Proteins mediating vectorial translocation: Purification of the active domain of the endoplasmic reticulum docking protein
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Methods in Enzymology, 96 (1983), S. 692-700
Works by Bernhard Dobberstein ; 027
- Event
-
Veröffentlichung
- (where)
-
Heidelberg
- (who)
-
Universitätsbibliothek Heidelberg
- (when)
-
2009
- Creator
- DOI
-
10.11588/heidok.00009184
- URN
-
urn:nbn:de:bsz:16-opus-91842
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:57 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Meyer, David I.
- Dobberstein, Bernhard
- Universitätsbibliothek Heidelberg
Time of origin
- 2009
Other Objects (12)
Protein translocation at the endoplasmic reticulum membrane in Arabidopsis thaliana
Protein synthesis on the endoplasmic reticulum
A Membrane Component Essential for Vectorial Translocation of Nascent Proteins across the Endoplasmic Reticulum: Requirements for Its Extraction and Reassociation with the Membrane
Intramembrane proteases in endoplasmic reticulum protein homeostasis
Protein degradation from the mammalian endoplasmic reticulum
Protein insertion into the membrane of the endoplasmic reticulum: The architecture of the translocation site
Protein C-mannosylation within the endoplasmic reticulum, [...]. [Band].*
Thioredoxin‐interacting protein regulates protein disulfide isomerases and endoplasmic reticulum stress
Interplay of proteins and lipids during endoplasmic reticulum-associated protein degradation
Identification of endoplasmic reticulum-shaping proteins in Plasmodium parasites
ORMDL proteins are a conserved new family of endoplasmic reticulum membrane proteins
Study of protein O-mannosylation in the context of endoplasmic reticulum protein homeostasis
Protein translocation at the endoplasmic reticulum membrane in Arabidopsis thaliana
Protein synthesis on the endoplasmic reticulum
A Membrane Component Essential for Vectorial Translocation of Nascent Proteins across the Endoplasmic Reticulum: Requirements for Its Extraction and Reassociation with the Membrane
Intramembrane proteases in endoplasmic reticulum protein homeostasis
Protein degradation from the mammalian endoplasmic reticulum
Protein insertion into the membrane of the endoplasmic reticulum: The architecture of the translocation site
Protein C-mannosylation within the endoplasmic reticulum, [...]. [Band].*
Thioredoxin‐interacting protein regulates protein disulfide isomerases and endoplasmic reticulum stress
Interplay of proteins and lipids during endoplasmic reticulum-associated protein degradation
Identification of endoplasmic reticulum-shaping proteins in Plasmodium parasites
ORMDL proteins are a conserved new family of endoplasmic reticulum membrane proteins
Study of protein O-mannosylation in the context of endoplasmic reticulum protein homeostasis
Protein translocation at the endoplasmic reticulum membrane in Arabidopsis thaliana
Protein synthesis on the endoplasmic reticulum
A Membrane Component Essential for Vectorial Translocation of Nascent Proteins across the Endoplasmic Reticulum: Requirements for Its Extraction and Reassociation with the Membrane
Intramembrane proteases in endoplasmic reticulum protein homeostasis
Protein degradation from the mammalian endoplasmic reticulum
Protein insertion into the membrane of the endoplasmic reticulum: The architecture of the translocation site
Protein C-mannosylation within the endoplasmic reticulum, [...]. [Band].*
Thioredoxin‐interacting protein regulates protein disulfide isomerases and endoplasmic reticulum stress
Interplay of proteins and lipids during endoplasmic reticulum-associated protein degradation
Identification of endoplasmic reticulum-shaping proteins in Plasmodium parasites
ORMDL proteins are a conserved new family of endoplasmic reticulum membrane proteins