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Alessandro Occhialini: Receptor Membrane Ring-H2 (RMR) Proteins in Plants : Investigation of AtRMR localization and interaction in plant secretory pathway - Livro de bolso
[EAN: 9783659391866], Neubuch, [PU: LAP LAMBERT Academic Publishing], nach der Bestellung gedruckt Neuware -In plant cells it has been demonstrated that many vacuolar proteins are sorted … mais…
[EAN: 9783659391866], Neubuch, [PU: LAP LAMBERT Academic Publishing], nach der Bestellung gedruckt Neuware -In plant cells it has been demonstrated that many vacuolar proteins are sorted to their final destination by cargo receptors. These receptors are transmembrane proteins able to bind soluble vacuolar proteins determining their transport to vacuoles. This study is focused on AtRMR, a family of putative receptors composed of six genes in Arabidopsis thaliana. These experiments showed that AtRMR1 localizes in the trans-Golgi network while AtRMR2 localizes in the endoplasmic reticulum. This different localization is due to a putative localization signal present in the AtRMR1 linker. Also this study demonstrated that AtRMR1 can make homodimers and can interact with AtRMR2 making heterodimers. These dimers localize in the trans-Golgi network. Finally the transmembrane and the linker are probably the domains involved in protein-protein interaction. This book provided new information about the physiology of AtRMR traffic and dimerization, improving the comprehension of the mechanisms and the localization signals involved in protein sorting to vacuoles. Therefore this book should be useful for plant biologists or anyone else is interested in protein trafficking in plant secretory pathway. 308 pp. Englisch, Books<
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Paperback, [PU: LAP Lambert Academic Publishing], In plant cells it has been demonstrated that many vacuolar proteins are sorted to their final destination by cargo receptors. These recep… mais…
Paperback, [PU: LAP Lambert Academic Publishing], In plant cells it has been demonstrated that many vacuolar proteins are sorted to their final destination by cargo receptors. These receptors are transmembrane proteins able to bind soluble vacuolar proteins determining their transport to vacuoles. This study is focused on AtRMR, a family of putative receptors composed of six genes in Arabidopsis thaliana. These experiments showed that AtRMR1 localizes in the trans-Golgi network while AtRMR2 localizes in the endoplasmic reticulum. This different localization is due to a putative localization signal present in the AtRMR1 linker. Also this study demonstrated that AtRMR1 can make homodimers and can interact with AtRMR2 making heterodimers. These dimers localize in the trans-Golgi network. Finally the transmembrane and the linker are probably the domains involved in protein-protein interaction. This book provided new information about the physiology of AtRMR traffic and dimerization, improving the comprehension of the mechanisms and the localization signals involved in protein sorting to vacuoles. Therefore this book should be useful for plant biologists or anyone else is interested in protein trafficking in plant secretory pathway., Biology, Life Sciences<
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In plant cells it has been demonstrated that many vacuolar proteins are sorted to their final destination by cargo receptors. These receptors are transmembrane proteins able to bind solub… mais…
In plant cells it has been demonstrated that many vacuolar proteins are sorted to their final destination by cargo receptors. These receptors are transmembrane proteins able to bind soluble vacuolar proteins determining their transport to vacuoles. This study is focused on AtRMR, a family of putative receptors composed of six genes in Arabidopsis thaliana. These experiments showed that AtRMR1 localizes in the trans-Golgi network while AtRMR2 localizes in the endoplasmic reticulum. This different localization is due to a putative localization signal present in the AtRMR1 linker. Also this study demonstrated that AtRMR1 can make homodimers and can interact with AtRMR2 making heterodimers. These dimers localize in the trans-Golgi network. Finally the transmembrane and the linker are probably the domains involved in protein-protein interaction. This book provided new information about the physiology of AtRMR traffic and dimerization, improving the comprehension of the mechanisms and the localization signals involved in protein sorting to vacuoles. Therefore this book should be useful for plant biologists or anyone else is interested in protein trafficking in plant secretory pathway. Bücher, Hörbücher & Kalender / Bücher / Sachbuch / Naturwissenschaften / Biologie<
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Occhialini, Alessandro: Receptor Membrane Ring-H2 (RMR) Proteins in Plants Investigation of AtRMR localization and interaction in plant secretory pathway - nuovo livro
Occhialini, Alessandro: Receptor Membrane Ring-H2 (RMR) Proteins in Plants Investigation of AtRMR localization and interaction in plant secretory pathway - nuovo livro
[EAN: 9783659391866], Neubuch, [PU: LAP LAMBERT Academic Publishing], nach der Bestellung gedruckt Neuware -In plant cells it has been demonstrated that many vacuolar proteins are sorted … mais…
[EAN: 9783659391866], Neubuch, [PU: LAP LAMBERT Academic Publishing], nach der Bestellung gedruckt Neuware -In plant cells it has been demonstrated that many vacuolar proteins are sorted to their final destination by cargo receptors. These receptors are transmembrane proteins able to bind soluble vacuolar proteins determining their transport to vacuoles. This study is focused on AtRMR, a family of putative receptors composed of six genes in Arabidopsis thaliana. These experiments showed that AtRMR1 localizes in the trans-Golgi network while AtRMR2 localizes in the endoplasmic reticulum. This different localization is due to a putative localization signal present in the AtRMR1 linker. Also this study demonstrated that AtRMR1 can make homodimers and can interact with AtRMR2 making heterodimers. These dimers localize in the trans-Golgi network. Finally the transmembrane and the linker are probably the domains involved in protein-protein interaction. This book provided new information about the physiology of AtRMR traffic and dimerization, improving the comprehension of the mechanisms and the localization signals involved in protein sorting to vacuoles. Therefore this book should be useful for plant biologists or anyone else is interested in protein trafficking in plant secretory pathway. 308 pp. Englisch, Books<
NEW BOOK. Custos de envio:Versandkostenfrei. (EUR 0.00) AHA-BUCH GmbH, Einbeck, Germany [51283250] [Rating: 5 (von 5)]
Paperback, [PU: LAP Lambert Academic Publishing], In plant cells it has been demonstrated that many vacuolar proteins are sorted to their final destination by cargo receptors. These recep… mais…
Paperback, [PU: LAP Lambert Academic Publishing], In plant cells it has been demonstrated that many vacuolar proteins are sorted to their final destination by cargo receptors. These receptors are transmembrane proteins able to bind soluble vacuolar proteins determining their transport to vacuoles. This study is focused on AtRMR, a family of putative receptors composed of six genes in Arabidopsis thaliana. These experiments showed that AtRMR1 localizes in the trans-Golgi network while AtRMR2 localizes in the endoplasmic reticulum. This different localization is due to a putative localization signal present in the AtRMR1 linker. Also this study demonstrated that AtRMR1 can make homodimers and can interact with AtRMR2 making heterodimers. These dimers localize in the trans-Golgi network. Finally the transmembrane and the linker are probably the domains involved in protein-protein interaction. This book provided new information about the physiology of AtRMR traffic and dimerization, improving the comprehension of the mechanisms and the localization signals involved in protein sorting to vacuoles. Therefore this book should be useful for plant biologists or anyone else is interested in protein trafficking in plant secretory pathway., Biology, Life Sciences<
In plant cells it has been demonstrated that many vacuolar proteins are sorted to their final destination by cargo receptors. These receptors are transmembrane proteins able to bind solub… mais…
In plant cells it has been demonstrated that many vacuolar proteins are sorted to their final destination by cargo receptors. These receptors are transmembrane proteins able to bind soluble vacuolar proteins determining their transport to vacuoles. This study is focused on AtRMR, a family of putative receptors composed of six genes in Arabidopsis thaliana. These experiments showed that AtRMR1 localizes in the trans-Golgi network while AtRMR2 localizes in the endoplasmic reticulum. This different localization is due to a putative localization signal present in the AtRMR1 linker. Also this study demonstrated that AtRMR1 can make homodimers and can interact with AtRMR2 making heterodimers. These dimers localize in the trans-Golgi network. Finally the transmembrane and the linker are probably the domains involved in protein-protein interaction. This book provided new information about the physiology of AtRMR traffic and dimerization, improving the comprehension of the mechanisms and the localization signals involved in protein sorting to vacuoles. Therefore this book should be useful for plant biologists or anyone else is interested in protein trafficking in plant secretory pathway. Bücher, Hörbücher & Kalender / Bücher / Sachbuch / Naturwissenschaften / Biologie<
Nr. GC3QP6NHIVV. Custos de envio:, Lieferzeit: 5 Tage, DE. (EUR 0.00)
Occhialini, Alessandro: Receptor Membrane Ring-H2 (RMR) Proteins in Plants Investigation of AtRMR localization and interaction in plant secretory pathway - nuovo livro
Occhialini, Alessandro: Receptor Membrane Ring-H2 (RMR) Proteins in Plants Investigation of AtRMR localization and interaction in plant secretory pathway - nuovo livro
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Dados detalhados do livro - Receptor Membrane Ring-H2 (RMR) Proteins in Plants
EAN (ISBN-13): 9783659391866 ISBN (ISBN-10): 3659391867 Livro de bolso Ano de publicação: 2013 Editor/Editora: LAP Lambert Academic Publishing
Livro na base de dados desde 2014-10-10T04:35:04-03:00 (Sao Paulo) Página de detalhes modificada pela última vez em 2023-06-01T15:53:28-03:00 (Sao Paulo) Número ISBN/EAN: 9783659391866
Número ISBN - Ortografia alternativa: 3-659-39186-7, 978-3-659-39186-6 Ortografia alternativa e termos de pesquisa relacionados: Autor do livro: alessandro Título do livro: pathway, plant, ring, membrane
