Phosphatase Modulators

Specificaties
Gebonden, 315 blz. | Engels
Humana Press | 2013e druk, 2013
ISBN13: 9781627035613
Rubricering
Humana Press 2013e druk, 2013 9781627035613
Onderdeel van serie Methods in Molecular Biology
€ 120,99
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Samenvatting

Driving further the research on mammalian alkaline phosphatase structure and function, Phosphatase Modulators collects expert contributions into one “how to” manual for basic scientists interested in initiating a drug discovery effort. While this book contains the traditional method chapters and some typical reviews on the structure and known functions of phosphatases, other contributions are meant to discuss approaches and alternatives useful in making “go/no-go” decisions in high throughput screening (HTS) and lead optimization campaigns. Many chapters focus on tissue-nonspecific alkaline phosphatase (TNAP) as well as protein phosphatases.  Written for the highly successful Methods in Molecular Biology series, chapters in this volume include the kind of detail and key implementation advice that promotes reproducible results.

 Step-by-step and practical, Phosphatase Modulators offers a path to understanding many of the facets and complexities associated with undertaking a drug discovery effort and will serve as a roadmap to initiating those efforts.

Specificaties

ISBN13:9781627035613
Taal:Engels
Bindwijze:gebonden
Aantal pagina's:315
Uitgever:Humana Press
Druk:2013

Inhoudsopgave

<p>1. Chemical Probe Development Versus Drug Development</p><p>            Michael R. Jackson</p><p> </p><p>2. Phosphatase High-Throughput Screening Assay Design and Selection</p><p>            Eduard A. Sergienko</p><p> </p><p>3. Multisystemic Functions of Alkaline Phosphatases</p><p>            René Buchet, José Luis Millán, and David Magne</p><p> </p><p>4. Robotic Implementation of Assays: Tissue-Nonspecific Alkaline Phosphatase (TNAP) Case Study</p><p>            Thomas D.Y. Chung</p><p> </p><p>5. Inhibitors of Tissue-Nonspecific Alkaline Phosphatase (TNAP): From Hits to Leads</p><p>            Peter Teriete, Anthony B. Pinkerton, and Nicholas D.P. Cosford</p><p> </p><p>6. A Method for Direct Assessment of Tissue-Nonspecific Alkaline Phosphatase (TNAP) Inhibitors in Blood Samples</p><p>            Eduard Sergienko, Qing Sun, and Chen-Ting Ma</p><p> </p><p>7. Isolation and Characteristics of Matrix Vesicles</p><p>            René Buchet, Slawomir Pikula, David Magne, and Saïda Mebarek</p><p> </p><p>8. The Use of Tissue-Nonspecific Alkaline Phosphatase (TNAP) and PHOSPHO1 Inhibitors to Affect Mineralization by Cultured Cells</p><p>            Tina Kiffer-Moreira and Sonoko Narisawa</p><p> </p><p>9. Modulators of Intestinal Alkaline Phosphatase</p><p>            Ekaterina V. Bobkova, Tina Kiffer-Moreira, and Eduard A. Sergienko</p><p> </p><p>10. New Activity Assays for ENPP1 with Physiological Substrates ATP and ADP</p><p>            Chen-Ting Ma and Eduard Sergienko</p><p> </p><p>11. Structure of Acid Phosphatases</p><p>            César L. Araujo and Pirkko T. Vihko</p><p> </p><p>12. Purification of Prostatic Acid Phosphatase (PAP) for Structural and Functional Studies</p><p>            Annakaisa M. Herrala, Ileana B. Quintero, and Pirkko T. Vihko</p><p> </p><p>13. Protein Tyrosine Phosphatases: Structure, Function, and Implication in Human Disease</p><p>            Lutz Tautz, David A. Critton, and Stefan Grotegut</p><p> </p><p>14. High-Throughput Screening for Protein Tyrosine Phosphatase Activity Modulators</p><p>            Lutz Tautz and Eduard A. Sergienko</p><p> </p><p>15. Evaluating Effects of Tyrosine Phosphatase Inhibitors on T Cell Receptor Signaling</p><p>            Souad Rahmouni, Laurence Delacroix, Wallace H. Liu, and Lutz Tautz</p><p> </p><p>16. Interactor-Guided Dephosphorylation by Protein Phosphatase-1</p><p>            Shannah Boens, Kathelijne Szekér, Aleyde Van Eynde, and Mathieu Bollen</p><p> </p><p>17. Structure, Regulation, and Pharmacological Modulation of PP2A Phosphatases</p><p>            Caroline Lambrecht, Dorien Haesen, Ward Sents, Elitsa Ivanova, and Veerle Janssens</p>
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