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Titlebook: Lipid and Protein Traffic; Pathways and Molecul Jos A. F. Op den Kamp Conference proceedings 1998 Springer-Verlag Berlin Heidelberg 1998 Ch

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书目名称Lipid and Protein Traffic
副标题Pathways and Molecul
编辑Jos A. F. Op den Kamp
视频video
概述A complete overview of recent progress in the field
丛书名称Nato ASI Subseries H:
图书封面Titlebook: Lipid and Protein Traffic; Pathways and Molecul Jos A. F. Op den Kamp Conference proceedings 1998 Springer-Verlag Berlin Heidelberg 1998 Ch
描述The meeting on "Molecular Mechanisms of Lipid and Protein Traffic", sponsored by NATO Scientific Affairs Division as an Advanced Study Institute and by the Federation of European Biochemical Societies as a Lecture Course was held in Cargese, France, in June 1997. The program included introductory lectures, specialized up-to-date contributions, poster sessions, tutorials and workshops. Emphasis was laid on the new developments in the field of membrane dynamics, in particular on the insertion and translocation of proteins; on intracellular protein, lipid and membrane traffic and sorting and on the mutual interactions between the various events occurring during membrane biogenesis. Mitochondrial biogenesis, chloroplast assembly and the insertion of proteins into peroxisomes were highlighted. Much progress in these research areas has been made in recent years and the ASI provided an excellent opportunity to illustrate this progress in comparison with previous meetings on a similar topic. Not only graduate students and postdocs took advantage from this program but also experienced scientists were given the opportunity to obtain a complete overview of recent progress and the remodeling o
出版日期Conference proceedings 1998
关键词Chloroplast; Lipid; Oxidation; Peroxisom; bacteria; biomembrane; escherichia coli; glycoprotein; membrane; mi
版次1
doihttps://doi.org/10.1007/978-3-642-51463-0
isbn_softcover978-3-642-51465-4
isbn_ebook978-3-642-51463-0Series ISSN 1010-8793
issn_series 1010-8793
copyrightSpringer-Verlag Berlin Heidelberg 1998
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Do the Type I Signal Peptidases of , Compete for Binding and Cleavage of Secretory Precursor Proteiing of other precursors was improved. The latter observation indicates that the presence of SipS can interfere with efficient processing of certain precursor proteins, which raises the question whether the type I signal peptidases of . compete for binding and cleavage of secretory precursor proteins.
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Studies on N-Glycosylation of Proteins in the Endoplasmic Reticulum,cases oligosaccharide chains of these proteins are essential because if they are absent or altered, several processes can be affected. These processes are: (1) protein stability; (2) subcellular localization; (3) normal folding; or (4) protein secretion. The diverse biological roles for N-linked oligosaccharides have been reviewed (Varki, 1993).
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1010-8793 entific Affairs Division as an Advanced Study Institute and by the Federation of European Biochemical Societies as a Lecture Course was held in Cargese, France, in June 1997. The program included introductory lectures, specialized up-to-date contributions, poster sessions, tutorials and workshops. E
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Protein Targeting into and within Chloroplasts,ly, the information presented has been obtained with chloroplasts, but is assumed to apply to all plastid types. Readers desiring more detailed information are referred to a number of excellent recent reviews on this topic (Cline and Henry, 1996; Kouranov and Schnell, 1996; Hauke and Schatz, 1997).
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Import, Folding and Degradation of Proteins by Mitochondria,a recognize the proteins they must import? How do they transport them across one or even both of their membranes? And how do they degrade them? The answers to these questions bear not only on the mechanism of mitochondrial biogenesis, but also tell on the mechanism(s) by which proteins are transported across biological membranes (2).
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https://doi.org/10.1007/978-3-642-51463-0Chloroplast; Lipid; Oxidation; Peroxisom; bacteria; biomembrane; escherichia coli; glycoprotein; membrane; mi
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Nato ASI Subseries H:http://image.papertrans.cn/l/image/586865.jpg
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