crystal structure of a mammalian purple acid phosphatase
@en
P2093
B Ek-Rylander
C Svensson
F Lindqvist
G Andersson
J Uppenberg
P304
P356
10.1006/JMBI.1999.2896
P407
P577
1999-07-02T00:00:00Z