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  • 1
    Online Resource
    Online Resource
    Collagen : Volume I: Biochemistry. (2017)
    Milton :Taylor & Francis Group,
    Details
    Keywords: Electronic books.
    Description / Table of Contents: This series was conceived to integrate current aspects of ongoing research in the collagen field. This book consists of a spectrum of papers which discuss diverse aspects such as X-ray structure, the thermodynamics and mechanism of fibrillogenesis, and the use of collagen as a biomaterial for the manufacturing of many implantable devices.
    Type of Medium: Online Resource
    Pages: 1 online resource (310 pages)
    Edition: 1st ed.
    ISBN: 9781351079242
    URL: https://ebookcentral.proquest.com/lib/geomar/detail.action?docID=5228186
    Language: English
    Note: Cover -- Title Page -- Copyright Page -- Preface -- The Editor -- Volume 1 Contributors -- Table of Contents -- Chapter 1 Molecular Structures and Functions of Collagen -- Chapter 2 Energetics and Thermodynamics of Collagen Self-Assembly -- Chapter 3 X-Ray Diffraction as A Tool For Studying Collagen Structure -- Chapter 4 Collagen Fibrillogenesis -- Chapter 5 Collagen Types: Structure, Distribution, and Functions -- Chapter 6 Cross-Linking of Collagen -- Chapter 7 Interactions between Structural Glycoproteins and Collagen -- Chapter 8 Biochemistry and Physiology of Mammalian Collagenases -- Chapter 9 Molecular Anatomy of the Vertebrate Eye: Distribution of Collagen in Ocular Tissues -- Chapter 10 Cartilage Collagens -- Chapter 11 Collagens in Nervous Tissue -- Chapter 12 Collagen in Heart Valves -- Chapter 13 Collagens of Normal and Diseased Blood Vessel Wall -- Index.
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    GEOMAR EBL
  • 2
    Online Resource
    Online Resource
    Collagen : Volume II: Biochemistry and Biomechanics. (2017)
    Milton :Taylor & Francis Group,
    Details
    Keywords: Electronic books.
    Description / Table of Contents: This series was conceived to integrate current aspects of ongoing research in the collagen field. This book consists of a spectrum of papers which discuss diverse aspects such as X-ray structure, the thermodynamics and mechanism of fibrillogenesis, and the use of collagen as a biomaterial for the manufacturing of many implantable devices.
    Type of Medium: Online Resource
    Pages: 1 online resource (312 pages)
    Edition: 1st ed.
    ISBN: 9781351079235
    URL: https://ebookcentral.proquest.com/lib/geomar/detail.action?docID=5228328
    Language: English
    Note: Cover -- Title Page -- Copyright Page -- PREFACE -- THE EDITOR -- VOLUME II: CONTRIBUTORS -- Volume II: Table of Contents -- Chapter 1 Collagen Fibrils during Development and Maturation and their Contribution to the Mechanical Attributes of Connective Tissue -- Chapter 2 Phylogenetic Aspects of Collagen Structure and Function -- Chapter 3 Histochemical Localization of Collagen and of Proteoglycans in Tissues -- Chapter 4 Structure and Organization of Macromolecules in Basement Membranes -- Chapter 5 Changes in the Morphology and Chemistry of Connective Tissues during Aging -- Chapter 6 Fibrogenic Processes during Tissue Repair -- Chapter 7 The Liver as a Bioecological System: Modifications during Regeneration and Repair -- Chapter 8 Method of Treatment of Fibrotic Lesions by Topical Administration of Lathyrogenic Drugs -- Chapter 9 Hierarchical Structure of Collagen and its Relationship to the Physical Properties of Tendon -- Chapter 10 Contributions of Elastin and Collagen Organization to Passive Mechanical Properties of Arterial Tissue -- Chapter 11 Current Advances on the Study of the Biomechanical Properties of Tendons and Ligaments -- Chapter 12 The Collagen Framework of Articular Cartilage: Its Profound Influence on Normal and Abnormal Load-Bearing Function -- Chapter 13 Viscoelastic Properties of Articular Cartilage and Meniscus -- Index.
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    GEOMAR EBL
  • 3
    Electronic Resource
    Electronic Resource
    The Cross-Linking and Structure Modification of the Collagen Matrix in the Design of Cardiovascular Prosthesis (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of cardiac surgery 3 (1988), S. 0 
    Details
    ISSN: 1540-8191
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract Glutaraldehyde cross-linking of native or reconstituted collagen fibrils and tissues rich in collagen significantly reduces biodegradation. Other aldehydes are less efficient than glutaraldehyde in generating chemically, biologically, and thermally stable cross-links. Implants of collagenous materials cross-linked with glutaraldehyde are subject long-term to calcification, biodegradation, and low-grade immune reactions. We have attempted to overcome these problems by enhancing cross-linking through (a) bridging of activated carboxyl groups with diamines and (b) using glutaraldehyde to cross-link the ε–NH2 groups in collagen and the unreacted amines introduced by aliphatic dismines. This cross-linking reduces tissue degradation and nearly eliminates humoral antibody induction. Covalent binding of diphosphonates, specifically 3-amino-1-hydroxypopane-1, 1-diphosphonic acid (3-APD), and to a lesser extent chondroitin sulfate to collagen or to the cross-ling-enhanced collagen network reduces its potential for calcification. Platelet aggregation also is reduced by glutaraldehyde cross-linking and nearly eliminated by the covalent binding of chondroitin sulfate to collagen. The cytotoxicity of residual glutaraldehyde can be minimized by chemical neutralization and thorough rough rinsing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1540-8191.1988.tb00446.x
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    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    The progeny of rabbit articular chondrocytes synthesize collagen types I and III and type I trimer, but not type II. Verifications by cyanogen bromide peptide analysis (1977)
    s.l. : American Chemical Society
    Biochemistry 16 (1977), S. 865-872 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00624a009
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    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    Synthesis of aldehydes and their interactions during the in vitro aging of collagen (1971)
    s.l. : American Chemical Society
    Biochemistry 10 (1971), S. 2337-2342 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00788a025
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    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Characterization of the aldehydes present on the cyanogen bromide peptides from mature rat skin collagen (1971)
    s.l. : American Chemical Society
    Biochemistry 10 (1971), S. 1640-1647 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00785a022
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    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Properties of a collagen molecule containing three identical components extracted from bovine articular cartilage (1971)
    s.l. : American Chemical Society
    Biochemistry 10 (1971), S. 3905-3911 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00797a017
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    Paper (German National Licenses)
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  • 8
    Electronic Resource
    Electronic Resource
    Effects of non-steroidal anti-inflammatory drugs on demineralized bone-induced bone formation (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 27 (1992), S. 0 
    Details
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The inhibitory effect of some non-steroidal anti-inflammatory drugs (NSAIDs) on bone resorption is well documented. To explore the effect of NSAIDs on bone formation, we investigated the time course and dose/response characteristics of treatment with various non-steroidal anti-inflammatory drugs (NSAIDs) on ectopic bone formation induced by demineralized bone matrix (DBM) in the rat model. Using biochemical assays, both inhibitory and stimulatory effects on bone formation were found in rats treated with NSAIDs prior to DBM implantation depending on the type and amount of drug administered. There appears to be an enhancement of bone formation for acetaminophen (50 mg/kg), acetylsalicylic acid (50 mg/kg), and ibuprofen (50 mg/kg). Indomethacin (4 mg/kg) and piroxicam (4 mg/kg) had inhibitory effects. Flurbiprofen, on the other hand, did not appear to affect bone formation significantly. In contrast, there was no effect of NSAIDs on bone formation in rats treated with the drugs after implantation of the DBM. It appears that the time course of the drug administration is critical, suggesting that early events in bone formation may be modulated by arachidonic acid metabolites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0765.1992.tb02082.x
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    Paper (German National Licenses)
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  • 9
    Electronic Resource
    Electronic Resource
    Metabolic pathways and control mechanisms involved in the biosynthesis and turnover of collagen in normal and pathological connective tissues (1973)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of oral pathology & medicine 2 (1973), S. 0 
    Details
    ISSN: 1600-0714
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract. The biosynthesis of collagen molecules and their subsequent assembly into fibers involves a complex series of post-ribosomal modifications which occur intracellularly and extracellularly. Some of these subtle alterations lead to the formation of intramolecular and intermolecular cross-links, whereas others seem to dictate the 3-dimensional organization of the collagen fibers. For their normal function, tissues require an optimum amount of collagen and proteoglycans. Such a balance coupled with specificity built into collagen seems to assure adequate function. Changes in the rates of synthesis, turnover or transcription of genetic information which affect the type of collagen deposited at a particular site may lead lo a stale of disease.It is hoped that our current understanding of such mechanisms, coupled with our ability to inhibit or accelerate some of these processes, will allow us lo effectively control the metabolism of connective tissues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1600-0714.1973.tb01682.x
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    Paper (German National Licenses)
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  • 10
    Electronic Resource
    Electronic Resource
    A 210,000-Dalton Pepsin-resistant Fragment of Type IX Collagen (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 460 (1985), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1985.tb51230.x
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    Paper (German National Licenses)
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