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Co-translational protein targeting in bacteria

199/199 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.

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The 199 checked references that resolve

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The presence of a helix breaker in the hydrophobic core of signal sequences of secretory proteins prevents recognition by the signal‐recognition particle in Escherichia coli

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Signal Recognition Particle: An Essential Protein-Targeting Machine

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SecYEG activates GTPases to drive the completion of cotranslational protein targeting

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Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA

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FtsY, the bacterial signal‐recognition particle receptor, interacts functionally and physically with the SecYEG translocon

resolves10.1091/mbc.e12-06-0434

Fingerloop activates cargo delivery and unloading during cotranslational protein targeting

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The Crystal Structure of the Signal Recognition Particle in Complex with Its Receptor

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Characterization of cold-sensitive secY mutants of Escherichia coli

resolves10.1074/jbc.M705429200

Membrane Targeting of Ribosomes and Their Release Require Distinct and Separable Functions of FtsY

resolves10.1038/nsmb.2605

SIMIBI twins in protein targeting and localization

resolves10.1073/pnas.0702570104

The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP

resolves10.1038/nsmb.2141

Structural basis for the molecular evolution of SRP-GTPase activation by protein

resolves10.1038/srep45089

Isolation and characterization of the E. coli membrane protein production strain Mutant56(DE3)

resolves10.1093/embo-reports/kve154

YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids

resolves10.1038/nsmb.3086

Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions

resolves10.1074/jbc.M300929200

Export of β-Lactamase Is Independent of the Signal Recognition Particle

resolves10.1242/jcs.166116

Co-translational membrane association of the Escherichia coli SRP receptor

resolves10.1073/pnas.0808584106

A signal-anchor sequence stimulates signal recognition particle binding to ribosomes from inside the exit tunnel

resolves10.1038/340482a0

Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle

resolves10.1016/j.bbamem.2010.07.025

Early targeting events during membrane protein biogenesis in Escherichia coli

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Remote Origins of Tail-Anchored Proteins

resolves10.1038/ncomms5180

Interplay between trigger factor and other protein biogenesis factors on the ribosome

resolves10.1038/nsmb.1402

Signal sequence–independent membrane targeting of ribosomes containing short nascent peptides within the exit tunnel

resolves10.1016/j.jmb.2009.04.061

Two Cooperating Helices Constitute the Lipid-binding Domain of the Bacterial SRP Receptor

resolves10.1091/mbc.e11-02-0152

Signal sequence–independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle

resolves10.1261/rna.1285609

Conformation of the signal recognition particle in ribosomal targeting complexes

resolves10.1016/j.celrep.2011.12.007

DnaK Functions as a Central Hub in the E. coli Chaperone Network

resolves10.1111/j.1365-2958.2004.04278.x

Subcellular sites for bacterial protein export

resolves10.1016/j.bbamcr.2013.11.007

Chaperone networking facilitates protein targeting to the bacterial cytoplasmic membrane

resolves10.1093/bioinformatics/bts149

Large-scale analysis of conserved rare codon clusters suggests an involvement in co-translational molecular recognition events

resolves10.1042/BJ20121227

Breaking on through to the other side: protein export through the bacterial Sec system

resolves10.1083/jcb.201609022

Preprotein mature domains contain translocase targeting signals that are essential for secretion

resolves10.1016/j.bmc.2014.11.017

Design, syntheses and evaluation of 4-oxo-5-cyano thiouracils as SecA inhibitors

resolves10.1515/BC.2002.176

YidC, a Newly Defined Evolutionarily Conserved Protein, Mediates Membrane Protein Assembly in Bacteria

resolves10.1242/jcs.054494

Eeyarestatin I inhibits Sec61-mediated protein translocation at the endoplasmic reticulum

resolves10.1007/s00018-003-3006-y

The bacterial translocase: a dynamic protein channel complex

resolves10.1093/emboj/19.4.531

Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity

resolves10.1038/ja.2015.53

Identification of small-molecule inhibitors against SecA by structure-based virtual ligand screening

resolves10.1074/jbc.M509647200

A Dual Function for SecA in the Assembly of Single Spanning Membrane Proteins in Escherichia coli

resolves10.1038/nmicrobiol.2016.265

The signal recognition particle contacts uL23 and scans substrate translation inside the ribosomal tunnel

resolves10.1007/s00284-009-9439-2

The Distinct Anchoring Mechanism of FtsY from Different Microbes

resolves10.1128/JB.01366-07

Functional Overlap but Lack of Complete Cross-Complementation of Streptococcus mutans and Escherichia coli YidC Orthologs

resolves10.1074/jbc.270.34.20106

SecYEG and SecA Are the Stoichiometric Components of Preprotein Translocase

resolves10.1111/mmi.13452

The bacterial SRP receptor, FtsY, is activated on binding to the translocon

resolves10.1146/annurev.biochem.77.061606.160747

Protein Translocation Across the Bacterial Cytoplasmic Membrane

resolves10.1038/nature02250

Substrate twinning activates the signal recognition particle and its receptor

resolves10.1083/jcb.200306069

Ligand crowding at a nascent signal sequence

resolves10.1128/JB.186.8.2492-2494.2004

The CoreEscherichia coliSignal Recognition Particle Receptor Contains Only the N and G Domains of FtsY

resolves10.1074/jbc.M110.140921

Genetic Evidence for Functional Interaction of the Escherichia coli Signal Recognition Particle Receptor with Acidic Lipids in Vivo

resolves10.1038/nsmb.1952

Cryo-EM structure of the E. coli translating ribosome in complex with SRP and its receptor

resolves10.1046/j.1432-1033.2003.03531.x

The sensor protein KdpD inserts into the Escherichia coli membrane independent of the Sec translocase and YidC

resolves10.1016/j.jmb.2006.10.083

The Mechanosensitive Channel Protein MscL Is Targeted by the SRP to The Novel YidC Membrane Insertion Pathway of Escherichia coli

resolves10.7554/eLife.03440

mRNA-programmed translation pauses in the targeting of E. coli membrane proteins

resolves10.1126/science.1090827

Heterodimeric GTPase Core of the SRP Targeting Complex

resolves10.1074/jbc.M111.245696

Membrane Localization of Small Proteins in Escherichia coli

resolves10.1371/journal.pntd.0004403

What Makes a Bacterial Species Pathogenic?:Comparative Genomic Analysis of the Genus Leptospira

resolves10.1038/385361a0

Structure of the conserved GTPase domain of the signal recognition particle

resolves10.1038/11572

resolves10.1073/pnas.0809951106

Independent gene duplications of the YidC/Oxa/Alb3 family enabled a specialized cotranslational function

resolves10.1016/j.jsb.2006.10.025

Structure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY

resolves10.1073/pnas.0914680107

The action of cardiolipin on the bacterial translocon

resolves10.1371/journal.pgen.1007017

The bacterial Sec system is required for the organization and function of the MreB cytoskeleton

resolves10.1261/rna.2196403

The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosome

resolves10.1261/rna.7219805

Conformation of 4.5S RNA in the signal recognition particle and on the 30S ribosomal subunit

resolves10.1038/nsmb.1994

Structural basis of signal-sequence recognition by the signal recognition particle

resolves10.1038/nature02342

Structure of the signal recognition particle interacting with the elongation-arrested ribosome

resolves10.1126/science.1124864

Signal Recognition Particle Receptor Exposes the Ribosomal Translocon Binding Site

resolves10.1038/nature05326

Following the signal sequence from ribosomal tunnel exit to signal recognition particle

resolves10.1073/pnas.0508778102

Streptococcal viability and diminished stress tolerance in mutants lacking the signal recognition particle pathway or YidC2

resolves10.1073/pnas.1521260112

Altered Escherichia coli membrane protein assembly machinery allows proper membrane assembly of eukaryotic protein vitamin K epoxide reductase

resolves10.1016/j.tibs.2006.08.004

The surprising complexity of signal sequences

resolves10.1083/jcb.200204144

Accumulation of endoplasmic membranes and novel membrane-bound ribosome–signal recognition particle receptor complexes inEscherichia coli

resolves10.1093/embo-reports/kve226

Evidence for coupling of membrane targeting and function of the signal recognition particle (SRP) receptor FtsY

resolves10.1038/nsmb.2421

Dynamic switch of the signal recognition particle from scanning to targeting

resolves10.1083/jcb.200503035

Early encounters of a nascent membrane protein

resolves10.1038/sj.embor.7400261

The two membrane segments of leader peptidase partition one by one into the lipid bilayer via a Sec/YidC interface

resolves10.1128/JB.187.9.2983-2991.2005

Use of Thioredoxin as a Reporter To Identify a Subset of Escherichia coli Signal Sequences That Promote Signal Recognition Particle-Dependent Translocation

resolves10.1016/j.molcel.2010.12.028

SecA Interacts with Ribosomes in Order to Facilitate Posttranslational Translocation in Bacteria

resolves10.1128/JB.00622-16

SecA Cotranslationally Interacts with Nascent Substrate Proteins In Vivo

resolves10.1111/j.1365-2958.2005.04696.x

Ribosome‐based protein folding systems are structurally divergent but functionally universal across biological kingdoms

resolves10.1371/journal.pone.0028413

Nascentome Analysis Uncovers Futile Protein Synthesis in Escherichia coli

resolves10.1006/jmbi.1999.3427

Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP

resolves10.1017/S1355838201002205

Important role of the tetraloop region of 4.5S RNA in SRP binding to its receptor FtsY

resolves10.1038/nature08870

Recognition of a signal peptide by the signal recognition particle

resolves10.1016/0958-1669(92)90075-T

Protein export in Escherichia coli

resolves10.1038/ncomms10471

Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon

resolves10.1038/ncomms15470

Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome

resolves10.1242/jcs.165746

Decatransin, a novel natural product inhibiting protein translocation at the Sec61/SecY translocon

resolves10.1099/00221287-146-10-2595

Expression of the ftsY gene, encoding a homologue of the α subunit of mammalian signal recognition particle receptor, is controlled by different promoters in vegetative and sporulating cells of Bacillus subtilis

resolves10.1046/j.1365-2958.1999.01686.x

A molecular switch in SecA protein couples ATP hydrolysis to protein translocation

resolves10.1074/jbc.M509100200

Selective SecA Association with Signal Sequences in Ribosome-bound Nascent Chains

resolves10.1016/j.jmb.2013.07.042

Elucidating the Native Architecture of the YidC: Ribosome Complex

resolves10.1016/j.celrep.2016.11.059

Structural Dynamics of the YidC:Ribosome Complex during Membrane Protein Biogenesis

resolves10.1093/nar/gku883

Structure of the complete bacterial SRP Alu domain

resolves10.1126/science.1101952

Mechanism of Ammonia Transport by Amt/MEP/Rh: Structure of AmtB at 1.35 Å

resolves10.1007/s00232-017-0012-9

Driving Forces of Translocation Through Bacterial Translocon SecYEG

resolves10.1074/jbc.C100683200

The Integration of YidC into the Cytoplasmic Membrane ofEscherichia coli Requires the Signal Recognition Particle, SecA and SecYEG

resolves10.1083/jcb.150.3.689

Dissecting the Translocase and Integrase Functions of the Escherichia coli Secyeg Translocon

resolves10.1007/s10254-002-0002-9

Signal recognition particle-depencent protein targeting, universal to all kingdoms of life

resolves10.1091/mbc.10.7.2163

In Vitro Studies with Purified Components Reveal Signal Recognition Particle (SRP) and SecA/SecB as Constituents of Two Independent Protein-targeting Pathways ofEscherichia coli

resolves10.1016/j.molcel.2009.04.019

YidC and Oxa1 Form Dimeric Insertion Pores on the Translating Ribosome

resolves10.1042/BCJ20160545

Membrane protein insertion and assembly by the bacterial holo-translocon SecYEG–SecDF–YajC–YidC

resolves10.1038/nature01047

L23 protein functions as a chaperone docking site on the ribosome

resolves10.1016/j.resmic.2013.03.016

Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways

resolves10.1111/j.1600-0854.2011.01167.x

The Bacterial SRP Receptor, SecA and the Ribosome Use Overlapping Binding Sites on the SecY Translocon

resolves10.1083/jcb.201502103

Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon

resolves10.1007/978-1-4939-6887-9_7

Optimizing E. coli-Based Membrane Protein Production Using Lemo21(DE3) or pReX and GFP-Fusions

resolves10.1074/jbc.271.11.6423

Reinitiation of Protein Translocation across the Endoplasmic Reticulum Membrane for the Topogenesis of Multispanning Membrane Proteins

resolves10.1016/0014-5793(95)00997-N

The functioning of the SRP receptor FtsY in protein‐targeting in E. coli is correlated with its ability to bind and hydrolyse GTP

resolves10.1083/jcb.201004129

Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting

resolves10.1146/annurev.cb.02.110186.001531

Cotranslational and Posttranslational Protein Translocation in Prokaryotic Systems

resolves10.1073/pnas.051484198

The targeting pathway of Escherichia coli presecretory and integral membrane proteins is specified by the hydrophobicity of the targeting signal

resolves10.1016/0092-8674(90)90742-W

The ATPase activity of secA is regulated by acidic phospholipids, secY, and the leader and mature domains of precursor proteins

resolves10.1371/journal.pbio.1001735

Heat Shock Transcription Factor σ32 Co-opts the Signal Recognition Particle to Regulate Protein Homeostasis in E. coli

resolves10.1002/j.1460-2075.1994.tb06511.x

An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY.

resolves10.1111/j.1365-2958.2008.06246.x

An amphiphilic region in the cytoplasmic domain of KdpD is recognized by the signal recognition particle and targeted to the Escherichia coli membrane

resolves10.1016/j.celrep.2016.07.042

A Link between Integral Membrane Protein Expression and Simulated Integration Efficiency

resolves10.1093/nar/gkx888

Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence

resolves10.1038/367657a0

Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor

resolves10.1186/1741-7007-7-76

Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor

resolves10.1038/385365a0

Crystal structure of the NG domain from the signal-recognition particle receptor FtsY

resolves10.1016/S0966-842X(01)02174-6

The Sec protein-translocation pathway

resolves10.1016/S0079-6603(00)66028-2

Protein traffic in bacteria: Multiple routes from the ribosome to and across the membrane

resolves10.1083/jcb.200402067

Role of YidC in folding of polytopic membrane proteins

resolves10.1128/jb.174.7.2185-2192.1992

Small cytoplasmic RNA of Bacillus subtilis: functional relationship with human signal recognition particle 7S RNA and Escherichia coli 4.5S RNA

resolves10.1074/jbc.274.19.13569

Bacillus subtilis Histone-like Protein, HBsu, Is an Integral Component of a SRP-like Particle That Can Bind theAlu Domain of Small Cytoplasmic RNA

resolves10.1002/pro.669

Reprogramming chaperone pathways to improve membrane protein expression in Escherichia coli

resolves10.1007/978-1-61779-921-1_12

Folding Engineering Strategies for Efficient Membrane Protein Production in E. coli

resolves10.1093/emboj/19.23.6419

SRP‐dependent co‐translational targeting and SecA‐dependent translocation analyzed as individual steps in the export of a bacterial protein

resolves10.1126/science.1195691

Translation-Independent Localization of mRNA in E. coli

resolves10.1074/jbc.M117.813469

Improving membrane protein expression by optimizing integration efficiency

resolves10.1016/j.bbamem.2011.08.018

Manipulating the genetic code for membrane protein production: What have we learnt so far?

resolves10.1016/j.febslet.2013.05.063

Improved production of membrane proteins in Escherichia coli by selective codon substitutions

resolves10.7554/eLife.04418

Real-time observation of signal recognition particle binding to actively translating ribosomes

resolves10.1074/jbc.M114.563239

Signal Recognition Particle-ribosome Binding Is Sensitive to Nascent Chain Length

resolves10.1016/j.cell.2011.10.044

Selective Ribosome Profiling Reveals the Cotranslational Chaperone Action of Trigger Factor In Vivo

resolves10.1074/jbc.M705430200

Escherichia coli Signal Recognition Particle Receptor FtsY Contains an Essential and Autonomous Membrane-binding Amphipathic Helix

resolves10.1371/journal.pone.0057370

Downregulation of yidC in Escherichia coli by Antisense RNA Expression Results in Sensitization to Antibacterial Essential Oils Eugenol and Carvacrol

resolves10.1038/nsmb.2919

Local slowdown of translation by nonoptimal codons promotes nascent-chain recognition by SRP in vivo

resolves10.1021/bi011639y

Role of SRP RNA in the GTPase Cycles of Ffh and FtsY

resolves10.1038/nmeth.1701

SignalP 4.0: discriminating signal peptides from transmembrane regions

resolves10.1038/s41598-017-19019-w

The interaction network of the YidC insertase with the SecYEG translocon, SRP and the SRP receptor FtsY

resolves10.1146/annurev.micro.59.030804.121353

DIVERSITY AND EVOLUTION OF PROTEIN TRANSLOCATION

resolves10.1126/science.1072366

Distinct Modes of Signal Recognition Particle Interaction with the Ribosome

resolves10.1093/emboj/16.16.4880

Co‐translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor

resolves10.1016/j.bbamem.2015.06.024

Characterization of the annular lipid shell of the Sec translocon

resolves10.1016/j.jmb.2016.09.001

Membrane Targeting and Insertion of the C-Tail Protein SciP

resolves10.1016/0955-0674(90)90101-J

Translocation of proteins with signal sequences across membranes

resolves10.1038/ncomms15562

Signal recognition particle prevents N-terminal processing of bacterial membrane proteins

resolves10.1146/annurev-cellbio-100616-060439

Structural and Mechanistic Insights into Protein Translocation

resolves10.1016/j.jmb.2014.05.005

SecA Drives Transmembrane Insertion of RodZ, an Unusual Single-Span Membrane Protein

resolves10.1093/nar/gkf468

Prediction of signal recognition particle RNA genes

resolves10.1016/j.jmb.2016.03.022

Protein Elongation, Co-translational Folding and Targeting

resolves10.1038/340478a0

Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP–binding domains

resolves10.1093/nar/gkg107

SRPDB: Signal Recognition Particle Database

resolves10.1074/jbc.M112.446583

YidC Occupies the Lateral Gate of the SecYEG Translocon and Is Sequentially Displaced by a Nascent Membrane Protein

resolves10.1038/s41598-017-00109-8

YidC and SecYEG form a heterotetrameric protein translocation channel

resolves10.1038/35020586

YidC mediates membrane protein insertion in bacteria

resolves10.1038/nsmb.2615

Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding

resolves10.1083/jcb.201311028

Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting

resolves10.1038/nature05182

Structure of the E. coli signal recognition particle bound to a translating ribosome

resolves10.1038/nature19070

Global profiling of SRP interaction with nascent polypeptides

resolves10.1111/j.1751-7915.2009.00148.x

Revolutionizing membrane protein overexpression in bacteria

resolves10.1093/femsre/fuv034

How bacteria maintain location and number of flagella?

resolves10.1093/emboj/19.4.542

YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase

resolves10.1111/mmi.12465

The <scp>C</scp>‐terminal regions of <scp>YidC</scp> from <scp>R</scp>hodopirellula baltica and <scp>O</scp>ceanicaulis alexandrii bind to ribosomes and partially substitute for <scp>SRP</scp> receptor function in <scp>E</scp>scherichia coli

resolves10.1038/nchembio.2169

YidC assists the stepwise and stochastic folding of membrane proteins

resolves10.1371/journal.pbio.0020320

Mechanism of Association and Reciprocal Activation of Two GTPases

resolves10.1074/jbc.M113.506634

Cryo-electron Microscopic Structure of SecA Protein Bound to the 70S Ribosome

resolves10.1038/nsmb1025

RNA-mediated interaction between the peptide-binding and GTPase domains of the signal recognition particle

resolves10.1074/jbc.M110.212340

Lipids Trigger a Conformational Switch That Regulates Signal Recognition Particle (SRP)-mediated Protein Targeting

resolves10.1146/annurev-biochem-070611-102400

Small Proteins Can No Longer Be Ignored

resolves10.1074/jbc.M600205200

SecA Supports a Constant Rate of Preprotein Translocation

resolves10.1038/nrmicro.2016.161

Protein export through the bacterial Sec pathway

resolves10.1038/nature09980

Structure and function of a membrane component SecDF that enhances protein export

resolves10.1093/emboj/17.9.2504

The Escherichia coli SRP and SecB targeting pathways converge at the translocon

resolves10.1016/j.febslet.2004.08.069

F1F0 ATP synthase subunit c is targeted by the SRP to YidC in the E. coli inner membrane

resolves10.1074/jbc.M306527200

SecYEG Proteoliposomes Catalyze the Δϕ-Dependent Membrane Insertion of FtsQ

resolves10.1007/s00018-017-2743-2

Inhibitors of protein translocation across membranes of the secretory pathway: novel antimicrobial and anticancer agents

resolves10.1016/j.molcel.2013.10.005

The Structural Basis of FtsY Recruitment and GTPase Activation by SRP RNA

resolves10.1073/pnas.1424453112

Ribosome–SRP–FtsY cotranslational targeting complex in the closed state

resolves10.1038/nsmb.2546

Structural basis of signal sequence surveillance and selection by the SRP–FtsY complex

resolves10.7554/eLife.07975

Structures of the scanning and engaged states of the mammalian SRP-ribosome complex

resolves10.1073/pnas.0804090105

Tuning Escherichia coli for membrane protein overexpression

resolves10.1083/jcb.91.2.545

Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein.

resolves10.1083/jcb.201704036

SecA mediates cotranslational targeting and translocation of an inner membrane protein

resolves10.1016/j.jmb.2008.01.040

A Cleavable N-Terminal Membrane Anchor is Involved in Membrane Binding of the Escherichia coli SRP Receptor

resolves10.1091/mbc.e11-07-0590

Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by theEscherichia colisignal recognition particle

resolves10.1128/JB.01465-13

YlxM Is a Newly Identified Accessory Protein That Influences the Function of Signal Recognition Particle Pathway Components in Streptococcus mutans

resolves10.1074/jbc.M405490200

Sec/SRP Requirements and Energetics of Membrane Insertion of Subunits a, b, and c of the Escherichia coli F1F0 ATP Synthase

resolves10.1128/mBio.00020-10

Escherichia coli SRP, Its Protein Subunit Ffh, and the Ffh M Domain Are Able To Selectively Limit Membrane Protein Expression When Overexpressed

resolves10.1007/s00018-009-0160-x

Protein transport across and into cell membranes in bacteria and archaea

resolves10.1128/JB.186.17.5956-5960.2004

FlhF, the Third Signal Recognition Particle-GTPase of Bacillus subtilis , Is Dispensable for Protein Secretion

resolves10.1016/j.jmb.2008.05.049

Demonstration of a Multistep Mechanism for Assembly of the SRP·SRP Receptor Complex: Implications for the Catalytic Role of SRP RNA

resolves10.1126/science.1186743

Sequential Checkpoints Govern Substrate Selection During Cotranslational Protein Targeting

resolves10.1073/pnas.1019051108

Direct visualization reveals dynamics of a transient intermediate during protein assembly

resolves10.1371/journal.pone.0092994

Signal Recognition Particle and SecA Cooperate during Export of Secretory Proteins with Highly Hydrophobic Signal Sequences

resolves10.1074/jbc.M113.491613

YidC Protein, a Molecular Chaperone for LacY Protein Folding via the SecYEG Protein Machinery

resolves10.1016/j.jmb.2012.09.026

Both YidC and SecYEG Are Required for Translocation of the Periplasmic Loops 1 and 2 of the Multispanning Membrane Protein TatC

The 6 references without a DOI — listed, not checked

no DOI — not checkedTargeting and insertion of membrane proteins

no DOI — not checkedCotranslational signal-independent SRP preloading during membrane targeting

no DOI — not checkedTargeting and integration of bacterial membrane proteins

no DOI — not checkedSRP, FtsY, DnaK and YidC are required for the biogenesis of the E. coli tail-anchored membrane proteins DjlC and Flk

no DOI — not checkedAntibiotic targeting of the bacterial secretory pathway

no DOI — not checkedSignals for protein targeting into and across membranes

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