Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes

By Tom A. Rapoport. Nature, 2007

992 citations recorded by the source corpus.

Subfields: Genetics, Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/18a64447f179f3819a5b765b741aa158d2a5ac82

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Citations in the corpus

Quality control: ER-associated degradation: protein quality control and beyond. (2014, neutral): “Newly synthesized membrane and secreted proteins enter the ER in an unfolded state through a protein-conducting channel named the translocon (Rapoport, 2007).”
Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones (2015, positive): “Besides the canonical roles of chaperones under stressful conditions, Hsp70s have been identified playing several housekeeping roles in the cell under normal conditions such as assisted folding [6,7], oligomeric complex assembly [8], cell cycle regulation [9], import of unfolded polypeptides in the ”
Spatially resolved, highly multiplexed RNA profiling in single cells (2015, positive): “To reach these locations, proteins must pass through the secretion pathway, which often requires translation of mRNA at the endoplasmic reticulum (ER) (34, 35).”
Stochastic mechano-chemical kinetics of molecular motors: A multidisciplinary enterprise from a physicist’s perspective (2012, neutral): “However, depending on the source and type of the cell used, this translocation process can be explained by either power stroke or Brownian ratchet [1290, 1291, 1292, 1293, 1294].”
Topology Prediction of α-Helical Transmembrane Proteins (2016, neutral): “Adapted from [30].”
The endoplasmic reticulum: structure, function and response to cellular signaling (2015, background): “Translation continues on the ER and the emerging polypeptide can co-translationally enter the ER through the translocon [2], which is a channel that contains several Sec proteins and spans the lipid bilayer [13].”