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Forces on nascent polypeptides during membrane insertion and translocation via the Sec translocon

https://doi.org/10.1101/310698
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1016/j.bbamem.2016.02.017openalex-snapshot
Decrypting protein insertion through the translocon with free-energy calculations
inferredcites →https://doi.org/10.1016/j.bbrc.2010.01.073openalex-snapshot
Divergent stalling sequences sense and control cellular physiology
inferredcites →https://doi.org/10.1016/j.cell.2014.05.024openalex-snapshot
Structure of the Mammalian Ribosome-Sec61 Complex to 3.4 Å Resolution
inferredcites →https://doi.org/10.1016/j.celrep.2012.08.039openalex-snapshot
Long-Timescale Dynamics and Regulation of Sec-Facilitated Protein Translocation
inferredcites →https://doi.org/10.1016/j.celrep.2016.07.042openalex-snapshot
A Link between Integral Membrane Protein Expression and Simulated Integration Efficiency
inferredcites →https://doi.org/10.1016/j.jmb.2014.09.014openalex-snapshot
Mechanisms of Integral Membrane Protein Insertion and Folding
inferredcites →https://doi.org/10.1016/j.sbi.2005.07.004openalex-snapshot
Transmembrane helices before, during, and after insertion
inferredcites →https://doi.org/10.1016/s0092-8674(00)00028-3openalex-snapshot
The Sec61p Complex Mediates the Integration of a Membrane Protein by Allowing Lipid Partitioning of the Transmembrane Domain
inferredcites →https://doi.org/10.1021/ja3034526openalex-snapshot
Direct Simulation of Early-Stage Sec-Facilitated Protein Translocation
inferredcites →https://doi.org/10.1021/jp406925yopenalex-snapshot
On the Nature of the Apparent Free Energy of Inserting Amino Acids into Membrane through the Translocon
inferredcites →https://doi.org/10.1038/nature02218openalex-snapshot
X-ray structure of a protein-conducting channel
inferredcites →https://doi.org/10.1038/nature03216openalex-snapshot
Recognition of transmembrane helices by the endoplasmic reticulum translocon
inferredcites →https://doi.org/10.1038/nature06384openalex-snapshot
Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
inferredcites →https://doi.org/10.1038/nature12950openalex-snapshot
Structures of the Sec61 complex engaged in nascent peptide translocation or membrane insertion
inferredcites →https://doi.org/10.1038/ncomms6263openalex-snapshot
Lateral opening of the bacterial translocon on ribosome binding and signal peptide insertion
inferredcites →https://doi.org/10.1038/ncomms9099openalex-snapshot
Dual-topology insertion of a dual-topology membrane protein
inferredcites →https://doi.org/10.1038/nsb1096-842openalex-snapshot
Experimentally determined hydrophobicity scale for proteins at membrane interfaces
inferredcites →https://doi.org/10.1038/nsmb.2026openalex-snapshot
Cryo-EM structure of the ribosome–SecYE complex in the membrane environment
inferredcites →https://doi.org/10.1038/nsmb.2376openalex-snapshot
A biphasic pulling force acts on transmembrane helices during translocon-mediated membrane integration
inferredcites →https://doi.org/10.1038/nsmb.2940openalex-snapshot
Charge-driven dynamics of nascent-chain movement through the SecYEG translocon
inferredcites →https://doi.org/10.1038/nsmb.3355openalex-snapshot
Cotranslational folding of spectrin domains via partially structured states
inferredcites →https://doi.org/10.1073/pnas.0806085105openalex-snapshot
Theory, analysis, and interpretation of single-molecule force spectroscopy experiments
inferredcites →https://doi.org/10.1073/pnas.0914752107openalex-snapshot
Hydrophobically stabilized open state for the lateral gate of the Sec translocon
inferredcites →https://doi.org/10.1073/pnas.1012556107openalex-snapshot
Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes
inferredcites →https://doi.org/10.1073/pnas.1306787110openalex-snapshot
Cotranslational folding of membrane proteins probed by arrest-peptide–mediated force measurements
inferredcites →https://doi.org/10.1073/pnas.1318432110openalex-snapshot
Functional asymmetry within the Sec61p translocon
inferredcites →https://doi.org/10.1074/jbc.m117.813469openalex-snapshot
Improving membrane protein expression by optimizing integration efficiency
inferredcites →https://doi.org/10.1074/jbc.m707219200openalex-snapshot
Mutations in the Sec61p Channel Affecting Signal Sequence Recognition and Membrane Protein Topology
inferredcites →https://doi.org/10.1083/jcb.201207163openalex-snapshot
A gating motif in the translocation channel sets the hydrophobicity threshold for signal sequence function
inferredcites →https://doi.org/10.1091/mbc.3.2.129openalex-snapshot
Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum.
inferredcites →https://doi.org/10.1091/mbc.e10-01-0060openalex-snapshot
The Hydrophobic Core of the Sec61 Translocon Defines the Hydrophobicity Threshold for Membrane Integration
inferredcites →https://doi.org/10.1093/emboj/cdg361openalex-snapshot
Molecular mechanism of signal sequence orientation in the endoplasmic reticulum
inferredcites →https://doi.org/10.1109/mcse.2014.80openalex-snapshot
XSEDE: Accelerating Scientific Discovery
inferredcites →https://doi.org/10.1126/science.1261909openalex-snapshot
Mechanical force releases nascent chain–mediated ribosome arrest in vitro and in vivo
inferredcites →https://doi.org/10.1146/annurev-biophys-051013-022926openalex-snapshot
Energetics of Membrane Protein Folding
inferredcites →https://doi.org/10.1146/annurev-cellbio-092910-154125openalex-snapshot
Membrane Protein Insertion at the Endoplasmic Reticulum
inferredcites →https://doi.org/10.1146/annurev.biochem.77.061606.160747openalex-snapshot
Protein Translocation Across the Bacterial Cytoplasmic Membrane
inferredcites →https://doi.org/10.1371/journal.pcbi.1005427openalex-snapshot
Structurally detailed coarse-grained model for Sec-facilitated co-translational protein translocation and membrane integration
inferredcites →https://doi.org/10.1371/journal.pcbi.1005595openalex-snapshot
Unicycler: Resolving bacterial genome assemblies from short and long sequencing reads
inferredcites →https://doi.org/10.7554/elife.08697openalex-snapshot
Regulation of multispanning membrane protein topology via post-translational annealing

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1002/1873-3468.14286openalex-snapshot
Upstream charged and hydrophobic residues impact the timing of membrane insertion of transmembrane helices
inferred← citeshttps://doi.org/10.70675/a6000bacze626z44ceza648z6e7cb02e2defopenalex-snapshot
Implication de l'hypoxie et du stress du réticulum endoplasmique dans l'altération phénotypique des cellules épithéliales alvéolaires
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