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Cellular peptidases in immune functions and diseases 2 [[electronic resource] /] / edited by Jürgen Langner and Siegfried Ansorge
| Cellular peptidases in immune functions and diseases 2 [[electronic resource] /] / edited by Jürgen Langner and Siegfried Ansorge |
| Edizione | [1st ed. 2002.] |
| Pubbl/distr/stampa | New York, : Kluwer Academic/Plenum, c2000 |
| Descrizione fisica | 1 online resource (537 p.) |
| Disciplina | 616.07/9 |
| Altri autori (Persone) |
LangnerJürgen
AnsorgeSiegfried |
| Collana | Advances in experimental medicine and biology |
| Soggetto topico |
Peptidase - Immunology
Peptidase - Pathophysiology Endopeptidases - Immunology Endopeptidases - Pathophysiology |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-280-04290-7
9786610042906 0-306-46826-3 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | Membrane Ectopeptidases with Influence on Immune Functions -- Review: The Role of Membrane Peptidase in Immune Functions -- Structure and Function of Aminopeptidase N -- Modulation of WNT-5At Eexpression by Actinonin: Linkage of APN to the WNT-Pathway? -- Enzymatic Activity Is Not A Precondition For The Intracellular Calcium Increase Mediated By mAbs Specific For Aminopeptidase N/CD13 -- Transforming Growth Factor-? Increases the Expression of Aminopeptidase N/CD13 mRNA and Protein in Monocytes and Monocytic Cell Lines -- Cell-Cell Contact Between Lymphocytes and Fibroblast-Like Synovioctyes Induces Lymphocytic Expression of Aminopeptidase n/cd13 and Results in Lymphocytic Activation -- Natural Substrates of Dipeptidyl Peptidase IV -- Relating Structure to Function in the Beta-Propeller Domain of Dipeptidyl Peptidase IV -- Development of a Tertiary-Structure Model of the C-Terminal Domain of DPP IV -- Post Proline Cleaving Peptidases Having DP IV Like Enzyme Activity -- A New Type of Fluorogenic Substrates for Determination of Cellular Dipeptidyl Peptidese IV (DP IV/CD26) Activity -- Potent Inhibitors of Dipeptidyl Peptidase iv and Their Mechanisms of Inhibition -- N-Terminal HIV-1 Tat Nonapeptides as Inhibitors of Dipeptidyl Peptidase IV. Conformational Characterization -- Signal Transduction Events Induced or Affected by Inhibition of the Catalytic Activity of Dipeptidyl Peptidase IV (DP IV, CD26) -- Specific Inhibitors of Dipeptidyl Peptidase IV Suppress mRNA Expression of DP IV/CD26 and Cytokines -- Dipeptidyl Peptidase IV in Inflammatory CNS Disease -- Dipeptidyl Peptidase IV (CD26): Role in T Cell Activation and Autoimmune Disease -- 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 -- DNA Synthesis in Cultured Human Keratinocytes and Hacat Kerationcytes is Reduced by Specific Inhibition of Dipeptidyl Peptidase IV (CD26) Enzymatic Activity -- Attractin: A Cub-Family Protease Involved in T Cell-Monocyte/Macrophage Interactions -- Analogs of Glucose-Dependent Insulinotropic Polypeptide With Increased Dipeptidyl Peptidase IV Resistance -- Dipeptidyl Peptidase IV (DPP IV, CD26) In Patients With Mental Eating Disorders -- The Membrane-Bound Ectopeptidase CPM as a Marker Of Macrophage Maturation in vitro And in vivo -- Matrix Metalloproteinases (MMP-8, -13 and -14) Interact with the Clotting System and Degrade Fibrinogen and Factor XII (Hagemann Factor) -- The Neprilysin Family in Health and Disease -- Cellular Endopeptidases: New Cathepsins; Results from Knock-out-mice; Regulatory Aspects -- Review: Novel Cysteine Proteases of the Papain Family -- Development and Validation of Homology Models of Human Cathepsins K, S, H, and F -- The Function of Propeptide Domains of Cysteine Proteinases -- Human Cathepsins W and F form A New Subgroup of Cathepsins that is Evolutionary Separated from the Cathepsin B- and L-Like Cysteine Proteases -- Cathepsin K Expression in Human Lung -- Expression of Cathepsins B and L in Human Lung Epithelial Cells is Regulated by Cytokines -- Functions of Cathepsin K in Bone Resorption -- Ceramide as an Activator Lipid of Cathepsin D -- Human Cathepsin X -- A Novel Proteolytic Mechanism for Termination of the Ca2+ Signalling Evoked by Proteinase-Activated Receptor-1 (PAR-1) in Rat Astrocytes -- Natural and Synthetic Inhibitors of The Tumor-Associated Serine Protease Urokinase-Type Plasminogen Activator -- Processing of Interleukin-18 by Human Vascular Smooth Muscle Cells -- Peptidases and Peptidase Inhibitors in Pathogensis of Diseases -- Review: Peptidases and Peptidase Inhibitors in the Pathogenesis of Diseases -- The Role of Proteolysis in Alzheimer’s Disease -- Observing Proteases in Living Cells -- The Role of Cysteine Proteases in Intracellular Pancreatic Serine Protease Activation -- Peptidases in the Asthmatic Airways -- Inactivation of Interleukin-6 by Neutrophil Proteases at Sites of Inflammation -- Antisense Inhibition of Cathepsin Bina Human Osteosarcoma Cell Line -- Protease-Protease Inhibitor Balance in the Gastric Mucosa -- The Role of Bacterial and Host Proteinases in Periodontal Disease -- Multifunctional Role of Proteases in Rhumatic Diseases -- Evidence of Proteolytic Activation of Transforming Growth Factor ? in Synovial Fluid -- Matrix Metalloproteinases and Tace Play A Role in The Pathogenesis of Endometriosis -- Influence of Proliferation, Differentiation and Dedifferentiation Factors on the Expression of the Lysosomal Cysteine Proteinase Cathepsin L (CL) in Thyroid Cancer Cell Lines. |
| Record Nr. | UNINA-9910455259603321 |
| New York, : Kluwer Academic/Plenum, c2000 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Cellular peptidases in immune functions and diseases 2 [[electronic resource] /] / edited by Jürgen Langner and Siegfried Ansorge
| Cellular peptidases in immune functions and diseases 2 [[electronic resource] /] / edited by Jürgen Langner and Siegfried Ansorge |
| Edizione | [1st ed. 2002.] |
| Pubbl/distr/stampa | New York, : Kluwer Academic/Plenum, c2000 |
| Descrizione fisica | 1 online resource (537 p.) |
| Disciplina | 616.07/9 |
| Altri autori (Persone) |
LangnerJürgen
AnsorgeSiegfried |
| Collana | Advances in Experimental Medicine and Biology |
| Soggetto topico |
Peptidase - Immunology
Peptidase - Pathophysiology Endopeptidases - Immunology Endopeptidases - Pathophysiology |
| ISBN |
1-280-04290-7
9786610042906 0-306-46826-3 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | Membrane Ectopeptidases with Influence on Immune Functions -- Review: The Role of Membrane Peptidase in Immune Functions -- Structure and Function of Aminopeptidase N -- Modulation of WNT-5At Eexpression by Actinonin: Linkage of APN to the WNT-Pathway? -- Enzymatic Activity Is Not A Precondition For The Intracellular Calcium Increase Mediated By mAbs Specific For Aminopeptidase N/CD13 -- Transforming Growth Factor-? Increases the Expression of Aminopeptidase N/CD13 mRNA and Protein in Monocytes and Monocytic Cell Lines -- Cell-Cell Contact Between Lymphocytes and Fibroblast-Like Synovioctyes Induces Lymphocytic Expression of Aminopeptidase n/cd13 and Results in Lymphocytic Activation -- Natural Substrates of Dipeptidyl Peptidase IV -- Relating Structure to Function in the Beta-Propeller Domain of Dipeptidyl Peptidase IV -- Development of a Tertiary-Structure Model of the C-Terminal Domain of DPP IV -- Post Proline Cleaving Peptidases Having DP IV Like Enzyme Activity -- A New Type of Fluorogenic Substrates for Determination of Cellular Dipeptidyl Peptidese IV (DP IV/CD26) Activity -- Potent Inhibitors of Dipeptidyl Peptidase iv and Their Mechanisms of Inhibition -- N-Terminal HIV-1 Tat Nonapeptides as Inhibitors of Dipeptidyl Peptidase IV. Conformational Characterization -- Signal Transduction Events Induced or Affected by Inhibition of the Catalytic Activity of Dipeptidyl Peptidase IV (DP IV, CD26) -- Specific Inhibitors of Dipeptidyl Peptidase IV Suppress mRNA Expression of DP IV/CD26 and Cytokines -- Dipeptidyl Peptidase IV in Inflammatory CNS Disease -- Dipeptidyl Peptidase IV (CD26): Role in T Cell Activation and Autoimmune Disease -- 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 -- DNA Synthesis in Cultured Human Keratinocytes and Hacat Kerationcytes is Reduced by Specific Inhibition of Dipeptidyl Peptidase IV (CD26) Enzymatic Activity -- Attractin: A Cub-Family Protease Involved in T Cell-Monocyte/Macrophage Interactions -- Analogs of Glucose-Dependent Insulinotropic Polypeptide With Increased Dipeptidyl Peptidase IV Resistance -- Dipeptidyl Peptidase IV (DPP IV, CD26) In Patients With Mental Eating Disorders -- The Membrane-Bound Ectopeptidase CPM as a Marker Of Macrophage Maturation in vitro And in vivo -- Matrix Metalloproteinases (MMP-8, -13 and -14) Interact with the Clotting System and Degrade Fibrinogen and Factor XII (Hagemann Factor) -- The Neprilysin Family in Health and Disease -- Cellular Endopeptidases: New Cathepsins; Results from Knock-out-mice; Regulatory Aspects -- Review: Novel Cysteine Proteases of the Papain Family -- Development and Validation of Homology Models of Human Cathepsins K, S, H, and F -- The Function of Propeptide Domains of Cysteine Proteinases -- Human Cathepsins W and F form A New Subgroup of Cathepsins that is Evolutionary Separated from the Cathepsin B- and L-Like Cysteine Proteases -- Cathepsin K Expression in Human Lung -- Expression of Cathepsins B and L in Human Lung Epithelial Cells is Regulated by Cytokines -- Functions of Cathepsin K in Bone Resorption -- Ceramide as an Activator Lipid of Cathepsin D -- Human Cathepsin X -- A Novel Proteolytic Mechanism for Termination of the Ca2+ Signalling Evoked by Proteinase-Activated Receptor-1 (PAR-1) in Rat Astrocytes -- Natural and Synthetic Inhibitors of The Tumor-Associated Serine Protease Urokinase-Type Plasminogen Activator -- Processing of Interleukin-18 by Human Vascular Smooth Muscle Cells -- Peptidases and Peptidase Inhibitors in Pathogensis of Diseases -- Review: Peptidases and Peptidase Inhibitors in the Pathogenesis of Diseases -- The Role of Proteolysis in Alzheimer’s Disease -- Observing Proteases in Living Cells -- The Role of Cysteine Proteases in Intracellular Pancreatic Serine Protease Activation -- Peptidases in the Asthmatic Airways -- Inactivation of Interleukin-6 by Neutrophil Proteases at Sites of Inflammation -- Antisense Inhibition of Cathepsin Bina Human Osteosarcoma Cell Line -- Protease-Protease Inhibitor Balance in the Gastric Mucosa -- The Role of Bacterial and Host Proteinases in Periodontal Disease -- Multifunctional Role of Proteases in Rhumatic Diseases -- Evidence of Proteolytic Activation of Transforming Growth Factor ? in Synovial Fluid -- Matrix Metalloproteinases and Tace Play A Role in The Pathogenesis of Endometriosis -- Influence of Proliferation, Differentiation and Dedifferentiation Factors on the Expression of the Lysosomal Cysteine Proteinase Cathepsin L (CL) in Thyroid Cancer Cell Lines. |
| Record Nr. | UNINA-9910779963203321 |
| New York, : Kluwer Academic/Plenum, c2000 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
Cellular peptidases in immune functions and diseases 2 / / edited by Jurgen Langner and Siegfried Ansorge
| Cellular peptidases in immune functions and diseases 2 / / edited by Jurgen Langner and Siegfried Ansorge |
| Edizione | [1st ed. 2002.] |
| Pubbl/distr/stampa | New York, : Kluwer Academic/Plenum, c2000 |
| Descrizione fisica | 1 online resource (537 p.) |
| Disciplina | 616.07/9 |
| Altri autori (Persone) |
LangnerJurgen
AnsorgeSiegfried |
| Collana | Advances in experimental medicine and biology |
| Soggetto topico |
Peptidase - Immunology
Peptidase - Pathophysiology Endopeptidases - Immunology Endopeptidases - Pathophysiology |
| ISBN |
1-280-04290-7
9786610042906 0-306-46826-3 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | Membrane Ectopeptidases with Influence on Immune Functions -- Review: The Role of Membrane Peptidase in Immune Functions -- Structure and Function of Aminopeptidase N -- Modulation of WNT-5At Eexpression by Actinonin: Linkage of APN to the WNT-Pathway? -- Enzymatic Activity Is Not A Precondition For The Intracellular Calcium Increase Mediated By mAbs Specific For Aminopeptidase N/CD13 -- Transforming Growth Factor-? Increases the Expression of Aminopeptidase N/CD13 mRNA and Protein in Monocytes and Monocytic Cell Lines -- Cell-Cell Contact Between Lymphocytes and Fibroblast-Like Synovioctyes Induces Lymphocytic Expression of Aminopeptidase n/cd13 and Results in Lymphocytic Activation -- Natural Substrates of Dipeptidyl Peptidase IV -- Relating Structure to Function in the Beta-Propeller Domain of Dipeptidyl Peptidase IV -- Development of a Tertiary-Structure Model of the C-Terminal Domain of DPP IV -- Post Proline Cleaving Peptidases Having DP IV Like Enzyme Activity -- A New Type of Fluorogenic Substrates for Determination of Cellular Dipeptidyl Peptidese IV (DP IV/CD26) Activity -- Potent Inhibitors of Dipeptidyl Peptidase iv and Their Mechanisms of Inhibition -- N-Terminal HIV-1 Tat Nonapeptides as Inhibitors of Dipeptidyl Peptidase IV. Conformational Characterization -- Signal Transduction Events Induced or Affected by Inhibition of the Catalytic Activity of Dipeptidyl Peptidase IV (DP IV, CD26) -- Specific Inhibitors of Dipeptidyl Peptidase IV Suppress mRNA Expression of DP IV/CD26 and Cytokines -- Dipeptidyl Peptidase IV in Inflammatory CNS Disease -- Dipeptidyl Peptidase IV (CD26): Role in T Cell Activation and Autoimmune Disease -- 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 -- DNA Synthesis in Cultured Human Keratinocytes and Hacat Kerationcytes is Reduced by Specific Inhibition of Dipeptidyl Peptidase IV (CD26) Enzymatic Activity -- Attractin: A Cub-Family Protease Involved in T Cell-Monocyte/Macrophage Interactions -- Analogs of Glucose-Dependent Insulinotropic Polypeptide With Increased Dipeptidyl Peptidase IV Resistance -- Dipeptidyl Peptidase IV (DPP IV, CD26) In Patients With Mental Eating Disorders -- The Membrane-Bound Ectopeptidase CPM as a Marker Of Macrophage Maturation in vitro And in vivo -- Matrix Metalloproteinases (MMP-8, -13 and -14) Interact with the Clotting System and Degrade Fibrinogen and Factor XII (Hagemann Factor) -- The Neprilysin Family in Health and Disease -- Cellular Endopeptidases: New Cathepsins; Results from Knock-out-mice; Regulatory Aspects -- Review: Novel Cysteine Proteases of the Papain Family -- Development and Validation of Homology Models of Human Cathepsins K, S, H, and F -- The Function of Propeptide Domains of Cysteine Proteinases -- Human Cathepsins W and F form A New Subgroup of Cathepsins that is Evolutionary Separated from the Cathepsin B- and L-Like Cysteine Proteases -- Cathepsin K Expression in Human Lung -- Expression of Cathepsins B and L in Human Lung Epithelial Cells is Regulated by Cytokines -- Functions of Cathepsin K in Bone Resorption -- Ceramide as an Activator Lipid of Cathepsin D -- Human Cathepsin X -- A Novel Proteolytic Mechanism for Termination of the Ca2+ Signalling Evoked by Proteinase-Activated Receptor-1 (PAR-1) in Rat Astrocytes -- Natural and Synthetic Inhibitors of The Tumor-Associated Serine Protease Urokinase-Type Plasminogen Activator -- Processing of Interleukin-18 by Human Vascular Smooth Muscle Cells -- Peptidases and Peptidase Inhibitors in Pathogensis of Diseases -- Review: Peptidases and Peptidase Inhibitors in the Pathogenesis of Diseases -- The Role of Proteolysis in Alzheimer’s Disease -- Observing Proteases in Living Cells -- The Role of Cysteine Proteases in Intracellular Pancreatic Serine Protease Activation -- Peptidases in the Asthmatic Airways -- Inactivation of Interleukin-6 by Neutrophil Proteases at Sites of Inflammation -- Antisense Inhibition of Cathepsin Bina Human Osteosarcoma Cell Line -- Protease-Protease Inhibitor Balance in the Gastric Mucosa -- The Role of Bacterial and Host Proteinases in Periodontal Disease -- Multifunctional Role of Proteases in Rhumatic Diseases -- Evidence of Proteolytic Activation of Transforming Growth Factor ? in Synovial Fluid -- Matrix Metalloproteinases and Tace Play A Role in The Pathogenesis of Endometriosis -- Influence of Proliferation, Differentiation and Dedifferentiation Factors on the Expression of the Lysosomal Cysteine Proteinase Cathepsin L (CL) in Thyroid Cancer Cell Lines. |
| Record Nr. | UNINA-9910828021203321 |
| New York, : Kluwer Academic/Plenum, c2000 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
