Search Results - "Szedlacsek, Stefan E"
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Protein tyrosine phosphatases: structure-function relationships
Published in The FEBS journal (01-03-2008)“…Structural analysis of protein tyrosine phosphatases (PTPs) has expanded considerably in the last several years, producing more than 200 structures in this…”
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Microarray Strategy for Mapping the Substrate Specificity of Protein Tyrosine Phosphatase
Published in Angewandte Chemie (International ed.) (01-01-2007)“…Which substrate will it be? Phosphotyrosine peptide microarrays have allowed the substrate specificity to be mapped for two prototypical protein‐tyrosine…”
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3
Interface analysis of the complex between ERK2 and PTP-SL
Published in PloS one (08-05-2009)“…The activity of ERK2, an essential component of MAP-kinase pathway, is under the strict control of various effector proteins. Despite numerous efforts, no…”
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Functional, fractal nonlinear response with application to rate processes with memory, allometry, and population genetics
Published in Proceedings of the National Academy of Sciences - PNAS (20-03-2007)“…We give a functional generalization of fractal scaling laws applied to response problems as well as to probability distributions. We consider excitations and…”
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WDR1 is a novel EYA3 substrate and its dephosphorylation induces modifications of the cellular actin cytoskeleton
Published in Scientific reports (13-02-2018)“…Eyes absent (EYA) proteins are unusual proteins combining in a single polypeptide chain transactivation, threonine phosphatase, and tyrosine phosphatase…”
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Author Correction: WDR1 is a novel EYA3 substrate and its dephosphorylation induces modifications of the cellular actin cytoskeleton
Published in Scientific reports (20-05-2020)“…An amendment to this paper has been published and can be accessed via a link at the top of the paper…”
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Fisher's Theorems for Multivariable, Time- and Space-Dependent Systems, with Applications in Population Genetics and Chemical Kinetics
Published in Proceedings of the National Academy of Sciences - PNAS (12-07-2005)“…We study different physical, chemical, or biological processes involving replication, transformation, and disappearance processes, as well as transport…”
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Analysis of EYA3 Phosphorylation by Src Kinase Identifies Residues Involved in Cell Proliferation
Published in International journal of molecular sciences (13-12-2019)“…Eyes absent (EYA) are non-thiol-based protein tyrosine phosphatases (PTPs) that also have transcriptional co-activator functions. Their PTP activity is…”
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Phosphoketolases from Lactococcus lactis, Leuconostoc mesenteroides and Pseudomonas aeruginosa: dissimilar sequences, similar substrates but distinct enzymatic characteristics
Published in Applied microbiology and biotechnology (01-09-2014)“…Phosphoketolases (PKs) are large thiamine pyrophosphate (TPP)-dependent enzymes playing key roles in a number of essential pathways of carbohydrate metabolism…”
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10
Expression, Purification, and Kinetic Analysis of PTP Domains
Published in Methods in molecular biology (Clifton, N.J.) (01-01-2016)“…Protein tyrosine phosphatases (PTP) are a large group of enzymes which work together with protein tyrosine kinases to control the tyrosine phosphorylation of…”
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Identification and Specificity Profiling of Protein Prenyltransferase Inhibitors Using New Fluorescent Phosphoisoprenoids
Published in Journal of the American Chemical Society (08-03-2006)“…Posttranslational modification of proteins with farnesyl and geranylgeranyl isoprenoids is a widespread phenomenon in eukaryotic organisms. Isoprenylation is…”
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The MAM (Meprin/A5-protein/PTPmu) Domain Is a Homophilic Binding Site Promoting the Lateral Dimerization of Receptor-like Protein-tyrosine Phosphatase μ
Published in The Journal of biological chemistry (25-06-2004)“…The MAM (meprin/A5-protein/PTPmu) domain is present in numerous proteins with diverse functions. PTPμ belongs to the MAM-containing subclass of…”
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Analysis of molecular determinants of PRL‐3
Published in Journal of cellular and molecular medicine (01-09-2009)“…In order to analyse whether a C‐terminal polybasic sequence represents a nuclear localization signal (NLS) we obtained several truncated and mutant forms of…”
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Kinetics of slow and tight-binding inhibitors
Published in Methods in enzymology (1995)Get more information
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Preliminary X-ray crystallographic analysis of the d-xylulose 5-phosphate phosphoketolase from Lactococcus lactis
Published in Acta crystallographica. Section F, Structural biology and crystallization communications (01-06-2010)“…Phosphoketolases are thiamine diphosphate‐dependent enzymes which play a central role in the pentose‐phosphate pathway of heterofermentative lactic acid…”
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Esterification of Oxysterols by Human Plasma Lecithin-Cholesterol Acyltransferase
Published in The Journal of biological chemistry (19-05-1995)“…In the present study, lecithin-cholesterol acyltransferase (LCAT) catalyzed esterification of oxysterols was investigated by using discoidal bilayer particles…”
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The MAM (Meprin/A5-protein/PTPmu) Domain Is a Homophilic Binding Site Promoting the Lateral Dimerization of Receptor-like Protein-tyrosine Phosphatase Î
Published in The Journal of biological chemistry (25-06-2004)“…The MAM ( m eprin/ A 5-protein/PTP m u) domain is present in numerous proteins with diverse functions. PTPμ belongs to the MAM-containing subclass of…”
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Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for map kinase regulation 1 1Edited by D. Rees
Published in Journal of molecular biology (01-08-2001)Get full text
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Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation
Published in Journal of molecular biology (17-08-2001)“…Protein tyrosine phosphatases PTP-SL and PTPBR7 are isoforms belonging to cytosolic membrane-associated and to receptor-like PTPs (RPTPs), respectively. They…”
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Intramolecular Interactions in Protein Tyrosine Phosphatase RPTPμ: Kinetic Evidence
Published in Biochemical and biophysical research communications (12-01-2001)“…The receptor-like protein tyrosine phosphatase RPTPμ contains three intracellular domains: the juxtamembrane (JM) and two phosphatase domains (D1 and D2). D1…”
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