Protein translocation across the bacterial cytoplasmic membrane.

By A. Driessen, N. Nouwen. Annual Review of Biochemistry, 2008

671 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

The bacterial cell envelope. (2010, background): “The second transmembrane helix functions to stop the translocation reaction and this helix exits the SecYEG translocator laterally where it remains in the IM (Van den Berg et al. 2004; Driessen and Nouwen 2008).”
Biological Diversity of Prokaryotic Type IV Secretion Systems (2009, background): “As exemplified with the GSP subunit SecY, polytopic proteins generally assemble as dimeric or higher-order multimeric channels (85, 99).”
A structural model of the active ribosome-bound membrane protein insertase YidC (2014, background): “While SecY is known to translocate hydrophilic nascent chains through its central aqueous channel (Cannon et al., 2005; Rapoport, 2007; Driessen and Nouwen, 2008) and insert TM domains through a lateral gate (Van den Berg et al., 2004; Gogala et al., 2014), our model suggests that the YidC…”
Stochastic mechano-chemical kinetics of molecular motors: A multidisciplinary enterprise from a physicist’s perspective (2012, background): “Therefore, it is not surprising that in some of the pathways, the secretion across the inner membranes of both Gram-positive and Gram-negative bacteria take place following identical routeseither the general secretion (Sec) pathway or the twin-arginine translocation (Tat) pathway [1244, 1228, 1245, ”