9780521411813 - sebs 53 post-transltn modifcat (society for experimental biology seminar series, no 53) von battey, n. h. (4 Ergebnisse)

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Zustand: Good. 1st Edition. Former library copy. Pages intact with minimal writing/highlighting. The binding may be loose and creased. Dust jackets/supplements are not included. Includes library markings. Stock photo provided. Product includes identifying sticker. Better World Books: Buy Books. Do Good.

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Anbieter: Ria Christie Collections, Uxbridge, Vereinigtes KönigreichRia Christie Collections
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Zustand: New. This book is about what happens to proteins once they have been synthesised within the plant cell. Editor(s): Battey, N. H.; etc.; Dickinson, H. G. (University of Oxford); Hetherington, A. M. (University of Lancaster). Series: Society for Experimental Biology Seminar Series. Num Pages: 332 pages, 70 b/w illus. 9 ta…bles. BIC Classification: PSTD. Category: (P) Professional & Vocational. Dimension: 228 x 152 x 22. Weight in Grams: 668. . 1993. 1st Edition. hardcover. . . . . Books ship from the US and Ireland.

- Hardcover
Anbieter: AHA-BUCH GmbH, Einbeck, DeutschlandAHA-BUCH GmbH
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EUR 201,39
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Buch. Zustand: Neu. Druck auf Anfrage Neuware - Printed after ordering - Post-translational modifications are now known to play a fundamental role in regulating the activity, location and function of a wide range of proteins. In plant cells work on different types of post-translational modifications has progressed largely along…independent lines. This book brings research workers together to allow an exchange of ideas, and reflects a diversity of interest whilst also revealing common ground. An introductory chapter reviewing recent progress in the field is followed by reviews of protein phosphorylation in bacteria and animals which provide a useful perspective on this subject in plants. Consideration is then given to plant protein kinases and the processes they control. Acylation and glycosylation, and their functions in protein targeting and folding are reviewed, along with the roles of glycoproteins in plant development and of ubiquitination in plant senescence.