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Hyaluronic acid : preparation, properties, application in biology and medicine / / Mikhail A. Selyanin, Petr Ya. Boykov and Vladimir N. Khabarov ; translated from the Russian version by scientific editor Felix Polyak
| Hyaluronic acid : preparation, properties, application in biology and medicine / / Mikhail A. Selyanin, Petr Ya. Boykov and Vladimir N. Khabarov ; translated from the Russian version by scientific editor Felix Polyak |
| Autore | Selyanin M. A (Michael A.) |
| Pubbl/distr/stampa | Chichester, England : , : Wiley, , 2015 |
| Descrizione fisica | 1 online resource (215 p.) |
| Disciplina | 612.015782 |
| Soggetto topico |
Hyaluronic acid
Organic acids |
| ISBN |
1-118-69595-X
1-118-69593-3 1-118-69592-5 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
Title Page; Copyright Page; Contents; Foreword; Introduction; Chapter 1 The History of Hyaluronic Acid Discovery, Foundational Research and Initial Use; 1.1 Discovery; 1.2 Foundational Research; 1.3 Initial Medical Applications; 1.4 Sources of Hyaluronan; 1.5 Current Medical Study and Use; 1.6 Impact and Future Directions; References; Chapter 2 The Biological Role of Hyaluronic Acid; 2.1 Hyaluronic Acid Phylogenesis; 2.1.1 Polysaccharide Structure and the Problems of Phylogenesis; 2.1.2 Physico-Chemical and Functional Differences of Polysaccharides
2.1.3 Biochemical Features of Hyaluronic Acid and Other Glycosaminoglycans2.2 Functions of Hyaluronan in Human Ontogenesis; 2.2.1 Role of Hyaluronic Acid in Fertilization; 2.2.2 Hyaluronan and Other Glucosaminoglycans in Cell Division, Migration and Differentiation; 2.2.3 Hyaluronic Acid and Sulfated Glycosaminoglycans in Maintaining a Differentiated Status of Cells; 2.2.4 Hyaluronan and Induction of Cellular Cycles for Differentiated Cells; 2.2.5 The Source of Hyaluronic Acid's Functional Properties and the Dynamics of its Synthesis and Degradation 2.2.6 The Rules of Biopolymer Functional Cleavage2.3 Hyaluronan Signalling Systems; 2.4 Hyaluronan Functions in the Extracellular Matrix; 2.4.1 Extracellular Space; 2.4.2 Composition and Functioning of the Extracellular Matrix; 2.4.3 The Role of Hyaluronan in Transportation of Substances through the Extracellular Matrix: Diffusion, Osmosis, Electro-Osmosis and Vesicular Transportation; 2.4.4 Hyaluronan in the Extracellular Matrix of Different Connective Tissues; References; Chapter 3 Methods of Hyaluronic Acid Production; 3.1 Hyaluronan Sources and Extraction 3.1.1 Hyaluronan Production from Animal Sources: General Methods3.1.2 Hyaluronan Purification; 3.1.3 The Chemical Production of Hyaluronan from Chicken Combs; 3.1.4 HA Production for Ophthalmology; 3.2 Bacterial Methods of Hyaluronic Acid Production; 3.3 Hyaluronan Destruction during Production, Storage and Sterilization; 3.4 Enzymatic Destruction of Hyaluronan; 3.4.1 Hyaluronidase Classification; 3.4.2 Properties and Functions of Hyaluronidases; 3.5 Non-Enzymatic Destruction of Hyaluronan; 3.5.1 Acid-Base Hydrolysis of Hyaluronan; 3.5.2 Oxidation-Reduction Depolymerization of Hyaluronan 3.6 Quality of Hyaluronan Commercial Products of Animal and Bacterial OriginReferences; Chapter 4 Molecular and Supramolecular Structure of Hyaluronic Acid; 4.1 Primary Structure of Hyaluronic Acid; 4.2 Structure of Hyaluronan in Solution; 4.3 Rheological Properties of Hyaluronic Acid; References; Chapter 5 Chemical Modifications, Solid Phase, Radio-Chemical and Enzymatic Transformations of Hyaluronic Acid; 5.1 Main Characteristics of Cross-Linked Hydrogels; 5.2 Methods of Hyaluronic Acid Cross-Linking; 5.2.1 Cross-Linking with Carbodiimides; 5.2.2 Cross-Linking with Aldehydes 5.2.3 Cross-Linking with Divinylsulfone |
| Record Nr. | UNINA-9910132397603321 |
Selyanin M. A (Michael A.)
|
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| Chichester, England : , : Wiley, , 2015 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
The nature and origin of amyloid fibrils [[electronic resource] /] / [editors, Gregory R. Bock (Organizer) and Jamie A. Goode]
| The nature and origin of amyloid fibrils [[electronic resource] /] / [editors, Gregory R. Bock (Organizer) and Jamie A. Goode] |
| Pubbl/distr/stampa | Chichester ; ; New York, : Wiley, 1996 |
| Descrizione fisica | 1 online resource (268 p.) |
| Disciplina |
612.015782
612.8 612.8042 |
| Altri autori (Persone) |
BockeGregory
GoodeJamie |
| Collana | Ciba Foundation symposium |
| Soggetto topico |
Amyloid
Amyloid beta-protein Amyloidosis |
| Soggetto genere / forma | Electronic books. |
| ISBN |
1-282-34797-7
9786612347979 0-470-51492-2 0-470-51493-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
THE NATURE AND ORIGIN OF AMYLOID FIBRILS; Contents; Participants; Preface; Introduction; In memoriam; A molecular model of the amyloid fibril; Refined fibril structures: the hydrophobic core in Alzheimer's amyloid b-protein and prion as revealed by X-ray diffraction; General discussion I; Modulating conformational factors in transthyretin amyloid; Proteoglycans and amyloid fibrillogenesis; Molecular mechanisms of fibrillogenesis and the protective role of amyloid P component: two possible avenues for therapy; General discussion II; Metabolism of amyloid proteins
Alzheimer's disease: genesis of amyloidApolipoprotein E and amyloidogenesis; Interaction of transthyretin with amyloid B-protein: binding and inhibition of amyloid formation; General discussion III; B-amyloid precursor protein and early-o nset Alzheimer's disease; Prion protein amyloid: separation of scrapie infectivity from PrP polymers; General discussion IV; Ageing and amyloid fibrillogenesis: lessons from apolipoprotein Al, transthyretin and islet amyloid polypeptide; General discussion V FAP mutations destabilize transthyretin facilitating conformational changes required for amyloid formationIndex of contributors; Subject index |
| Record Nr. | UNINA-9910144740203321 |
| Chichester ; ; New York, : Wiley, 1996 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||
The nature and origin of amyloid fibrils [[electronic resource] /] / [editors, Gregory R. Bock (Organizer) and Jamie A. Goode]
| The nature and origin of amyloid fibrils [[electronic resource] /] / [editors, Gregory R. Bock (Organizer) and Jamie A. Goode] |
| Pubbl/distr/stampa | Chichester ; ; New York, : Wiley, 1996 |
| Descrizione fisica | 1 online resource (268 p.) |
| Disciplina |
612.015782
612.8 612.8042 |
| Altri autori (Persone) |
BockeGregory
GoodeJamie |
| Collana | Ciba Foundation symposium |
| Soggetto topico |
Amyloid
Amyloid beta-protein Amyloidosis |
| ISBN |
1-282-34797-7
9786612347979 0-470-51492-2 0-470-51493-0 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto |
THE NATURE AND ORIGIN OF AMYLOID FIBRILS; Contents; Participants; Preface; Introduction; In memoriam; A molecular model of the amyloid fibril; Refined fibril structures: the hydrophobic core in Alzheimer's amyloid b-protein and prion as revealed by X-ray diffraction; General discussion I; Modulating conformational factors in transthyretin amyloid; Proteoglycans and amyloid fibrillogenesis; Molecular mechanisms of fibrillogenesis and the protective role of amyloid P component: two possible avenues for therapy; General discussion II; Metabolism of amyloid proteins
Alzheimer's disease: genesis of amyloidApolipoprotein E and amyloidogenesis; Interaction of transthyretin with amyloid B-protein: binding and inhibition of amyloid formation; General discussion III; B-amyloid precursor protein and early-o nset Alzheimer's disease; Prion protein amyloid: separation of scrapie infectivity from PrP polymers; General discussion IV; Ageing and amyloid fibrillogenesis: lessons from apolipoprotein Al, transthyretin and islet amyloid polypeptide; General discussion V FAP mutations destabilize transthyretin facilitating conformational changes required for amyloid formationIndex of contributors; Subject index |
| Record Nr. | UNINA-9910830473703321 |
| Chichester ; ; New York, : Wiley, 1996 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
| ||