Roughly one quarter of all genes code for integral membrane proteins that are inserted into
the plasma membrane of prokaryotes or the endoplasmic reticulum membrane of …

Co-translational protein targeting to the endoplasmic reticulum (ER), represents an
evolutionary-conserved mechanism to target proteins into the secretory pathway. In this …

Recent research has provided an abundance of new information on membrane
biochemistry. Now more than ever, it is essential to update our current understanding of …

Protein transport via the Sec translocon represents an evolutionary conserved mechanism
for delivering cytosolically-synthesized proteins to extra-cytosolic compartments. The Sec …

The topology of polytopic membrane proteins is determined by topogenic sequences in the
protein, protein-translocon interactions, and interactions during folding within the protein and …

Membrane protein folding and topogenesis are tuned to a given lipid profile since lipids and
proteins have co-evolved to follow a set of interdependent rules governing final protein …

In eukaryotes, most integral membrane proteins are synthesized, integrated into the
membrane, and folded properly in the endoplasmic reticulum (ER). We screened the …

The insertion and assembly of proteins into the inner membrane of bacteria are crucial for
many cellular processes, including cellular respiration, signal transduction, and ion and pH …

The membrane protein–folding problem can be articulated by two central questions. How is
protein topology established by selective peptide transport to opposite sides of the cellular …

The Sec61 complex is the major protein translocation channel of the endoplasmic reticulum
(ER), where it plays a central role in the biogenesis of membrane and secretory proteins …