Cellular Peptidases in Immune Functions and Diseases 2 - Advances in Experimental Medicine and Biology - International Conference on Cellular Peptidases in Immune Functions and Diseases - Libros - Springer Science+Business Media - 9780306463839 - 31 de mayo de 2000
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Cellular Peptidases in Immune Functions and Diseases 2 - Advances in Experimental Medicine and Biology 2002 edition

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Of the many special roles played by proteolytic enzymes in immune reactions, this study addresses aspects of membrane peptidases, signal transduction via ligation of membrane peptidases (especially of dipeptidyl peptidase IV/CD26 and aminopeptidase N/CD13), and regulation of membrane peptidases.


Marc Notes: Proceedings of an International Conference on Cellular Peptidases in Immune Functions and Diseases (II), held September 12-14, 1999, in Magdeburg, Germany--T.p. verso.; Includes bibliographical references and index. Table of Contents: Part I: Membrane Ectopeptidases with Influence on Immune Functions. Review: The Role of Membrane Peptidases in Immune Functions; U. Lendeckel, et al. Structure and Function of Aminopeptidase N; H. Sjostrom, et al. Modulation of WNT-5a Expression by Actinonin: Linkage of APN to the WNT-Pathway? U. Lendeckel, et al. Enzymatic Activity is not a Precondition for the Intracellular Calcium Increase Mediated by mAbs Specific for Aminopeptidase N/CD13; A. Navarrete Santos, et al. Transforming Growth Factor-b Increases the Expression of Aminopeptidase N/CD13 mRNA and Protein in Monocytes and Monocytic Cell Lines; A. Kehlen, et al. Cell-Cell Contact Between Lymphocytes and Fibroblast-like Synoviocytes Induces Lymphocytic Expression of Aminopeptidase N/CD13 and Results in Lymphocytic Activation; D. Riemann, et al. Natural Substrates of Dipeptidyl Peptidase IV; I. De Meester, et al. Relating Structure to Function in the Beta-Propeller Domain of Dipeptidyl Peptidase IV: Point Mutations that Influence Adenosine Deaminase Binding, Antibody Binding and Enzyme Activity; M. D. Gorrell, et al. Development of a Tertiary-Structure Model of the C-Terminal Domain of DPP IV; W. Brandt. Post Proline Cleaving Peptidases Having DP IV Like Enzyme Activity: Post-Proline Peptidases; C. A. Abbott, et al. A New Type of Fluorogenic Substrates for Determination of Cellular Dipeptidyl Peptidase IV (DP IV/CD26) Activity; S. Lorey, et al. Potent Inhibitors of Dipeptidyl Peptidase IV and their Mechanisms of Inhibition; A. Stockel-Maschek, et al. N-terminal HIV-1 TAT Nonapeptides as Inhibitors of Dipeptidyl Peptidase IV. Conformational Characterization; C. Mrestani-Klaus, et al. Signal Transduction Events Induced or Affected by Inhibition of the Catalytic Activity of Dipeptidyl Peptidase IV (DP IV, CD26); T. Kahne, et al. Specific Inhibitors of Dipeptidyl Peptidase IV Suppress mRNA Expression of DP IV/CD26 and Cytokines; M. Arndt, et al. Dipeptidyl Peptidase IV in Inflammatory CNS Disease; A. Steinbrecher, et al. Dipeptidyl Peptidase IV (CD26): Role in T Cell Activation and Autoimmune Disease; D. Reinhold, et al. Effects of Nonapeptides Derived from the N-Terminal Structure of Human Immunodeficiency Virus-1 (HIV-1) TAT on Suppression of CD26-Dependent T Cell Growth; S. Wrenger, et al. DNA Synthesis in Cultured Human Keratinocytes and HaCaT Keratinocytes is Reduced by Specific Inhibition of Dipeptidyl Peptidase IV (CD26) Enzymatic Activity; R. Vetter, et al. Attractin: A CUB-Family Protease Involved in T Cell-Monocyte/ Macrophage Interactions; J. S. Duke-Cohan, et al. Analogs of Glucose-Dependent Insulinotropic Polypeptide with Increased Dipeptidyl Peptidase IV Resistance; K. Kuhn-Wache, et al. Dipeptidyl Peptidase IV (DPP IV, CD26) in Patients with Mental Eating Disorders; M. Hildebrandt, et al. The Membrane-Bound Ectopeptidase CPM as a Marker of Macrophage Maturation in Vitro and in Vivo; M. Rehli, et al. Matrix Metalloproteinases (MMP-8, -13, and -14) Interact with the Clotting System and Degrade Fibrinogen and Factor XII (Hagemann Factor); H.arald Tschesche, et al. The Neprilysin Family in Health and Disease; A. J. Turner, et al. Part II: Cellular Endopeptidases: New Cathepsins; Results from Knock-out-mice; Regulatory Aspects. Review: Novel Cysteine Proteases of the Papain Family; F. Buhling, et al. Development and Validation of Homology Models of Human Cathepsins K, S, H, and F; A. Fengler, Wolfgang Brandt. The Function of Propeptide Domains of Cysteine Proteinases; B. Wiederanders. Human Cathepsins W and F Form" Review Citations:

Scitech Book News 09/01/2000 pg. 58 (EAN 9780306463839, Hardcover)

Medios de comunicación Libros     Hardcover Book   (Libro con lomo y cubierta duros)
Publicado 31 de mayo de 2000
ISBN13 9780306463839
Editores Springer Science+Business Media
Páginas 522
Dimensiones 178 × 254 × 30 mm   ·   1,15 kg
Editor Ansorge, Siegfried
Editor Langner, Jurgen

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