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Edité par LAP LAMBERT Academic Publishing, 2015
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Edité par LAP LAMBERT Academic Publishing, 2015
ISBN 10 : 3659685046 ISBN 13 : 9783659685040
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Ajouter au panierTaschenbuch. Etat : Neu. Properties of p20, a yeast eIF4E¿binding protein | Regulation of eukaryotic translation initiation | Daniela Ross | Taschenbuch | 84 S. | Englisch | 2015 | LAP LAMBERT Academic Publishing | EAN 9783659685040 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu.
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Edité par Carl Hanser Verlag GmbH & Co. KG, 2018
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Edité par LAP LAMBERT Academic Publishing Apr 2015, 2015
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Ajouter au panierTaschenbuch. Etat : Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -The yeast phosphoprotein p20 is a modulator of translation and shares with mammalian 4EBPs a conserved eIF4E-binding motif. In this book, six more phosphorylation sites have been found on p20 by means of proteomics and a non-phosphorylatable p20 isoform has been established. Moreover, a phenotype of p20 is demonstrated while differences between derivates of two genetically diverse laboratory yeast strains became visible. Investigation of p20 mutants under several stress conditions leads to the conclusion that mutations in p20 affecting its eIF4E binding result in p20 degradation and to a phenotype in a filamentous strain. Furthermore the influence of non-phosphorylatable or several other p20 mutants on translation of reporter mRNAs as well as p20 s effect on localisation of eIF4E are shown in this work. 84 pp. Englisch.
Langue: anglais
Edité par LAP LAMBERT Academic Publishing, 2015
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Ajouter au panierEtat : New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. Autor/Autorin: Ross DanielaBorn in Berlin/Germany, I have completed my studies of Biotechnology at the Beuth Hochschule first with a Diploma (purification of whey proteins in New Zealand) and additionally with a Master of Science (Proteomics of All.
Langue: anglais
Edité par LAP LAMBERT Academic Publishing Apr 2015, 2015
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Ajouter au panierTaschenbuch. Etat : Neu. This item is printed on demand - Print on Demand Titel. Neuware -The yeast phosphoprotein p20 is a modulator of translation and shares with mammalian 4EBPs a conserved eIF4E-binding motif. In this book, six more phosphorylation sites have been found on p20 by means of proteomics and a non-phosphorylatable p20 isoform has been established. Moreover, a phenotype of p20 is demonstrated while differences between derivates of two genetically diverse laboratory yeast strains became visible. Investigation of p20 mutants under several stress conditions leads to the conclusion that mutations in p20 affecting its eIF4E binding result in p20 degradation and to a phenotype in a filamentous strain. Furthermore the influence of non-phosphorylatable or several other p20 mutants on translation of reporter mRNAs as well as p20¿s effect on localisation of eIF4E are shown in this work.VDM Verlag, Dudweiler Landstraße 99, 66123 Saarbrücken 84 pp. Englisch.
Langue: anglais
Edité par LAP LAMBERT Academic Publishing, 2015
ISBN 10 : 3659685046 ISBN 13 : 9783659685040
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Ajouter au panierTaschenbuch. Etat : Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - The yeast phosphoprotein p20 is a modulator of translation and shares with mammalian 4EBPs a conserved eIF4E-binding motif. In this book, six more phosphorylation sites have been found on p20 by means of proteomics and a non-phosphorylatable p20 isoform has been established. Moreover, a phenotype of p20 is demonstrated while differences between derivates of two genetically diverse laboratory yeast strains became visible. Investigation of p20 mutants under several stress conditions leads to the conclusion that mutations in p20 affecting its eIF4E binding result in p20 degradation and to a phenotype in a filamentous strain. Furthermore the influence of non-phosphorylatable or several other p20 mutants on translation of reporter mRNAs as well as p20 s effect on localisation of eIF4E are shown in this work.