[beta]-Lactams : unique structures of distinction for novel molecules / / volume editor: Bimal K. Banik ; with contributions by B. K. Banik ...[et al.] |
Edizione | [1st ed. 2013.] |
Pubbl/distr/stampa | Berlin ; ; Heidelberg, : Springer, c2013 |
Descrizione fisica | 1 online resource (X, 226 p.) |
Disciplina | 547.642 |
Altri autori (Persone) | BanikBimal K |
Collana | Topics in heterocyclic chemistry |
Soggetto topico |
Beta lactamases
Hydrolases |
ISBN | 3-642-33188-2 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto | Advances in the Use of Enantiopure β-Lactams for the Synthesis of Biologically Active Compounds of Medicinal Interests -- β -Lactams from Fischer Carbene Complexes: Scope, Limitations, and Reaction Mechanism -- Synthesis of β-Lactams Through Alkyne–Nitrone Cycloadditions.-Preparation of Bis-β-Lactams by Ketene–Imine Cycloadditions -- The Chemistry and Biology of N-Thiolated β -Lactams -- Synthesis of β-Lactams and Their Chemical Manipulations Via Microwave-Induced Reactions. |
Record Nr. | UNINA-9910768190103321 |
Berlin ; ; Heidelberg, : Springer, c2013 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Hydrolases in organic synthesis [[electronic resource] ] : regio- and stereoselective biotransformations / / Uwe T. Bornscheuer and Romas J. Kazlauskas |
Autore | Bornscheuer U. T (Uwe Theo), <1964-> |
Edizione | [2nd ed.] |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH |
Descrizione fisica | 1 online resource (369 p.) |
Disciplina | 547.2 |
Altri autori (Persone) | KazlauskasR. J <1956-> (Romas J.) |
Soggetto topico |
Catalysis
Hydrolases Organic compounds - Synthesis |
Soggetto genere / forma | Electronic books. |
ISBN |
1-280-85420-0
9786610854202 3-527-60754-4 3-527-60712-9 |
Classificazione | 35.74 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Hydrolases in Organic Synthesis; Preface for the 2(nd) edition; Preface for the 1(st) edition; Acknowledgments; Contents; 1 Introduction; 2 Designing Enantioselective Reactions; 2.1 Kinetic Resolutions; 2.1.1 Recycling and Sequential Kinetic Resolutions; 2.1.2 Dynamic Kinetic Resolutions; 2.1.2.1 Introduction; 2.1.2.2 Racemization by Protonation/Deprotonation; 2.1.2.3 Racemization by Addition/Elimination; 2.1.2.4 Racemization by Nucleophilic Substitution; 2.1.2.5 Racemization by Oxidation/Reduction; 2.1.2.6 Related Strategies; 2.2 Asymmetric Syntheses
3 Choosing Reaction Media: Water and Organic Solvents3.1 Hydrolysis in Water; 3.2 Transesterifications and Condensations in Organic Solvents; 3.2.1 Increasing the Catalytic Activity in Organic Solvents; 3.2.1.1 Choosing the Best Organic Solvent for High Activity; 3.2.2 Increasing the Enantioselectivity in Organic Solvents; 3.2.3 Water Content and Water Activity; 3.3 Other Reaction Media; 3.3.1 Ionic Liquids; 3.3.2 Reverse Micelles; 3.3.3 Supercritical Fluids; 3.4 Immobilization; 3.4.1 Introduction; 3.4.1.1 Increasing the Surface Area to Increase Catalytic Activity 4 Protein Sources and Optimization of Biocatalyst Performance4.1 Accessing Biodiversity; 4.2 Creating Improved Biocatalysts; 4.2.1 Directed Evolution; 4.2.1.1 Methods to Create Mutant Libraries; 4.2.1.2 Assay Systems; 4.2.1.3 Selected Examples; 4.2.2 Focused Directed Evolution; 4.3 Catalytic Promiscuity in Hydrolases; 4.3.1 Reactions Involving Functional Group Analogs; 4.3.1.1 Perhydrolases; 4.3.2 Aldol and Michael additions Catalyzed by Hydrolases; 4.3.2.1 Aldol Additions; 4.3.2.2 Michael-Type Additions; 4.3.3 Modifications to Introduce New Reactivity in Hydrolases 4.3.3.1 Enantioselective Reduction of Hydroperoxides with Selenosubtilisin4.3.3.2 Vanadate-Modified Phosphatases as Peroxidases; 5 Lipases and Esterases; 5.1 Availability, Structures and Properties; 5.1.1 Lipases; 5.1.1.1 Classification of Lipases; 5.1.1.2 General Features of PPL, PCL, CRL, CAL-B, and RML; 5.1.2 Esterases; 5.1.3 Lipases and Esterases are α/β Hydrolases; 5.1.4 Lid or Flap in Interfacial Activation of Lipases; 5.1.5 Substrate Binding Site in Lipases and Esterases; 5.1.6 Designing Reactions with Lipases and Esterases; 5.1.6.1 Acyl Donor for Acylation Reactions 5.1.7 Assays for Lipases and Esterases5.1.7.1 Requirements for a Suitable Assay; 5.1.7.2 How to Distinguish Between Lipase, Esterase, and Protease; 5.2 Survey of Enantioselective Lipase-Catalyzed Reactions; 5.2.1 Alcohols; 5.2.1.1 Secondary Alcohols; 5.2.1.2 Primary Alcohols; 5.2.1.3 Other Alcohols, Amines, and Alcohol Analogs; 5.2.2 Carboxylic Acids; 5.2.2.1 General Considerations; 5.2.2.2 Carboxylic Acids with a Stereocenter at the α-Position; 5.2.2.3 Carboxylic Acids with a Stereocenter at the β-Position; 5.2.2.4 Other Carboxylic Acids; 5.2.2.5 Double Enantioselection; 5.2.2.6 Anhydrides 5.2.3 Lactones |
Record Nr. | UNINA-9910144323603321 |
Bornscheuer U. T (Uwe Theo), <1964-> | ||
Weinheim, : Wiley-VCH | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Hydrolases in organic synthesis [[electronic resource] ] : regio- and stereoselective biotransformations / / Uwe T. Bornscheuer and Romas J. Kazlauskas |
Autore | Bornscheuer U. T (Uwe Theo), <1964-> |
Edizione | [2nd ed.] |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH |
Descrizione fisica | 1 online resource (369 p.) |
Disciplina | 547.2 |
Altri autori (Persone) | KazlauskasR. J <1956-> (Romas J.) |
Soggetto topico |
Catalysis
Hydrolases Organic compounds - Synthesis |
ISBN |
1-280-85420-0
9786610854202 3-527-60754-4 3-527-60712-9 |
Classificazione | 35.74 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Hydrolases in Organic Synthesis; Preface for the 2(nd) edition; Preface for the 1(st) edition; Acknowledgments; Contents; 1 Introduction; 2 Designing Enantioselective Reactions; 2.1 Kinetic Resolutions; 2.1.1 Recycling and Sequential Kinetic Resolutions; 2.1.2 Dynamic Kinetic Resolutions; 2.1.2.1 Introduction; 2.1.2.2 Racemization by Protonation/Deprotonation; 2.1.2.3 Racemization by Addition/Elimination; 2.1.2.4 Racemization by Nucleophilic Substitution; 2.1.2.5 Racemization by Oxidation/Reduction; 2.1.2.6 Related Strategies; 2.2 Asymmetric Syntheses
3 Choosing Reaction Media: Water and Organic Solvents3.1 Hydrolysis in Water; 3.2 Transesterifications and Condensations in Organic Solvents; 3.2.1 Increasing the Catalytic Activity in Organic Solvents; 3.2.1.1 Choosing the Best Organic Solvent for High Activity; 3.2.2 Increasing the Enantioselectivity in Organic Solvents; 3.2.3 Water Content and Water Activity; 3.3 Other Reaction Media; 3.3.1 Ionic Liquids; 3.3.2 Reverse Micelles; 3.3.3 Supercritical Fluids; 3.4 Immobilization; 3.4.1 Introduction; 3.4.1.1 Increasing the Surface Area to Increase Catalytic Activity 4 Protein Sources and Optimization of Biocatalyst Performance4.1 Accessing Biodiversity; 4.2 Creating Improved Biocatalysts; 4.2.1 Directed Evolution; 4.2.1.1 Methods to Create Mutant Libraries; 4.2.1.2 Assay Systems; 4.2.1.3 Selected Examples; 4.2.2 Focused Directed Evolution; 4.3 Catalytic Promiscuity in Hydrolases; 4.3.1 Reactions Involving Functional Group Analogs; 4.3.1.1 Perhydrolases; 4.3.2 Aldol and Michael additions Catalyzed by Hydrolases; 4.3.2.1 Aldol Additions; 4.3.2.2 Michael-Type Additions; 4.3.3 Modifications to Introduce New Reactivity in Hydrolases 4.3.3.1 Enantioselective Reduction of Hydroperoxides with Selenosubtilisin4.3.3.2 Vanadate-Modified Phosphatases as Peroxidases; 5 Lipases and Esterases; 5.1 Availability, Structures and Properties; 5.1.1 Lipases; 5.1.1.1 Classification of Lipases; 5.1.1.2 General Features of PPL, PCL, CRL, CAL-B, and RML; 5.1.2 Esterases; 5.1.3 Lipases and Esterases are α/β Hydrolases; 5.1.4 Lid or Flap in Interfacial Activation of Lipases; 5.1.5 Substrate Binding Site in Lipases and Esterases; 5.1.6 Designing Reactions with Lipases and Esterases; 5.1.6.1 Acyl Donor for Acylation Reactions 5.1.7 Assays for Lipases and Esterases5.1.7.1 Requirements for a Suitable Assay; 5.1.7.2 How to Distinguish Between Lipase, Esterase, and Protease; 5.2 Survey of Enantioselective Lipase-Catalyzed Reactions; 5.2.1 Alcohols; 5.2.1.1 Secondary Alcohols; 5.2.1.2 Primary Alcohols; 5.2.1.3 Other Alcohols, Amines, and Alcohol Analogs; 5.2.2 Carboxylic Acids; 5.2.2.1 General Considerations; 5.2.2.2 Carboxylic Acids with a Stereocenter at the α-Position; 5.2.2.3 Carboxylic Acids with a Stereocenter at the β-Position; 5.2.2.4 Other Carboxylic Acids; 5.2.2.5 Double Enantioselection; 5.2.2.6 Anhydrides 5.2.3 Lactones |
Record Nr. | UNINA-9910830217203321 |
Bornscheuer U. T (Uwe Theo), <1964-> | ||
Weinheim, : Wiley-VCH | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Hydrolases in organic synthesis : regio- and stereoselective biotransformations / / Uwe T. Bornscheuer and Romas J. Kazlauskas |
Autore | Bornscheuer U. T (Uwe Theo), <1964-> |
Edizione | [2nd ed.] |
Pubbl/distr/stampa | Weinheim, : Wiley-VCH |
Descrizione fisica | 1 online resource (369 p.) |
Disciplina | 547.2 |
Altri autori (Persone) | KazlauskasR. J <1956-> (Romas J.) |
Soggetto topico |
Catalysis
Hydrolases Organic compounds - Synthesis |
ISBN |
1-280-85420-0
9786610854202 3-527-60754-4 3-527-60712-9 |
Classificazione | 35.74 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Hydrolases in Organic Synthesis; Preface for the 2(nd) edition; Preface for the 1(st) edition; Acknowledgments; Contents; 1 Introduction; 2 Designing Enantioselective Reactions; 2.1 Kinetic Resolutions; 2.1.1 Recycling and Sequential Kinetic Resolutions; 2.1.2 Dynamic Kinetic Resolutions; 2.1.2.1 Introduction; 2.1.2.2 Racemization by Protonation/Deprotonation; 2.1.2.3 Racemization by Addition/Elimination; 2.1.2.4 Racemization by Nucleophilic Substitution; 2.1.2.5 Racemization by Oxidation/Reduction; 2.1.2.6 Related Strategies; 2.2 Asymmetric Syntheses
3 Choosing Reaction Media: Water and Organic Solvents3.1 Hydrolysis in Water; 3.2 Transesterifications and Condensations in Organic Solvents; 3.2.1 Increasing the Catalytic Activity in Organic Solvents; 3.2.1.1 Choosing the Best Organic Solvent for High Activity; 3.2.2 Increasing the Enantioselectivity in Organic Solvents; 3.2.3 Water Content and Water Activity; 3.3 Other Reaction Media; 3.3.1 Ionic Liquids; 3.3.2 Reverse Micelles; 3.3.3 Supercritical Fluids; 3.4 Immobilization; 3.4.1 Introduction; 3.4.1.1 Increasing the Surface Area to Increase Catalytic Activity 4 Protein Sources and Optimization of Biocatalyst Performance4.1 Accessing Biodiversity; 4.2 Creating Improved Biocatalysts; 4.2.1 Directed Evolution; 4.2.1.1 Methods to Create Mutant Libraries; 4.2.1.2 Assay Systems; 4.2.1.3 Selected Examples; 4.2.2 Focused Directed Evolution; 4.3 Catalytic Promiscuity in Hydrolases; 4.3.1 Reactions Involving Functional Group Analogs; 4.3.1.1 Perhydrolases; 4.3.2 Aldol and Michael additions Catalyzed by Hydrolases; 4.3.2.1 Aldol Additions; 4.3.2.2 Michael-Type Additions; 4.3.3 Modifications to Introduce New Reactivity in Hydrolases 4.3.3.1 Enantioselective Reduction of Hydroperoxides with Selenosubtilisin4.3.3.2 Vanadate-Modified Phosphatases as Peroxidases; 5 Lipases and Esterases; 5.1 Availability, Structures and Properties; 5.1.1 Lipases; 5.1.1.1 Classification of Lipases; 5.1.1.2 General Features of PPL, PCL, CRL, CAL-B, and RML; 5.1.2 Esterases; 5.1.3 Lipases and Esterases are α/β Hydrolases; 5.1.4 Lid or Flap in Interfacial Activation of Lipases; 5.1.5 Substrate Binding Site in Lipases and Esterases; 5.1.6 Designing Reactions with Lipases and Esterases; 5.1.6.1 Acyl Donor for Acylation Reactions 5.1.7 Assays for Lipases and Esterases5.1.7.1 Requirements for a Suitable Assay; 5.1.7.2 How to Distinguish Between Lipase, Esterase, and Protease; 5.2 Survey of Enantioselective Lipase-Catalyzed Reactions; 5.2.1 Alcohols; 5.2.1.1 Secondary Alcohols; 5.2.1.2 Primary Alcohols; 5.2.1.3 Other Alcohols, Amines, and Alcohol Analogs; 5.2.2 Carboxylic Acids; 5.2.2.1 General Considerations; 5.2.2.2 Carboxylic Acids with a Stereocenter at the α-Position; 5.2.2.3 Carboxylic Acids with a Stereocenter at the β-Position; 5.2.2.4 Other Carboxylic Acids; 5.2.2.5 Double Enantioselection; 5.2.2.6 Anhydrides 5.2.3 Lactones |
Record Nr. | UNINA-9910876948003321 |
Bornscheuer U. T (Uwe Theo), <1964-> | ||
Weinheim, : Wiley-VCH | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Iminosugars as glycosidase inhibitors : Nojirimycin and beyond |
Pubbl/distr/stampa | [Place of publication not identified], : Wiley VCH, 1999 |
Descrizione fisica | 1 online resource (411 pages) |
Disciplina | 572/.793 |
Soggetto topico |
Glycosidases - Inhibitors
Imino compounds - Physiological effect Enzyme Inhibitors Glycoside Hydrolases Amino Sugars Carbohydrates Molecular Mechanisms of Pharmacological Action Hydrolases Pharmacologic Actions Chemicals and Drugs Enzymes Chemical Actions and Uses Enzymes and Coenzymes Animal Biochemistry Human Anatomy & Physiology Health & Biological Sciences |
Soggetto genere / forma | Electronic books. |
ISBN |
1-280-55869-5
9786610558698 3-527-60174-0 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Record Nr. | UNINA-9910146057803321 |
[Place of publication not identified], : Wiley VCH, 1999 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Iminosugars as glycosidase inhibitors : Nojirimycin and beyond |
Pubbl/distr/stampa | [Place of publication not identified], : Wiley VCH, 1999 |
Descrizione fisica | 1 online resource (411 pages) |
Disciplina | 572/.793 |
Soggetto topico |
Glycosidases - Inhibitors
Imino compounds - Physiological effect Enzyme Inhibitors Glycoside Hydrolases Amino Sugars Carbohydrates Molecular Mechanisms of Pharmacological Action Hydrolases Pharmacologic Actions Chemicals and Drugs Enzymes Chemical Actions and Uses Enzymes and Coenzymes Animal Biochemistry Human Anatomy & Physiology Health & Biological Sciences |
ISBN |
1-280-55869-5
9786610558698 3-527-60174-0 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Record Nr. | UNINA-9910830223903321 |
[Place of publication not identified], : Wiley VCH, 1999 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Iminosugars as glycosidase inhibitors : Nojirimycin and beyond |
Pubbl/distr/stampa | [Place of publication not identified], : Wiley VCH, 1999 |
Descrizione fisica | 1 online resource (411 pages) |
Disciplina | 572/.793 |
Soggetto topico |
Glycosidases - Inhibitors
Imino compounds - Physiological effect Enzyme Inhibitors Glycoside Hydrolases Amino Sugars Carbohydrates Molecular Mechanisms of Pharmacological Action Hydrolases Pharmacologic Actions Chemicals and Drugs Enzymes Chemical Actions and Uses Enzymes and Coenzymes Animal Biochemistry Human Anatomy & Physiology Health & Biological Sciences |
ISBN |
1-280-55869-5
9786610558698 3-527-60174-0 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Record Nr. | UNINA-9910876967303321 |
[Place of publication not identified], : Wiley VCH, 1999 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Mammalian alkaline phosphatases : from biology to applications in medicine and biotechnology / / Jose Luis Millan |
Autore | Millan Jose Luis |
Pubbl/distr/stampa | Weinheim ; ; Chichester, : Wiley-VCH, c2006 |
Descrizione fisica | 1 online resource (340 p.) |
Disciplina | 572.7553 |
Soggetto topico |
Alkaline phosphatase
Hydrolases |
ISBN |
1-280-72272-X
9786610722723 3-527-60806-0 3-527-60747-1 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Mammalian Alkaline Phosphatases; Contents; Preface; Abbreviations; Glossary; Introduction; Part I Gene and Protein Structure; 1 Gene Structure; 1.1 Genomic Organization and Complexity; 1.2 Restriction Fragment Length Polymorphisms; 2 Developmental Expression; 2.1 The TNAP Gene; 2.2 The TSAP Genes; 3 Gene Regulation; 3.1 The TNAP Gene; 3.2 The TSAP Genes; 4 Protein Structure and Functional Domains; 4.1 The Three-dimensional Structure of PLAP; 4.1.1 Overview of the Structure; 4.1.2 The Active Site; 4.1.3 The Calcium Site; 4.1.4 The Disulfide Bonds; 4.1.5 The N-terminal Arm
4.1.6 The Crown Domain4.1.7 The Monomer-Monomer Interface; 4.1.8 The Noncatalytic Peripheral Binding Site; 4.2 Genetic Polymorphism and Protein Variability; 4.3 Post-translational Modifications; 4.3.1 Glycosylation Sites; 4.3.2 Ectoplasmic Localization of APs via a GPI Anchor; 4.3.3 Nonenzymatic Glycation of APs; 4.3.4 Quaternary Structure of APs; 4.3.5 Subcellular Localization of APs; 5 Enzymatic Properties; 5.1 Catalytic Inhibition; 5.1.1 Competitive and Noncompetitive Inhibitors of APs; 5.1.2 Uncompetitive Inhibition; 5.1.2.1 Mechanism of Inhibition in PLAP/GCAP 5.1.2.2 Inhibitor Binding in TNAP5.2 Allosteric Behavior; 5.3 Catalytic Efficiency of Mammalian APs; 5.4 Substrate Specificities; 5.5 APs as Members of a Superfamily of Enzymes; 6 Epitope Maps; 6.1 Epitopes in PLAP and GCAP; 6.2 Epitopes in IAP; 6.3 Discrimination Between Bone and Liver TNAP; Part II In Vivo Functions; 7 The In Vivo Role of TNAP; 7.1 Function of TNAP in Bone; 7.1.1 Hypophosphatasia; 7.1.2 Hypophosphatasia Mutations; 7.1.3 Variable Penetrance and Expressivity; 7.2 Role of TNAP in Nonskeletal Tissues; 7.3 Proposed Biological Functions of TSAPs; 7.3.1 Proposed Functions of IAP 7.3.2 Putative Functions of GCAP and PLAP8 Knockout Mouse Models; 8.1 Phenotypic Abnormalities in Akp2(-/-) mice; 8.1.1 Developmental and Skeletal Defects; 8.1.2 Dental Abnormalities in Akp2(-/-) Mice; 8.1.3 Deficient Mineralization by Akp2(-/-) Osteoblasts In Vitro; 8.1.4 Metabolic Pathways Affected in Akp2(-/-) Mice; 8.1.4.1 Neuro-physiological Abnormalities; 8.1.4.2 The Function of TNAP in Bone Mineralization; 8.1.4.3 Co-expression of TNAP and Fibrillar Collagens Restricts Calcification to Skeletal Tissues; 8.1.4.4 Other Organs Affected in Akp2(-/-) Mice 8.2 Phenotypic Abnormalities in Akp3(-/-) Mice8.3 Phenotypic Abnormalities in Akp5(-/-) Mice; Part III AP Expression in Health and Disease; 9 APs as Physiological and Disease Markers; 9.1 Clinical Usefulness of TNAP; 9.1.1 TNAP as a Marker of Bone Formation; 9.1.2 TNAP and Bone Cancer or Bone Metastasis; 9.1.3 TNAP Expression in Cholestasis; 9.1.4 TNAP in Other Conditions; 9.2 Clinical Usefulness of PLAP in Normal and Complicated Pregnancies; 9.3 IAP Expression in Relation to ABO Status, Fat Feeding and Other Pathologies; 9.4 Complexes of APs and Immunoglobulins; 9.5 Hyperphosphatasia 10 Neoplastic Expression of PLAP, GCAP, IAP (Regan, Nagao, Kasahara) and TNAP Isozymes |
Record Nr. | UNINA-9910877326703321 |
Millan Jose Luis | ||
Weinheim ; ; Chichester, : Wiley-VCH, c2006 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Mammalian alkaline phosphatases [[electronic resource] ] : from biology to applications in medicine and biotechnology / / José Luis Millán |
Autore | Millán José Luis |
Pubbl/distr/stampa | Weinheim ; ; Chichester, : Wiley-VCH, c2006 |
Descrizione fisica | 1 online resource (340 p.) |
Disciplina | 572.7553 |
Soggetto topico |
Alkaline phosphatase
Hydrolases |
Soggetto genere / forma | Electronic books. |
ISBN |
1-280-72272-X
9786610722723 3-527-60806-0 3-527-60747-1 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Mammalian Alkaline Phosphatases; Contents; Preface; Abbreviations; Glossary; Introduction; Part I Gene and Protein Structure; 1 Gene Structure; 1.1 Genomic Organization and Complexity; 1.2 Restriction Fragment Length Polymorphisms; 2 Developmental Expression; 2.1 The TNAP Gene; 2.2 The TSAP Genes; 3 Gene Regulation; 3.1 The TNAP Gene; 3.2 The TSAP Genes; 4 Protein Structure and Functional Domains; 4.1 The Three-dimensional Structure of PLAP; 4.1.1 Overview of the Structure; 4.1.2 The Active Site; 4.1.3 The Calcium Site; 4.1.4 The Disulfide Bonds; 4.1.5 The N-terminal Arm
4.1.6 The Crown Domain4.1.7 The Monomer-Monomer Interface; 4.1.8 The Noncatalytic Peripheral Binding Site; 4.2 Genetic Polymorphism and Protein Variability; 4.3 Post-translational Modifications; 4.3.1 Glycosylation Sites; 4.3.2 Ectoplasmic Localization of APs via a GPI Anchor; 4.3.3 Nonenzymatic Glycation of APs; 4.3.4 Quaternary Structure of APs; 4.3.5 Subcellular Localization of APs; 5 Enzymatic Properties; 5.1 Catalytic Inhibition; 5.1.1 Competitive and Noncompetitive Inhibitors of APs; 5.1.2 Uncompetitive Inhibition; 5.1.2.1 Mechanism of Inhibition in PLAP/GCAP 5.1.2.2 Inhibitor Binding in TNAP5.2 Allosteric Behavior; 5.3 Catalytic Efficiency of Mammalian APs; 5.4 Substrate Specificities; 5.5 APs as Members of a Superfamily of Enzymes; 6 Epitope Maps; 6.1 Epitopes in PLAP and GCAP; 6.2 Epitopes in IAP; 6.3 Discrimination Between Bone and Liver TNAP; Part II In Vivo Functions; 7 The In Vivo Role of TNAP; 7.1 Function of TNAP in Bone; 7.1.1 Hypophosphatasia; 7.1.2 Hypophosphatasia Mutations; 7.1.3 Variable Penetrance and Expressivity; 7.2 Role of TNAP in Nonskeletal Tissues; 7.3 Proposed Biological Functions of TSAPs; 7.3.1 Proposed Functions of IAP 7.3.2 Putative Functions of GCAP and PLAP8 Knockout Mouse Models; 8.1 Phenotypic Abnormalities in Akp2(-/-) mice; 8.1.1 Developmental and Skeletal Defects; 8.1.2 Dental Abnormalities in Akp2(-/-) Mice; 8.1.3 Deficient Mineralization by Akp2(-/-) Osteoblasts In Vitro; 8.1.4 Metabolic Pathways Affected in Akp2(-/-) Mice; 8.1.4.1 Neuro-physiological Abnormalities; 8.1.4.2 The Function of TNAP in Bone Mineralization; 8.1.4.3 Co-expression of TNAP and Fibrillar Collagens Restricts Calcification to Skeletal Tissues; 8.1.4.4 Other Organs Affected in Akp2(-/-) Mice 8.2 Phenotypic Abnormalities in Akp3(-/-) Mice8.3 Phenotypic Abnormalities in Akp5(-/-) Mice; Part III AP Expression in Health and Disease; 9 APs as Physiological and Disease Markers; 9.1 Clinical Usefulness of TNAP; 9.1.1 TNAP as a Marker of Bone Formation; 9.1.2 TNAP and Bone Cancer or Bone Metastasis; 9.1.3 TNAP Expression in Cholestasis; 9.1.4 TNAP in Other Conditions; 9.2 Clinical Usefulness of PLAP in Normal and Complicated Pregnancies; 9.3 IAP Expression in Relation to ABO Status, Fat Feeding and Other Pathologies; 9.4 Complexes of APs and Immunoglobulins; 9.5 Hyperphosphatasia 10 Neoplastic Expression of PLAP, GCAP, IAP (Regan, Nagao, Kasahara) and TNAP Isozymes |
Record Nr. | UNINA-9910143962103321 |
Millán José Luis | ||
Weinheim ; ; Chichester, : Wiley-VCH, c2006 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
|
Mammalian alkaline phosphatases [[electronic resource] ] : from biology to applications in medicine and biotechnology / / José Luis Millán |
Autore | Millán José Luis |
Pubbl/distr/stampa | Weinheim ; ; Chichester, : Wiley-VCH, c2006 |
Descrizione fisica | 1 online resource (340 p.) |
Disciplina | 572.7553 |
Soggetto topico |
Alkaline phosphatase
Hydrolases |
ISBN |
1-280-72272-X
9786610722723 3-527-60806-0 3-527-60747-1 |
Formato | Materiale a stampa |
Livello bibliografico | Monografia |
Lingua di pubblicazione | eng |
Nota di contenuto |
Mammalian Alkaline Phosphatases; Contents; Preface; Abbreviations; Glossary; Introduction; Part I Gene and Protein Structure; 1 Gene Structure; 1.1 Genomic Organization and Complexity; 1.2 Restriction Fragment Length Polymorphisms; 2 Developmental Expression; 2.1 The TNAP Gene; 2.2 The TSAP Genes; 3 Gene Regulation; 3.1 The TNAP Gene; 3.2 The TSAP Genes; 4 Protein Structure and Functional Domains; 4.1 The Three-dimensional Structure of PLAP; 4.1.1 Overview of the Structure; 4.1.2 The Active Site; 4.1.3 The Calcium Site; 4.1.4 The Disulfide Bonds; 4.1.5 The N-terminal Arm
4.1.6 The Crown Domain4.1.7 The Monomer-Monomer Interface; 4.1.8 The Noncatalytic Peripheral Binding Site; 4.2 Genetic Polymorphism and Protein Variability; 4.3 Post-translational Modifications; 4.3.1 Glycosylation Sites; 4.3.2 Ectoplasmic Localization of APs via a GPI Anchor; 4.3.3 Nonenzymatic Glycation of APs; 4.3.4 Quaternary Structure of APs; 4.3.5 Subcellular Localization of APs; 5 Enzymatic Properties; 5.1 Catalytic Inhibition; 5.1.1 Competitive and Noncompetitive Inhibitors of APs; 5.1.2 Uncompetitive Inhibition; 5.1.2.1 Mechanism of Inhibition in PLAP/GCAP 5.1.2.2 Inhibitor Binding in TNAP5.2 Allosteric Behavior; 5.3 Catalytic Efficiency of Mammalian APs; 5.4 Substrate Specificities; 5.5 APs as Members of a Superfamily of Enzymes; 6 Epitope Maps; 6.1 Epitopes in PLAP and GCAP; 6.2 Epitopes in IAP; 6.3 Discrimination Between Bone and Liver TNAP; Part II In Vivo Functions; 7 The In Vivo Role of TNAP; 7.1 Function of TNAP in Bone; 7.1.1 Hypophosphatasia; 7.1.2 Hypophosphatasia Mutations; 7.1.3 Variable Penetrance and Expressivity; 7.2 Role of TNAP in Nonskeletal Tissues; 7.3 Proposed Biological Functions of TSAPs; 7.3.1 Proposed Functions of IAP 7.3.2 Putative Functions of GCAP and PLAP8 Knockout Mouse Models; 8.1 Phenotypic Abnormalities in Akp2(-/-) mice; 8.1.1 Developmental and Skeletal Defects; 8.1.2 Dental Abnormalities in Akp2(-/-) Mice; 8.1.3 Deficient Mineralization by Akp2(-/-) Osteoblasts In Vitro; 8.1.4 Metabolic Pathways Affected in Akp2(-/-) Mice; 8.1.4.1 Neuro-physiological Abnormalities; 8.1.4.2 The Function of TNAP in Bone Mineralization; 8.1.4.3 Co-expression of TNAP and Fibrillar Collagens Restricts Calcification to Skeletal Tissues; 8.1.4.4 Other Organs Affected in Akp2(-/-) Mice 8.2 Phenotypic Abnormalities in Akp3(-/-) Mice8.3 Phenotypic Abnormalities in Akp5(-/-) Mice; Part III AP Expression in Health and Disease; 9 APs as Physiological and Disease Markers; 9.1 Clinical Usefulness of TNAP; 9.1.1 TNAP as a Marker of Bone Formation; 9.1.2 TNAP and Bone Cancer or Bone Metastasis; 9.1.3 TNAP Expression in Cholestasis; 9.1.4 TNAP in Other Conditions; 9.2 Clinical Usefulness of PLAP in Normal and Complicated Pregnancies; 9.3 IAP Expression in Relation to ABO Status, Fat Feeding and Other Pathologies; 9.4 Complexes of APs and Immunoglobulins; 9.5 Hyperphosphatasia 10 Neoplastic Expression of PLAP, GCAP, IAP (Regan, Nagao, Kasahara) and TNAP Isozymes |
Record Nr. | UNINA-9910830650403321 |
Millán José Luis | ||
Weinheim ; ; Chichester, : Wiley-VCH, c2006 | ||
Materiale a stampa | ||
Lo trovi qui: Univ. Federico II | ||
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