- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
1471-2121
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
N-acetylation and phosphorylation of Sec complex subunits in the ER membrane ; volume:13 ; number:1 ; day:13 ; month:12 ; year:2012 ; pages:1-15 ; date:12.2012
BMC cell biology ; 13, Heft 1 (13.12.2012), 1-15, 12.2012
- Creator
-
Soromani, Christina
Zeng, Naiyan
Hollemeyer, Klaus
Heinzle, Elmar
Klein, Marie-Christine
Tretter, Thomas
Seaman, Matthew N J.
Römisch, Karin
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1186/1471-2121-13-34
- URN
-
urn:nbn:de:101:1-2021081406195899968632
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 10:47 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
- Soromani, Christina
- Zeng, Naiyan
- Hollemeyer, Klaus
- Heinzle, Elmar
- Klein, Marie-Christine
- Tretter, Thomas
- Seaman, Matthew N J.
- Römisch, Karin
- SpringerLink (Online service)
Other Objects (12)
Acetylation of insulin receptor substrate-1 is permissive for tyrosine phosphorylation
Auxiliary subunits : shepherding AMPA receptors to the plasma membrane
The role of mitochondrial acetylation state in the regulation of oxidative phosphorylation
Monitoring phosphorylation and acetylation of CRISPR-mediated HiBiT-tagged endogenous proteins
SecYEG/YidC-Mediated Membrane Protein Biogenesis
Tip60- and sirtuin 2-regulated MARCKS acetylation and phosphorylation are required for diabetic embryopathy
Dynamic regulation of KIF15 phosphorylation and acetylation promotes focal adhesions disassembly in pancreatic cancer
The ribosome-SecYEG complex in the membrane environment
![[Sec. XIII]. - [Sec. XV.]](https://iiif.deutsche-digitale-bibliothek.de/image/2/853bcc84-e790-401b-8664-041381af10dd/full/!306,450/0/default.jpg)
[Sec. XIII]. - [Sec. XV.]
![Sec. XI. - [Sec. XII.]](https://iiif.deutsche-digitale-bibliothek.de/image/2/24c73c8b-a269-4b4d-a06b-72f3ce60b0ee/full/!306,450/0/default.jpg)
Sec. XI. - [Sec. XII.]
Role of a bacterial glycolipid in Sec-independent membrane protein insertion
Sec
Acetylation of insulin receptor substrate-1 is permissive for tyrosine phosphorylation
Auxiliary subunits : shepherding AMPA receptors to the plasma membrane
The role of mitochondrial acetylation state in the regulation of oxidative phosphorylation
Monitoring phosphorylation and acetylation of CRISPR-mediated HiBiT-tagged endogenous proteins
SecYEG/YidC-Mediated Membrane Protein Biogenesis
Tip60- and sirtuin 2-regulated MARCKS acetylation and phosphorylation are required for diabetic embryopathy
Dynamic regulation of KIF15 phosphorylation and acetylation promotes focal adhesions disassembly in pancreatic cancer
The ribosome-SecYEG complex in the membrane environment
[Sec. XIII]. - [Sec. XV.]
Sec. XI. - [Sec. XII.]
Role of a bacterial glycolipid in Sec-independent membrane protein insertion
Sec
Acetylation of insulin receptor substrate-1 is permissive for tyrosine phosphorylation
Auxiliary subunits : shepherding AMPA receptors to the plasma membrane
The role of mitochondrial acetylation state in the regulation of oxidative phosphorylation
Monitoring phosphorylation and acetylation of CRISPR-mediated HiBiT-tagged endogenous proteins
SecYEG/YidC-Mediated Membrane Protein Biogenesis
Tip60- and sirtuin 2-regulated MARCKS acetylation and phosphorylation are required for diabetic embryopathy
Dynamic regulation of KIF15 phosphorylation and acetylation promotes focal adhesions disassembly in pancreatic cancer
The ribosome-SecYEG complex in the membrane environment
[Sec. XIII]. - [Sec. XV.]
Sec. XI. - [Sec. XII.]
Role of a bacterial glycolipid in Sec-independent membrane protein insertion