Post-translational modifications in plants:
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 researc...
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Weitere Verfasser: | , , |
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Format: | Elektronisch E-Book |
Sprache: | English |
Veröffentlicht: |
Cambridge
Cambridge University Press
1993
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Schriftenreihe: | Society for Experimental Biology seminar series
53 |
Schlagworte: | |
Online-Zugang: | BSB01 FHN01 Volltext |
Zusammenfassung: | 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 |
Beschreibung: | Title from publisher's bibliographic system (viewed on 05 Oct 2015) |
Beschreibung: | 1 online resource (xx, 310 pages) |
ISBN: | 9780511600401 |
DOI: | 10.1017/CBO9780511600401 |
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505 | 8 | |a Some 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 | 8 | |a Distribution 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 | 8 | |a Detection, 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 | |a 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 | ||
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Datensatz im Suchindex
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any_adam_object | |
author2 | Battey, N. H. Dickinson, Hugh G. Hetherington, A. M. |
author2_role | edt edt edt |
author2_variant | n h b nh nhb h g d hg hgd a m h am amh |
author_facet | Battey, N. H. Dickinson, Hugh G. Hetherington, A. M. |
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contents | Some 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 Distribution 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 Detection, 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 |
ctrlnum | (ZDB-20-CBO)CR9780511600401 (OCoLC)849959729 (DE-599)BVBBV043941439 |
dewey-full | 581.19/296 |
dewey-hundreds | 500 - Natural sciences and mathematics |
dewey-ones | 581 - Specific topics in natural history of plants |
dewey-raw | 581.19/296 |
dewey-search | 581.19/296 |
dewey-sort | 3581.19 3296 |
dewey-tens | 580 - Plants |
discipline | Biologie |
doi_str_mv | 10.1017/CBO9780511600401 |
format | Electronic eBook |
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isbn | 9780511600401 |
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spelling | Post-translational modifications in plants edited by N.H. Battey, H.G. Dickinson, A.M. Hetherington Cambridge Cambridge University Press 1993 1 online resource (xx, 310 pages) txt rdacontent c rdamedia cr rdacarrier Society for Experimental Biology seminar series 53 Title from publisher's bibliographic system (viewed on 05 Oct 2015) Some 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 Distribution 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 Detection, 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 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 Post-translational modification / Congresses Plant proteins / Synthesis / Congresses Proteine (DE-588)4076388-2 gnd rswk-swf Pflanzen (DE-588)4045539-7 gnd rswk-swf Posttranslationale Änderung (DE-588)4204069-3 gnd rswk-swf (DE-588)1071861417 Konferenzschrift gnd-content Posttranslationale Änderung (DE-588)4204069-3 s Proteine (DE-588)4076388-2 s Pflanzen (DE-588)4045539-7 s 1\p DE-604 Battey, N. H. edt Dickinson, Hugh G. edt Hetherington, A. M. edt Erscheint auch als Druckausgabe 978-0-521-41181-3 https://doi.org/10.1017/CBO9780511600401 Verlag URL des Erstveröffentlichers Volltext 1\p cgwrk 20201028 DE-101 https://d-nb.info/provenance/plan#cgwrk |
spellingShingle | Post-translational modifications in plants Some 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 Distribution 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 Detection, 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 Post-translational modification / Congresses Plant proteins / Synthesis / Congresses Proteine (DE-588)4076388-2 gnd Pflanzen (DE-588)4045539-7 gnd Posttranslationale Änderung (DE-588)4204069-3 gnd |
subject_GND | (DE-588)4076388-2 (DE-588)4045539-7 (DE-588)4204069-3 (DE-588)1071861417 |
title | Post-translational modifications in plants |
title_auth | Post-translational modifications in plants |
title_exact_search | Post-translational modifications in plants |
title_full | Post-translational modifications in plants edited by N.H. Battey, H.G. Dickinson, A.M. Hetherington |
title_fullStr | Post-translational modifications in plants edited by N.H. Battey, H.G. Dickinson, A.M. Hetherington |
title_full_unstemmed | Post-translational modifications in plants edited by N.H. Battey, H.G. Dickinson, A.M. Hetherington |
title_short | Post-translational modifications in plants |
title_sort | post translational modifications in plants |
topic | Post-translational modification / Congresses Plant proteins / Synthesis / Congresses Proteine (DE-588)4076388-2 gnd Pflanzen (DE-588)4045539-7 gnd Posttranslationale Änderung (DE-588)4204069-3 gnd |
topic_facet | Post-translational modification / Congresses Plant proteins / Synthesis / Congresses Proteine Pflanzen Posttranslationale Änderung Konferenzschrift |
url | https://doi.org/10.1017/CBO9780511600401 |
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