000			04407nam a22004098i 4500
001			CR9780511600401
003			UkCbUP
005			20200124160230.0
006			m|||||o||d||||||||
007			cr||||||||||||
008			090722s1993||||enk o ||1 0|eng|d
020			_a9780511600401 (ebook)
020			_z9780521411813 (hardback)
040			_aUkCbUP _beng _erda _cUkCbUP
050	0	0	_aQK898.P8 _bP67 1993
082	0	0	_a581.19/296 _220
245	0	0	_aPost-translational modifications in plants / _cedited by N.H. Battey, H.G. Dickinson, A.M. Hetherington.
264		1	_aCambridge : _bCambridge University Press, _c1993.
300			_a1 online resource (xx, 310 pages) : _bdigital, PDF file(s).
336			_atext _btxt _2rdacontent
337			_acomputer _bc _2rdamedia
338			_aonline resource _bcr _2rdacarrier
490	1		_aSociety for Experimental Biology seminar series ; _v53
500			_aTitle from publisher's bibliographic system (viewed on 05 Oct 2015).
505	0		_aSome roles of post-translational modifications in plants / N.H. Battey, H.G. Dickinson and A.M. Hetherington -- Signal transduction and protein phosphorylation in bacteria / R.A. Dixon -- Roles of protein phosphorylation in animal cells / D.G. Hardie -- The significance of post-translational modification of proteins by phosphorylation in the regulation of plant development and metabolism / K.M. Fallon and A.J. Trewavas -- Post-translational modification of chloroplast proteins and the regulation of protein turnover / A.K. Mattoo [and others] -- Purification of a small phosphoprotein from chloroplasts and characterisation of its phosphoryl group / J. Soll -- Use of synthetic peptides to study G proteins and protein kinases within plant cells / I.R. White [and others] -- Activation of membrane-associated protein kinase by lipids, its substrates, and its function in signal transduction / G.F.E. Scherer, A. Führ and M. Schütte.
505	0		_aDistribution and function of Ca2+-dependent, calmodulin-independent protein kinases / N.H. Battey, S.M. Ritchie and H.D. Blackbourn -- Phosphorylation of the plasma membrane proton pump / M.R. Sussman -- The regulation of phosphoenolpyruvate carboxylase by reversible phosphorylation / H.G. Nimmo -- Protein phosphorylation and circadian rhythms / L. Rensing [and others] -- Control of translation by phosphorylation of mRNP proteins in Fucus and Xenopus / A.D. Shirras [and others] -- Regulation of plant metabolism by reversible protein (serine/threonine) phosphorylation / R.W. MacKintosh and C. MacKintosh.
505	0		_aDetection, biosynthesis and some functions of glycans N-linked to plant secreted proteins / L. Faye [and others] -- Biosynthesis, intracellular transport and processing of ricin / J.M. Lord and L.M. Roberts -- Post-translational processing of concanavalin A / D.J. Bowles -- The role of cell surface glycoproteins in differentiation and morphogenesis / J.P. Knox -- Ubiquitination of proteins during floral development and senescence / S.E. Courtney, C.C. Rider and A.D. Stead.
520			_aPost-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.
650		0	_aPost-translational modification _vCongresses.
650		0	_aPlant proteins _xSynthesis _vCongresses.
700	1		_aBattey, N. H., _eeditor.
700	1		_aDickinson, Hugh G., _eeditor.
700	1		_aHetherington, A. M., _eeditor.
776	0	8	_iPrint version: _z9780521411813
830		0	_aSeminar series (Society for Experimental Biology (Great Britain)) ; _v53.
856	4	0	_uhttps://doi.org/10.1017/CBO9780511600401
999			_c517577 _d517575