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Titlebook: Chaperones; Ineke Braakman Book 20061st edition Springer-Verlag Berlin Heidelberg 2006 Chaperone.Organelle.Peroxisom.biology.biosynthesis.

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書(shū)目名稱Chaperones
編輯Ineke Braakman
視頻videohttp://file.papertrans.cn/224/223940/223940.mp4
概述Uniquely combines the basics of the subject area with the latest results.An excellent starting point for novices as well as a source of substantial information for experts.Includes supplementary mater
叢書(shū)名稱Topics in Current Genetics
圖書(shū)封面Titlebook: Chaperones;  Ineke Braakman Book 20061st edition Springer-Verlag Berlin Heidelberg 2006 Chaperone.Organelle.Peroxisom.biology.biosynthesis.
描述.Molecular chaperones interact with virtually every newly synthesized protein. Their role is not limited to this, as an increasing number of protein-protein interactions are found to be mediated by molecular chaperones. They reside in large complexes, in every cellular compartment, and to some extent even outside cells. These proteins are of interest to a large number of scientists, not only to those interested in protein biosynthesis, but also in relation to protein transport, organelle biogenesis, and cell stress. ..Whereas excellent reviews on molecular chaperones are published, they often focus on the latest results without reiterating the basics. The goal of this volume was to assemble a collection of reviews on molecular chaperones that would be both timely and basic, which would make them an excellent entrance for novices into the field and suitable for teaching purposes..
出版日期Book 20061st edition
關(guān)鍵詞Chaperone; Organelle; Peroxisom; biology; biosynthesis; cell; mitochondria; molecular biology; prokaryotes; p
版次1
doihttps://doi.org/10.1007/b100697
isbn_softcover978-3-642-06902-4
isbn_ebook978-3-540-32581-9Series ISSN 1610-2096 Series E-ISSN 1610-6970
issn_series 1610-2096
copyrightSpringer-Verlag Berlin Heidelberg 2006
The information of publication is updating

書(shū)目名稱Chaperones影響因子(影響力)




書(shū)目名稱Chaperones影響因子(影響力)學(xué)科排名




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Folding of newly synthesised proteins in the endoplasmic reticulum,n of all the proteins that the cell secretes, or needs to express at the cell surface or within the secretory pathway itself. The type of proteins that pass through the ER is very varied, ranging from small, secreted peptide hormones, to large cell surface receptors. To the uninitiated, protein fold
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Chaperone proteins and peroxisomal protein import,involved in the formation and maintenance of peroxisomes has been discovered, and can be categorised into genes important for protein import into the peroxisome and genes involved in the maintenance of the organelles’ size and abundance. Thorough cell biological and biochemical studies revealed grea
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The Hsp60 chaperonins from prokaryotes and eukaryotes,roup I chaperonins from eubacteria and their endosymbiotic counterparts in eukaryotic cells, and the Group II chaperonins from archaea and the eukaryotic cytosol. While the two classes have some similarity to each other in structural and functional characteristics, they also have a number of importa
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Chaperones978-3-540-32581-9Series ISSN 1610-2096 Series E-ISSN 1610-6970
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