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Structural and Mechanistic Insights into Protein Translocation

https://doi.org/10.1146/annurev-cellbio-100616-060439
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93/93 checkable references clean · checked 2026-07-22

Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.

The 93 checked references that resolve
resolves10.1146/annurev-biochem-072711-164732
Signal Recognition Particle: An Essential Protein-Targeting Machine
resolves10.7554/eLife.15598
Two-way communication between SecY and SecA suggests a Brownian ratchet mechanism for protein translocation
resolves10.1016/j.cell.2013.02.003
A Network of Cytosolic Factors Targets SRP-Independent Proteins to the Endoplasmic Reticulum
resolves10.1016/j.cell.2014.03.063
A “Push and Slide” Mechanism Allows Sequence-Insensitive Translocation of Secretory Proteins by the SecA ATPase
resolves10.1016/j.resmic.2013.03.007
The Sec-dependent pathway
resolves10.1038/ncomms5103
Visualization of a polytopic membrane protein during SecY-mediated membrane insertion
resolves10.1083/jcb.200412019
Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY
resolves10.1038/nature19309
Cotranslational signal-independent SRP preloading during membrane targeting
resolves10.1016/j.ceb.2016.03.021
N-linked glycosylation and homeostasis of the endoplasmic reticulum
resolves10.1098/rstb.2015.0025
Channel crossing: how are proteins shipped across the bacterial plasma membrane?
resolves10.1038/nrm2657
Delivering proteins for export from the cytosol
resolves10.1038/embor.2009.87
The SecY complex forms a channel capable of ionic discrimination
resolves10.1016/j.str.2015.08.002
Membrane Insertases Are Present in All Three Domains of Life
resolves10.1016/j.bbamcr.2013.12.022
The membrane insertase YidC
resolves10.1016/S0092-8674(00)81115-0
The Cotranslational Integration of Membrane Proteins into the Phospholipid Bilayer Is a Multistep Process
resolves10.1093/emboj/16.10.2756
Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme
resolves10.1038/nature02250
Substrate twinning activates the signal recognition particle and its receptor
resolves10.1073/pnas.1012556107
Lateral opening of a translocon upon entry of protein suggests the mechanism of insertion into membranes
resolves10.1016/j.cbpa.2015.09.016
Dynamics of co-translational protein targeting
resolves10.1016/0092-8674(94)90155-4
Topological ?frustration? in multispanning E. coli inner membrane proteins
resolves10.1038/nature12950
Structures of the Sec61 complex engaged in nascent peptide translocation or membrane insertion
resolves10.1038/357047a0
A protein of the endoplasmic reticulum involved early in polypeptide translocation
resolves10.1016/0092-8674(93)90483-7
Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
resolves10.1515/BC.2009.102
Protein targeting by the signal recognition particle
resolves10.1128/JB.181.11.3438-3444.1999
Mapping an Interface of SecY (PrlA) and SecE (PrlG) by Using Synthetic Phenotypes and In Vivo Cross-Linking
resolves10.1016/0092-8674(90)90160-G
The binding cascade of SecB to SecA to SecYE mediates preprotein targeting to the E. coli plasma membrane
resolves10.1111/j.1432-1033.1993.tb17933.x
A tetrameric complex of membrane proteins in the endoplasmic reticulum
resolves10.1016/S0092-8674(00)00028-3
The Sec61p Complex Mediates the Integration of a Membrane Protein by Allowing Lipid Partitioning of the Transmembrane Domain
resolves10.1038/nature03216
Recognition of transmembrane helices by the endoplasmic reticulum translocon
resolves10.1128/JB.187.9.2983-2991.2005
Use of Thioredoxin as a Reporter To Identify a Subset of <i>Escherichia coli</i> Signal Sequences That Promote Signal Recognition Particle-Dependent Translocation
resolves10.1126/science.1074424
Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of SecA
resolves10.1038/nature08870
Recognition of a signal peptide by the signal recognition particle
resolves10.1038/ncomms10471
Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon
resolves10.1016/0092-8674(81)90239-7
Different exported proteins in E. coli show differences in the temporal mode of processing in vivo
resolves10.1091/mbc.E10-01-0060
The Hydrophobic Core of the Sec61 Translocon Defines the Hydrophobicity Threshold for Membrane Integration
resolves10.1016/S0092-8674(00)81418-X
Crystal Structure of the Signal Sequence Binding Subunit of the Signal Recognition Particle
resolves10.1042/bj20021291
The thylakoid membrane protein ALB3 associates with the cpSecY-translocase in Arabidopsis thaliana
resolves10.1074/jbc.M113.477893
The Bacterial Translocon SecYEG Opens upon Ribosome Binding
resolves10.1016/S1097-2765(02)00685-8
Protein Folding during Cotranslational Translocation in the Endoplasmic Reticulum
resolves10.1038/nature13167
Structural basis of Sec-independent membrane protein insertion by YidC
resolves10.1091/mbc.E03-05-0325
The Endoplasmic Reticulum Membrane Is Permeable to Small Molecules
resolves10.1038/nature17163
Crystal structure of a substrate-engaged SecY protein-translocation channel
resolves10.1016/j.molcel.2007.05.002
The Plug Domain of the SecY Protein Stabilizes the Closed State of the Translocation Channel and Maintains a Membrane Seal
resolves10.1006/jmbi.2000.4302
Ratcheting in post-translational protein translocation: a mathematical model11Edited by G. von Heijne
resolves10.1016/S0021-9258(19)36699-2
Membrane assembly of the triple-spanning coronavirus M protein. Individual transmembrane domains show preferred orientation.
resolves10.1098/rstb.2011.0201
The bacterial Sec-translocase: structure and mechanism
resolves10.1101/cshperspect.a013342
Protein Translocation across the Rough Endoplasmic Reticulum
resolves10.1126/science.1261671
Structure of the Get3 targeting factor in complex with its membrane protein cargo
resolves10.1016/S0092-8674(00)80767-9
BiP Acts as a Molecular Ratchet during Posttranslational Transport of Prepro-α Factor across the ER Membrane
resolves10.1016/S0021-9258(18)71491-9
Functional and Nonfunctional LamB Signal Sequences Can Be Distinguished by Their Biophysical Properties
resolves10.1016/S1097-2765(00)80158-6
J Proteins Catalytically Activate Hsp70 Molecules to Trap a Wide Range of Peptide Sequences
resolves10.1083/jcb.134.2.269
Signal sequences specify the targeting route to the endoplasmic reticulum membrane.
resolves10.1093/protein/10.1.1
Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
resolves10.1016/0092-8674(95)90077-2
Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p
resolves10.1038/nature12720
Structure of the SecY channel during initiation of protein translocation
resolves10.1038/nature10014
Preserving the membrane barrier for small molecules during bacterial protein translocation
resolves10.1146/annurev-biophys-050511-102312
Mechanisms of Sec61/SecY-Mediated Protein Translocation Across Membranes
resolves10.1038/ncomms9403
Structure of the native Sec61 protein-conducting channel
resolves10.1016/S0092-8674(00)81738-9
Signal Sequence Recognition in Posttranslational Protein Transport across the Yeast ER Membrane
resolves10.1083/jcb.151.1.167
Spontaneous Release of Cytosolic Proteins from Posttranslational Substrates before Their Transport into the Endoplasmic Reticulum
resolves10.1002/j.1460-2075.1994.tb06293.x
SecD and SecF facilitate protein export in Escherichia coli.
resolves10.1038/nature06384
Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
resolves10.1016/j.tcb.2004.09.002
Membrane-protein integration and the role of the translocation channel
resolves10.1016/0022-2836(87)90186-0
Mathematical modeling of the effects of the signal recognition particle on translation and translocation of proteins across the endoplasmic reticulum membrane
resolves10.1021/bi00069a025
Conformational behavior of Escherichia coli OmpA signal peptides in membrane mimetic environments
resolves10.1073/pnas.0809592106
Energy transduction in protein transport and the ATP hydrolytic cycle of SecA
resolves10.1074/jbc.M207295200
The Permeability of the Endoplasmic Reticulum Is Dynamically Coupled to Protein Synthesis
resolves10.1074/jbc.M112.446583
YidC Occupies the Lateral Gate of the SecYEG Translocon and Is Sequentially Displaced by a Nascent Membrane Protein
resolves10.1016/j.molcel.2007.03.022
Determining the Conductance of the SecY Protein Translocation Channel for Small Molecules
resolves10.1038/nature19070
Global profiling of SRP interaction with nascent polypeptides
resolves10.1128/JB.185.19.5706-5713.2003
The DsbA Signal Sequence Directs Efficient, Cotranslational Export of Passenger Proteins to the <i>Escherichia coli</i> Periplasm via the Signal Recognition Particle Pathway
resolves10.1093/emboj/19.4.542
YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase
resolves10.1126/science.1188950
Control of Membrane Protein Topology by a Single C-Terminal Residue
resolves10.1016/j.cell.2011.11.048
A Calmodulin-Dependent Translocation Pathway for Small Secretory Proteins
resolves10.1016/0092-8674(91)90455-8
A protein-conducting channel in the endoplasmic reticulum
resolves10.1016/j.celrep.2015.10.025
Crystal Structures of SecYEG in Lipidic Cubic Phase Elucidate a Precise Resting and a Peptide-Bound State
resolves10.1111/febs.12296
Structural diversity of calmodulin binding to its target sites
resolves10.1074/jbc.M116.761122
Two alternative binding mechanisms connect the protein translocation Sec71-Sec72 complex with heat shock proteins
resolves10.1038/nature09980
Structure and function of a membrane component SecDF that enhances protein export
resolves10.1038/nature07421
Conformational transition of Sec machinery inferred from bacterial SecYE structures
resolves10.1038/nature02218
X-ray structure of a protein-conducting channel
resolves10.1083/jcb.134.1.25
Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane.
resolves10.1002/j.1460-2075.1986.tb04601.x
The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans‐membrane topology
resolves10.1038/nrm2063
Membrane-protein topology
resolves10.1016/j.cell.2014.05.024
Structure of the Mammalian Ribosome-Sec61 Complex to 3.4 Å Resolution
resolves10.7554/eLife.07975
Structures of the scanning and engaged states of the mammalian SRP-ribosome complex
resolves10.1126/science.aad4992
Structure of the Sec61 channel opened by a signal sequence
resolves10.1016/j.ceb.2016.04.009
Toward a structural understanding of co-translational protein translocation
resolves10.7554/eLife.03035
A structural model of the active ribosome-bound membrane protein insertase YidC
resolves10.1083/jcb.104.2.201
Direct probing of the interaction between the signal sequence of nascent preprolactin and the signal recognition particle by specific cross-linking.
resolves10.1021/bi00490a017
Conformational requirement of signal sequences functioning in yeast: circular dichroism and proton nuclear magnetic resonance studies of synthetic peptides
resolves10.1074/jbc.M113.491613
YidC Protein, a Molecular Chaperone for LacY Protein Folding via the SecYEG Protein Machinery
resolves10.1038/nature07335
Structure of a complex of the ATPase SecA and the protein-translocation channel
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