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Alessandro Occhialini: Receptor Membrane Ring-H2 (RMR) Proteins in Plants : Investigation of AtRMR localization and interaction in plant secretory pathway - Livres de poche
[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 … Plus…
[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<
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… Plus…
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… Plus…
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 - nouveau livre
Occhialini, Alessandro: Receptor Membrane Ring-H2 (RMR) Proteins in Plants Investigation of AtRMR localization and interaction in plant secretory pathway - nouveau livre
[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 … Plus…
[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<
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… Plus…
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… Plus…
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. Frais d'envoi, 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 - nouveau livre
Occhialini, Alessandro: Receptor Membrane Ring-H2 (RMR) Proteins in Plants Investigation of AtRMR localization and interaction in plant secretory pathway - nouveau livre
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Informations détaillées sur le livre - Receptor Membrane Ring-H2 (RMR) Proteins in Plants
EAN (ISBN-13): 9783659391866 ISBN (ISBN-10): 3659391867 Livre de poche Date de parution: 2013 Editeur: LAP Lambert Academic Publishing
Livre dans la base de données depuis 2014-10-10T09:35:04+02:00 (Zurich) Page de détail modifiée en dernier sur 2023-06-01T20:53:28+02:00 (Zurich) ISBN/EAN: 9783659391866
ISBN - Autres types d'écriture: 3-659-39186-7, 978-3-659-39186-6 Autres types d'écriture et termes associés: Auteur du livre: alessandro Titre du livre: pathway, plant, ring, membrane
