AbstractProteins involved in protein translocation across the membrane of the endoplasmic reticulum assemble into different oligomeric complexes depending on their state of function. To analyse such membrane protein complexes we fractionated proteins of mammalian rough microsomes and analysed them using blue native PAGE and immunoblotting. Among the proteins characterised are the Sec61p complex, the oligosaccharyl transferase (OST) complex, the translocon-associated protein (TRAP) complex, the TRAM and RAMP4 proteins, the signal recognition particle (SRP) and the SRP receptor (SR). Interestingly, the RAMP4 protein, SR and OST complex display more than one oligomeric form
AbstractThe heterotrimeric Sec61p complex is a major component of the protein-conducting channel of ...
The heterotrimeric Sec61p complex is a major component of the protein-conducting channel of the endo...
AbstractProtein translocation into the endoplasmic reticulum (ER) is the first and decisive step in ...
The translocation site (translocon), at which nascent polypeptides pass through the endoplasmic reti...
Translocation across or integration into the rough endoplasmic reticulum (RER) membrane is the first...
In mammalian cells, proteins are typically translocated across the endoplasmic reticulum (ER) membra...
High-resolution structures provide new insights into how an RNA-protein complex recognizes the sign...
Protein translocation across the endoplasmic reticulum (ER) membrane is fundamental for protein sort...
AbstractWe have analyzed early phases of the cotranslational transport of the secretory protein prep...
The transport of proteins across the endoplasmic reticulum (ER) membrane can occur either cotransla-...
AbstractAs summarized in this minireview, two different signal recognition events, one involving SRP...
We have used the homobifunctional cross-linking reagent disuccinimidyl suberate (DSS) to identify pr...
AbstractDuring cotranslational translocation of proteins into the endoplasmic reticulum (ER) transla...
Protein synthesis, transport, and N-glycosylation are coupled at the mammalian endoplasmic reticulum...
SummaryIn eukaryotic cells, cotranslational protein translocation across the endoplasmic reticulum (...
AbstractThe heterotrimeric Sec61p complex is a major component of the protein-conducting channel of ...
The heterotrimeric Sec61p complex is a major component of the protein-conducting channel of the endo...
AbstractProtein translocation into the endoplasmic reticulum (ER) is the first and decisive step in ...
The translocation site (translocon), at which nascent polypeptides pass through the endoplasmic reti...
Translocation across or integration into the rough endoplasmic reticulum (RER) membrane is the first...
In mammalian cells, proteins are typically translocated across the endoplasmic reticulum (ER) membra...
High-resolution structures provide new insights into how an RNA-protein complex recognizes the sign...
Protein translocation across the endoplasmic reticulum (ER) membrane is fundamental for protein sort...
AbstractWe have analyzed early phases of the cotranslational transport of the secretory protein prep...
The transport of proteins across the endoplasmic reticulum (ER) membrane can occur either cotransla-...
AbstractAs summarized in this minireview, two different signal recognition events, one involving SRP...
We have used the homobifunctional cross-linking reagent disuccinimidyl suberate (DSS) to identify pr...
AbstractDuring cotranslational translocation of proteins into the endoplasmic reticulum (ER) transla...
Protein synthesis, transport, and N-glycosylation are coupled at the mammalian endoplasmic reticulum...
SummaryIn eukaryotic cells, cotranslational protein translocation across the endoplasmic reticulum (...
AbstractThe heterotrimeric Sec61p complex is a major component of the protein-conducting channel of ...
The heterotrimeric Sec61p complex is a major component of the protein-conducting channel of the endo...
AbstractProtein translocation into the endoplasmic reticulum (ER) is the first and decisive step in ...