Molecular chaperones of the heat shock cognate 70 kDa (HSC70) family are highly conserved in all living organisms and assist nascent protein folding in normal physiological conditions as well as in biotic and abiotic stress conditions. In the absence of specific inhibitors or viable knockout mutants...
Détails bibliographiques
| Publié dans: | Journal of experimental botany. - 1985. - 60(2009), 9 vom: 14., Seite 2653-64
|
|---|
| Auteur principal: |
Cazalé, Anne-Claire
(Auteur) |
|---|
| Autres auteurs: |
Clément, Mathilde,
Chiarenza, Serge,
Roncato, Marie-Anne,
Pochon, Nathalie,
Creff, Audrey,
Marin, Elena,
Leonhardt, Nathalie,
Noël, Laurent D |
|---|
| Format: | Article en ligne
|
|---|
| Langue: | English |
|---|
| Publié: |
2009
|
|---|
| Accès à la collection: | Journal of experimental botany
|
|---|
| Sujets: | Journal Article
Research Support, Non-U.S. Gov't
Arabidopsis Proteins
HSC70 Heat-Shock Proteins
Indoleacetic Acids
Cadmium
00BH33GNGH
Glucosyltransferases
EC 2.4.1.-
SGT1 protein, Arabidopsis
plus...
Arsenic
N712M78A8G |
|---|