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Lateral opening of the bacterial translocon on ribosome binding and signal peptide insertion
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/cphc.200900238openalex-snapshot
Fluorescence Quenching by Photoinduced Electron Transfer: A Reporter for Conformational Dynamics of Macromolecules
inferredcites →https://doi.org/10.1002/embj.201387465openalex-snapshot
GTP hydrolysis by EF‐G synchronizes tRNA movement on small and large ribosomal subunits
inferredcites →https://doi.org/10.1007/978-1-60327-412-8_8openalex-snapshot
Purification and Functional Reconstitution of the Bacterial Protein Translocation Pore, the SecYEG Complex
inferredcites →https://doi.org/10.1007/s00216-013-6790-8openalex-snapshot
Nanodisc-solubilized membrane protein library reflects the membrane proteome
inferredcites →https://doi.org/10.1016/j.celrep.2011.11.003openalex-snapshot
Structure of the SecY Complex Unlocked by a Preprotein Mimic
inferredcites →https://doi.org/10.1016/j.febslet.2009.10.024openalex-snapshot
Membrane protein assembly into Nanodiscs
inferredcites →https://doi.org/10.1016/j.jmb.2013.08.012openalex-snapshot
Monitoring the Activity of Single Translocons
inferredcites →https://doi.org/10.1016/j.str.2009.09.010openalex-snapshot
Regulation of the Protein-Conducting Channel by a Bound Ribosome
inferredcites →https://doi.org/10.1016/s0076-6879(09)64011-8openalex-snapshot
Reconstitution of Membrane Proteins in Phospholipid Bilayer Nanodiscs
inferredcites →https://doi.org/10.1017/s0033583500001797openalex-snapshot
Phase transitions and fluidity characteristics of lipids and cell membranes
inferredcites →https://doi.org/10.1021/bc0341324openalex-snapshot
Inter- and Intramolecular Fluorescence Quenching of Organic Dyes by Tryptophan
inferredcites →https://doi.org/10.1021/bi701398yopenalex-snapshot
Features of Transmembrane Segments That Promote the Lateral Release from the Translocase into the Lipid Phase
inferredcites →https://doi.org/10.1021/cb800059uopenalex-snapshot
Chain Dynamics of Nascent Polypeptides Emerging from the Ribosome
inferredcites →https://doi.org/10.1021/ja310777kopenalex-snapshot
Reconciling the Roles of Kinetic and Thermodynamic Factors in Membrane–Protein Insertion
inferredcites →https://doi.org/10.1038/nature00827openalex-snapshot
Three-dimensional structure of the bacterial protein-translocation complex SecYEG
inferredcites →https://doi.org/10.1038/nature02218openalex-snapshot
X-ray structure of a protein-conducting channel
inferredcites →https://doi.org/10.1038/nature06387openalex-snapshot
Molecular code for transmembrane-helix recognition by the Sec61 translocon
inferredcites →https://doi.org/10.1038/nature07335openalex-snapshot
Structure of a complex of the ATPase SecA and the protein-translocation channel
inferredcites →https://doi.org/10.1038/nature12720openalex-snapshot
Structure of the SecY channel during initiation of protein translocation
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/ncomms5103openalex-snapshot
Visualization of a polytopic membrane protein during SecY-mediated membrane insertion
inferredcites →https://doi.org/10.1038/nsmb.1402openalex-snapshot
Signal sequence–independent membrane targeting of ribosomes containing short nascent peptides within the exit tunnel
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/sj.emboj.7601661openalex-snapshot
Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA
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.1220361110openalex-snapshot
Exploring the nature of the translocon-assisted protein insertion
inferredcites →https://doi.org/10.1073/pnas.92.6.1945openalex-snapshot
GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs.
inferredcites →https://doi.org/10.1074/jbc.m111.297911openalex-snapshot
Competitive Binding of the SecA ATPase and Ribosomes to the SecYEG Translocon
inferredcites →https://doi.org/10.1074/jbc.m901855200openalex-snapshot
The Lateral Gate of SecYEG Opens during Protein Translocation
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.e10-01-0060openalex-snapshot
The Hydrophobic Core of the Sec61 Translocon Defines the Hydrophobicity Threshold for Membrane Integration
inferredcites →https://doi.org/10.1146/annurev-biophys-050511-102312openalex-snapshot
Mechanisms of Sec61/SecY-Mediated Protein Translocation Across Membranes
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Structural Basis of the Sec Translocon and YidC Revealed Through X-ray Crystallography
inferred← citeshttps://doi.org/10.1016/b978-0-323-99507-8.00049-4openalex-snapshot
Membrane protein folding, misfolding, and quality control
inferred← citeshttps://doi.org/10.1016/bs.abl.2018.05.003openalex-snapshot
Biophysical Analysis of Sec-Mediated Protein Translocation in Nanodiscs
inferred← citeshttps://doi.org/10.1016/j.bbamcr.2018.08.018openalex-snapshot
Profiling of signal sequence characteristics and requirement of different translocation components
inferred← citeshttps://doi.org/10.1016/j.bbamem.2016.02.017openalex-snapshot
Decrypting protein insertion through the translocon with free-energy calculations
inferred← citeshttps://doi.org/10.1016/j.bpj.2018.10.002openalex-snapshot
Forces on Nascent Polypeptides during Membrane Insertion and Translocation via the Sec Translocon
inferred← citeshttps://doi.org/10.1016/j.ceb.2016.04.009openalex-snapshot
Toward a structural understanding of co-translational protein translocation
inferred← citeshttps://doi.org/10.1016/j.jmb.2016.03.022openalex-snapshot
Protein Elongation, Co-translational Folding and Targeting
inferred← citeshttps://doi.org/10.1016/j.sbi.2016.11.020openalex-snapshot
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Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex
inferred← citeshttps://doi.org/10.1021/acs.langmuir.9b00126openalex-snapshot
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inferred← citeshttps://doi.org/10.1038/ncomms15562openalex-snapshot
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inferred← citeshttps://doi.org/10.1038/ncomms9403openalex-snapshot
Structure of the native Sec61 protein-conducting channel
inferred← citeshttps://doi.org/10.1038/nrmicro.2016.161openalex-snapshot
Protein export through the bacterial Sec pathway
inferred← citeshttps://doi.org/10.1038/s41598-017-00109-8openalex-snapshot
YidC and SecYEG form a heterotetrameric protein translocation channel
inferred← citeshttps://doi.org/10.1038/s41598-017-18830-9openalex-snapshot
Each protomer of a dimeric YidC functions as a single membrane insertase
inferred← citeshttps://doi.org/10.1038/s41598-018-28262-8openalex-snapshot
Cotranslational protein targeting to the membrane: Nascent-chain transfer in a quaternary complex formed at the translocon
inferred← citeshttps://doi.org/10.1038/s41598-020-73185-yopenalex-snapshot
SecY-mediated quality control prevents the translocation of non-gated porins
inferred← citeshttps://doi.org/10.1038/s41598-021-83224-xopenalex-snapshot
Molecular communication of the membrane insertase YidC with translocase SecYEG affects client proteins
inferred← citeshttps://doi.org/10.1038/s44318-023-00004-1openalex-snapshot
Dynamic coupling of fast channel gating with slow ATP-turnover underpins protein transport through the Sec translocon
inferred← citeshttps://doi.org/10.1039/c9ra07054kopenalex-snapshot
A supramolecular hydrophobic guest transport system based on a biological macrocycle
inferred← citeshttps://doi.org/10.1073/pnas.2100474118openalex-snapshot
Lateral gate dynamics of the bacterial translocon during cotranslational membrane protein insertion
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Role of the Cytosolic Loop C2 and the C Terminus of YidC in Ribosome Binding and Insertion Activity
inferred← citeshttps://doi.org/10.1074/jbc.ra119.010686openalex-snapshot
Noncompetitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome in Escherichia coli
inferred← citeshttps://doi.org/10.1083/jcb.201502103openalex-snapshot
Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon
inferred← citeshttps://doi.org/10.1093/nar/gkx888openalex-snapshot
Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence
inferred← citeshttps://doi.org/10.1098/rstb.2015.0025openalex-snapshot
Channel crossing: how are proteins shipped across the bacterial plasma membrane?
inferred← citeshttps://doi.org/10.1101/2020.12.09.414946openalex-snapshot
Recognition of discrete export signals in early flagellar subunits during bacterial Type III secretion
inferred← citeshttps://doi.org/10.1101/310698openalex-snapshot
Forces on nascent polypeptides during membrane insertion and translocation via the Sec translocon
inferred← citeshttps://doi.org/10.1101/793943openalex-snapshot
Energy landscape steering mediates dynamic coupling in ATP-driven protein translocation by the bacterial Sec machinery
inferred← citeshttps://doi.org/10.1101/cshperspect.a041250openalex-snapshot
Mechanism of Protein Translocation by the Sec61 Translocon Complex
inferred← citeshttps://doi.org/10.1101/cshperspect.a041251openalex-snapshot
The Biogenesis of Multipass Membrane Proteins
inferred← citeshttps://doi.org/10.1111/febs.15905openalex-snapshot
Membrane protein biogenesis at the ER: the highways and byways
inferred← citeshttps://doi.org/10.1111/mmi.13452openalex-snapshot
The bacterial SRP receptor, FtsY, is activated on binding to the translocon
inferred← citeshttps://doi.org/10.1146/annurev-biochem-080125-020218openalex-snapshot
Membrane Protein Insertion in Mammalian Cells
inferred← citeshttps://doi.org/10.1146/annurev-biophys-052118-115352openalex-snapshot
Single-Molecule Studies on the Protein Translocon
inferred← citeshttps://doi.org/10.1159/000484563openalex-snapshot
Comparative Analyses of Transport Proteins Encoded within the Genomes of Bdellovibrio bacteriovorus HD100 and Bdellovibrio exovorus JSS
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Investigation of the Oligomeric State of Membrane-Bound SecA Using Förster Resonance Energy Transfer
inferred← citeshttps://doi.org/10.15252/embj.2019104054openalex-snapshot
Co‐translational insertion and topogenesis of bacterial membrane proteins monitored in real time
inferred← citeshttps://doi.org/10.15252/embr.201948191openalex-snapshot
Partially inserted nascent chain unzips the lateral gate of the Sec translocon
inferred← citeshttps://doi.org/10.25560/56941openalex-snapshot
Characterisation of the pathogenic Escherichia coli type three secretion system effector NleG
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Faculty Opinions recommendation of Each protomer of a dimeric YidC functions as a single membrane insertase.
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Faculty Opinions recommendation of Partially inserted nascent chain unzips the lateral gate of the Sec translocon.
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Recognition of discrete export signals in early flagellar subunits during bacterial type III secretion
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