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Showing 1 to 20 of 63 for “"protein tyrosine phosphatase"”.
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Investigations into the chemistry of protein tyrosine phosphatase redox regulation
… the reversible phosphorylation of specific protein tyrosine residues. This reversible phosphorylation serves as a biochemical "rheostat" that alters a protein's functional properties and leads to propagation of the signal. The phosphorylation status of these tyrosine residues, thus …
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Small Phosphomonoesters as Probes of Protein-Tyrosine Phosphatase Active Sites
… for differentiating between two families of protein phosphatases: the protein-tyrosine phosphatases [PTPs] and the dual-specificity protein phosphatases [DSPs]. Three PTPs, PTP-1B, Tc-PTPa, and PTP-H1, and three DSPs, Cdc-14, VHR, and IphP, were challenged in vitro with alpha-naphthyl …
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Characterization of the molecular environment of the protein tyrosine phosphatase PTP-BL
Contains fulltext : 18735.pdf (Publisher’s version ) (Open Access)
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Targeting the protein tyrosine phosphatase, SHP2, and PI3K in FLT3-ITD+ leukemia
Internal tandem duplications in the fms-like tyrosine kinase receptor (FLT3-ITDs) cause constitutive activation of the receptor and confer a poor prognosis in acute myeloid leukemia (AML). We hypothesized that Shp2 interacts with FLT3-ITD via protein complexes at tyrosine (Y) 768, 955, and/or 969 …
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Protein Tyrosine Phosphatase Receptor Type S (PTPRS) Regulates Hematopoietic Stem Cell Self-Renewal
… are regulated by signaling through protein tyrosine kinases (PTK) such as c-kit, Flt-3 and Tie2. PTKs work in concert with receptor protein tyrosine phosphatases (PTPs) to maintain cellular equilibrium. The functions of PTPs in counterbalancing PTK signaling in HSCs however remain …
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Synthesis of exo-affinity labeling agents of protein tyrosine phosphatase non-receptor type 1
… THE UNIVERSITY OF MISSOURI AT AUTHOR'S REQUEST.] Protein-tyrosine phosphatase 1B (PTP1B) is a negative regulator in the insulin signaling cascade. A lot of research has focused on inhibiting PTP1B but with no success. Only one drug is currently in phase II clinical trials. We have developed a …
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The Role Of Protein Tyrosine Phosphatase 1b In The Central Regulation Of Energy Homeostasis
Protein tyrosine phosphatase 1B (PTP1B) is a ubiquitously expressed tyrosine phosphatase implicated in the central control of energy homeostasis via negative regulation of leptin signaling. Mice with central nervous system (CNS)-specific PTP1B deficiency demonstrate clear metabolic improvements, …
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An investigation of the structure and function of the receptor-type protein tyrosine phosphatase CD148
CD148 is an R3 receptor-type protein tyrosine phosphatase (RPTP) found on platelet surfaces, where it has a vital dual role in regulating platelet signalling and thrombosis. Inhibition of CD148 has been suggested as a novel anti-thrombotic strategy. Loss-of-function polymorphisms located in the …
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The Effect of Phenol-Based Ligands on Vanadate Inhibition of the Protein Tyrosine Phosphatase Yop51*D162.
Studies of vanadate inhibition of the protein tyrosine phosphatase (PTP) YOP*[delta]162 were undertaken. Vanadate was found to be reversible competitive inhibitor with Ki,c = 1.64 +/- 0.07 [mu]M at pH = 5.5 and Ki,c = 3.05 +/- 0.05 [mu]M at pH = 7.3. Vanadate was not an uncompetitive inhibitor at …
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The Regulation of Src Homology 2 Domain-Containing Protein Tyrosine Phosphatase 2 (SHP-2) in Brain Microglia
SHP-2, a member of protein tyrosine phosphatases (PTPs), plays a role on the regulation of several signaling pathway such as NF-kB, MAP kinase, JAK-STAT, and PI3 kinase. However, the roles of SHP-2 in brain microglia activation are largely unknown. Here, I determined the regulation of SHP-2 on …
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Expanding our knowledge of protein tyrosine phosphatase-like phytases : mechanism, substrate specificity and pathways of myo-inositol hexakisphosphate dephosphorylation
A novel bacterial protein tyrosine phosphatase (PTP)-like enzyme has recently been isolated that has a PTP-like active site and fold and the ability to dephosphorylate myo-inositol hexakisphosphate. In order to expand our knowledge of this novel class of enzyme, four new representative genes were …
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The diverse branches of PTPRR protein tyrosine phosphatase function. New insights in cell differentiation, neuronal signalling and mouse behaviour
Contains fulltext : 161370.pdf (Publisher’s version ) (Open Access)
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Identification of a Low Molecular Weight Protein Tyrosine Phosphatase and Its Potential Physiological Substrates in Synechocystis sp. PCC 6803
The predicted protein product of open reading frame slr0328 from Synechocystis sp. PCC 6803, SynPTP, possesses significant amino acid sequence similarity with known low molecular weight protein tyrosine phosphatases (PTPs). To determine the gross functional properties of this hypothetical protein, …
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Non-autonomous regulation of bone mass accrual and the role of T-cell protein tyrosine phosphatase in the bone regulation of insulin sensitivity
… cascade is negatively regulated by ESP, a tyrosine phosphatase dephosphorylating the insulin receptor. is one of many tyrosine phosphatases expressed in osteoblasts, and this observation suggests that other protein tyrosine phosphatases may contribute to the attenuation of insulin receptor …
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The investigation of the genetic and pharmacological inhibition of striatal-enriched protein tyrosine phosphatase (STEP) and its role in hippocampal excitability and seizure propensity
Submission original under an indefinite embargo labeled 'Open Access'. The submission was exported from vireo on 2023-04-12 without embargo terms
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Modulation der IL-6-abhängigen Signaltransduktion durch die Protein-Tyrosinphosphatase SHP2
In the year 1993 a protein-tyrosine phosphatase, SH2 domain containing protein-tyrosine-phosphatase 2 (SHP2), has been discovered, which seems to play an important role in the signaltransduction of many cytokines. The aim of this work was to elucidate the role of the tyrosine phosporylation of SHP2 …
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Dual-specific protein phosphatases in the <i>Archaea</i>
… sequence similarity among the three families of phosphatases. All known LMW PTP remove phosphoryl groups esterified to the hydroxyl amino acid: tyrosine, whereas all members of the Cdc25 family are dual-specificity protein phosphatases that dephosphorylate all the hydroxyl amino acids: tyrosine, …
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