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Titlebook: Biology of Invertebrate and Lower Vertebrate Collagens; A. Bairati,R. Garrone Book 1985 Plenum Press, New York 1985 biology.invertebrates.

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发表于 2025-3-21 16:54:14 | 显示全部楼层 |阅读模式
期刊全称Biology of Invertebrate and Lower Vertebrate Collagens
影响因子2023A. Bairati,R. Garrone
视频video
学科分类NATO Science Series A:
图书封面Titlebook: Biology of Invertebrate and Lower Vertebrate Collagens;  A. Bairati,R. Garrone Book 1985 Plenum Press, New York 1985 biology.invertebrates.
影响因子Knowledge in the field of the biology of the extracellular matrix, and in particular of collagen, has made considerable progress over the last ten years, especially in mammals, birds and ln man with respect to very important applied medical aspects. Basic knowledge in the animal kingdom overall has increased more slowly and haphazardly. We, therefore, considered it useful to organize a meeting specifically devoted to the study of the invertebrate and lower vertebrate collagens. The NATO Scientific Division financed an Advanced Research Workshop aimed at bringing together experts qualified in collagen biology (with morphological, biochemical and genetic specialization) with researchers who are currently studying collagenous tissues of invertebrates and lower vertebrates. The Medical-Biology Committee of the CNR-Rome and the University of Milan also supplied interest and support for the organization of this Meeting. The format of the workshop consisted in: 1) main lectures on the most recent aspects of collagen biology; 2) minireviews on the current knowledge of collagenous tissues in the various invertebrate phyla and in fish; 3) contributed papers on particular aspects of research
Pindex Book 1985
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发表于 2025-3-21 23:56:35 | 显示全部楼层
https://doi.org/10.1007/978-1-4684-7636-1biology; invertebrates; mammals; paper; spectroscopy; tissue; vertebrates
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978-1-4684-7638-5Plenum Press, New York 1985
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,Leukämien im Kindesalter — Allgemeines,Three clear features of the structure of collagen fibrils are recognised and probably not seriously disputed:
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Structure of Collagen FibrilsThree clear features of the structure of collagen fibrils are recognised and probably not seriously disputed:
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,Thrombozytenfunktionsstörungen,or animal evolution. It is characterized by a precise wide angle X-ray diffraction pattern (2.8, 4 and 10 Å meridional spacings, and an approximately 11 Å equatorial reflection), and by glycine accounting for 1/3 of the aminoacid residues. The electron microscopical picture of this protein being qui
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Thomas Kühne,Alexandra Schifferlimolecular organizations whose formation is controlled by different collagen types. The type specific scaffolds of collagen, in which other extracellular matrix components are embedded, are responsible for the structure as well as for the biochemical properties of connective tissue. At present, three
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