multiple indicator cluster survey (mics) 2009 Search Results


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Macro International Inc multiple indicator cluster survey (mics) 2009
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Ahlborn GmbH naas02
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Becton Dickinson mouse anti-adenomatus polyposis coli (apc
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Takeda human gingival fibroblasts
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Knoell Germany phosphatase pten
Alexidine dihydrochloride is a selective inhibitor of PTPMT1. A, structure of alexidine dihydrochloride. B, inhibition of selected phosphatases by alexidine dihydrochloride. PTPMT1, VHR <t>phosphatase,</t> λ-Ppase, and T-cell PTPase assays were carried out with O-MFP as the substrate (n = 3), and <t>PTEN</t> assays were carried out with lipid substrate (n = 2). All assays were carried out by using optimum buffer and pH for each enzyme. The IC50 with PTPMT1 was 1.08 μM ± 0.08 with a Hill coefficient of 2.16 ± 0.31. Data are presented as the mean ± S.E.M. of independent experiments. C, comparison of the sequences of the catalytic motif of the protein tyrosine phosphatases assayed. Boxed residues are those conserved within the catalytic motif.
Phosphatase Pten, supplied by Knoell Germany, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Strube GmbH Co KG β 1a
Alexidine dihydrochloride is a selective inhibitor of PTPMT1. A, structure of alexidine dihydrochloride. B, inhibition of selected phosphatases by alexidine dihydrochloride. PTPMT1, VHR <t>phosphatase,</t> λ-Ppase, and T-cell PTPase assays were carried out with O-MFP as the substrate (n = 3), and <t>PTEN</t> assays were carried out with lipid substrate (n = 2). All assays were carried out by using optimum buffer and pH for each enzyme. The IC50 with PTPMT1 was 1.08 μM ± 0.08 with a Hill coefficient of 2.16 ± 0.31. Data are presented as the mean ± S.E.M. of independent experiments. C, comparison of the sequences of the catalytic motif of the protein tyrosine phosphatases assayed. Boxed residues are those conserved within the catalytic motif.
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Federation of European Neuroscience Societies fems microbiol lett
Alexidine dihydrochloride is a selective inhibitor of PTPMT1. A, structure of alexidine dihydrochloride. B, inhibition of selected phosphatases by alexidine dihydrochloride. PTPMT1, VHR <t>phosphatase,</t> λ-Ppase, and T-cell PTPase assays were carried out with O-MFP as the substrate (n = 3), and <t>PTEN</t> assays were carried out with lipid substrate (n = 2). All assays were carried out by using optimum buffer and pH for each enzyme. The IC50 with PTPMT1 was 1.08 μM ± 0.08 with a Hill coefficient of 2.16 ± 0.31. Data are presented as the mean ± S.E.M. of independent experiments. C, comparison of the sequences of the catalytic motif of the protein tyrosine phosphatases assayed. Boxed residues are those conserved within the catalytic motif.
Fems Microbiol Lett, supplied by Federation of European Neuroscience Societies, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Pharmacal Research Laboratories Inc quatracide pv
Alexidine dihydrochloride is a selective inhibitor of PTPMT1. A, structure of alexidine dihydrochloride. B, inhibition of selected phosphatases by alexidine dihydrochloride. PTPMT1, VHR <t>phosphatase,</t> λ-Ppase, and T-cell PTPase assays were carried out with O-MFP as the substrate (n = 3), and <t>PTEN</t> assays were carried out with lipid substrate (n = 2). All assays were carried out by using optimum buffer and pH for each enzyme. The IC50 with PTPMT1 was 1.08 μM ± 0.08 with a Hill coefficient of 2.16 ± 0.31. Data are presented as the mean ± S.E.M. of independent experiments. C, comparison of the sequences of the catalytic motif of the protein tyrosine phosphatases assayed. Boxed residues are those conserved within the catalytic motif.
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Neo MPS Inc mog35–55
Alexidine dihydrochloride is a selective inhibitor of PTPMT1. A, structure of alexidine dihydrochloride. B, inhibition of selected phosphatases by alexidine dihydrochloride. PTPMT1, VHR <t>phosphatase,</t> λ-Ppase, and T-cell PTPase assays were carried out with O-MFP as the substrate (n = 3), and <t>PTEN</t> assays were carried out with lipid substrate (n = 2). All assays were carried out by using optimum buffer and pH for each enzyme. The IC50 with PTPMT1 was 1.08 μM ± 0.08 with a Hill coefficient of 2.16 ± 0.31. Data are presented as the mean ± S.E.M. of independent experiments. C, comparison of the sequences of the catalytic motif of the protein tyrosine phosphatases assayed. Boxed residues are those conserved within the catalytic motif.
Mog35–55, supplied by Neo MPS Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Regulus Therapeutics 20-o-methyl 30cholesterol
Alexidine dihydrochloride is a selective inhibitor of PTPMT1. A, structure of alexidine dihydrochloride. B, inhibition of selected phosphatases by alexidine dihydrochloride. PTPMT1, VHR <t>phosphatase,</t> λ-Ppase, and T-cell PTPase assays were carried out with O-MFP as the substrate (n = 3), and <t>PTEN</t> assays were carried out with lipid substrate (n = 2). All assays were carried out by using optimum buffer and pH for each enzyme. The IC50 with PTPMT1 was 1.08 μM ± 0.08 with a Hill coefficient of 2.16 ± 0.31. Data are presented as the mean ± S.E.M. of independent experiments. C, comparison of the sequences of the catalytic motif of the protein tyrosine phosphatases assayed. Boxed residues are those conserved within the catalytic motif.
20 O Methyl 30cholesterol, supplied by Regulus Therapeutics, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Alexidine dihydrochloride is a selective inhibitor of PTPMT1. A, structure of alexidine dihydrochloride. B, inhibition of selected phosphatases by alexidine dihydrochloride. PTPMT1, VHR phosphatase, λ-Ppase, and T-cell PTPase assays were carried out with O-MFP as the substrate (n = 3), and PTEN assays were carried out with lipid substrate (n = 2). All assays were carried out by using optimum buffer and pH for each enzyme. The IC50 with PTPMT1 was 1.08 μM ± 0.08 with a Hill coefficient of 2.16 ± 0.31. Data are presented as the mean ± S.E.M. of independent experiments. C, comparison of the sequences of the catalytic motif of the protein tyrosine phosphatases assayed. Boxed residues are those conserved within the catalytic motif.

Journal: The Journal of Pharmacology and Experimental Therapeutics

Article Title: Pharmacological Targeting of the Mitochondrial Phosphatase PTPMT1 S⃞

doi: 10.1124/jpet.109.163329

Figure Lengend Snippet: Alexidine dihydrochloride is a selective inhibitor of PTPMT1. A, structure of alexidine dihydrochloride. B, inhibition of selected phosphatases by alexidine dihydrochloride. PTPMT1, VHR phosphatase, λ-Ppase, and T-cell PTPase assays were carried out with O-MFP as the substrate (n = 3), and PTEN assays were carried out with lipid substrate (n = 2). All assays were carried out by using optimum buffer and pH for each enzyme. The IC50 with PTPMT1 was 1.08 μM ± 0.08 with a Hill coefficient of 2.16 ± 0.31. Data are presented as the mean ± S.E.M. of independent experiments. C, comparison of the sequences of the catalytic motif of the protein tyrosine phosphatases assayed. Boxed residues are those conserved within the catalytic motif.

Article Snippet: J Enzyme Inhib Med Chem 19 :409–415 [ PubMed ] Lai JP, Bao S, Davis IC, Knoell DL. (2009) Inhibition of the phosphatase PTEN protects mice against oleic acid-induced acute lung injury.

Techniques: Inhibition, Comparison