SEC Translocation Channels
"SEC Translocation Channels" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
Universally conserved multiprotein complexes that form the protein transport channel of the general secretory (SEC) pathway. The SEC translocase is present in all bacteria, archaea, and eukaryotes. It is in the ENDOPLASMIC RETICULUM membrane of eukaryotic cells, in the THYLAKOID MEMBRANE in CHLOROPLASTS and in some protozoa in the INNER MITOCHONDRIAL MEMBRANE.
|SEC Translocation Channels
- SEC Translocation Channels
- Channels, SEC Translocation
- Translocation Channels, SEC
- SEC Translocase
- Translocase, SEC
- SEC Translocons
- Translocons, SEC
- SEC Complexes
- Complexes, SEC
- SEC61 Protein
- Protein, SEC61
- Sec Protein Translocation Systems
- SecYEG Translocon
- Translocon, SecYEG
- SecY Translocase
- Translocase, SecY
- SecYEG Protein Translocation System
- SecYEG Translocation Channels
- Channels, SecYEG Translocation
- Translocation Channels, SecYEG
- SecYEG Complexes
- Complexes, SecYEG
- SecYEG Complex
- Complex, SecYEG
- SEC61 Translocon
- Translocon, SEC61
- SEC61 Translocation Channels
- Channels, SEC61 Translocation
- Translocation Channels, SEC61
- Sec61 Complex
- Complex, Sec61
- Sec61 Protein Translocation System
- SEC61 Translocase
- Translocase, SEC61
Below are MeSH descriptors whose meaning is more general than "SEC Translocation Channels".
Below are MeSH descriptors whose meaning is more specific than "SEC Translocation Channels".
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Below are the most recent publications written about "SEC Translocation Channels" by people in Profiles.
Mechanism of an intramembrane chaperone for multipass membrane proteins. Nature. 2022 11; 611(7934):161-166.
Substrate-driven assembly of a translocon for multipass membrane proteins. Nature. 2022 11; 611(7934):167-172.
Contribution of the EssC ATPase to the assembly of the type 7b secretion system in Staphylococcus aureus. J Biol Chem. 2022 09; 298(9):102318.
An ER translocon for multi-pass membrane protein biogenesis. Elife. 2020 08 21; 9.
The architecture of EMC reveals a path for membrane protein insertion. Elife. 2020 05 27; 9.
Septal secretion of protein A in Staphylococcus aureus requires SecA and lipoteichoic acid synthesis. Elife. 2018 05 14; 7.
Identification of Oxa1 Homologs Operating in the Eukaryotic Endoplasmic Reticulum. Cell Rep. 2017 12 26; 21(13):3708-3716.
Secretion genes as determinants of Bacillus anthracis chain length. J Bacteriol. 2012 Aug; 194(15):3841-50.
The structural basis of tail-anchored membrane protein recognition by Get3. Nature. 2009 Sep 17; 461(7262):361-6.
Saccharomyces cerevisiae mitochondria lack a bacterial-type sec machinery. Protein Sci. 1996 Dec; 5(12):2651-2.