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Protein tyrosine phosphatases: structure, signaling and drug discovery/ Lalima G. Ahuja.

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dc.contributor.author Ahuja Lalima G.,
dc.date.accessioned 2024-01-29T22:57:03Z
dc.date.available 2024-01-29T22:57:03Z
dc.date.issued 2018
dc.identifier.citation Ahuja. Protein tyrosine phosphatases: structure, signaling and drug discovery - 1 online resource (xiv, 282 pages) - URL: https://libweb.kpfu.ru/ebsco/pdf/1913015.pdf
dc.identifier.isbn 3110421771
dc.identifier.isbn 9783110421774
dc.identifier.uri https://dspace.kpfu.ru/xmlui/handle/net/181503
dc.description Includes bibliographical references and index.
dc.description.abstract Protein tyrosine phosphatases remove phosphates from the phosphotyrosine residues of target proteins and reverse the action of various protein tyrosine kinases. This essential interplay between the opposing actions of protein tyrosine phosphatases and protein tyrosine kinases forms the basis of signaling networks that underlie the cellular workings of human physiology. Initially passed-off as housekeeping genes; these proteins were only acknowledged to maintain a steady background of phosphotyrosine levels in the cell. However, recent progress in studying their role in embryonic development and human disease has established their importance as regulators of signal regulation. Convincing evidence shows the role of mutations in these proteins to cause and/or intensify the severity of various diseases including metabolic and neurological disorders and also cancer. Protein tyrosine phosphatases have slowly, yet convincingly become crucial targets for therapeutic intervention of various human pathophysiologies. This book describes these signaling enzymes using the molecular details of their structure and mechanistic function. Various subtypes of cysteine-based Class I, II, III and the Haloacid dehalogenase related Class IV protein tyrosine phosphatases have been illustrated and explained. The superfamily of proteins is also described vis-a-vis its complimentary protein phosphoserine/phosphoserine phosphatases. Membrane bound receptor forms and the cytosolic non-receptor protein tyrosine phosphatases have been described for their biological function. This book serves as a reference for any reader looking to understand the sequence features, structural elements, molecular mechanism and cellular function of this superfamily of signaling enzymes.
dc.description.tableofcontents Frontmatter -- Preface -- About The Author -- Contents -- 1.Tyrosine Phosphorylation In Cell Signaling: Discovery And Beyond -- 2.Protein Phosphatases: Classification And Domain Architecture -- 3.Protein Tyrosine Phosphatases: Molecular Structure And Mechanism -- 4.The Receptor Protein Tyrosine Phosphatases: Structure And Function -- 5.The Double-Domain Receptor Protein Tyrosine Phosphatases -- 6 The Non-Receptor Protein Tyrosine Phosphatases: Part I -- 7.The Non-Receptor Protein Tyrosine Phosphatases: Part Ii -- 8.Protein Tyrosine Phosphatases: Strategies For Drug Development -- Index
dc.language English
dc.language.iso en
dc.subject.other Protein-tyrosine phosphatase.
dc.subject.other Biochemie.
dc.subject.other Medizinische Chemie.
dc.subject.other Proteintyrosinphosphatase.
dc.subject.other Signalproteine.
dc.subject.other Wirkstoffdesign.
dc.subject.other SCIENCE / Life Sciences / Biochemistry
dc.subject.other Electronic books.
dc.title Protein tyrosine phosphatases: structure, signaling and drug discovery/ Lalima G. Ahuja.
dc.type Book
dc.description.pages 1 online resource (xiv, 282 pages)
dc.collection Электронно-библиотечные системы
dc.source.id EN05CEBSCO05C3162


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