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Signal sequence–independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle
87/87 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 87 checked references that resolve
resolves10.1074/jbc.M201711200
Separate Analysis of Twin-arginine Translocation (Tat)-specific Membrane Binding and Translocation in Escherichia coli
resolves10.1083/jcb.200606093
Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
resolves10.1038/sj.embor.7400385
FtsY, the bacterial signal‐recognition particle receptor, interacts functionally and physically with the SecYEG translocon
resolves10.1126/science.1196473
The Crystal Structure of the Signal Recognition Particle in Complex with Its Receptor
resolves10.1074/jbc.M705429200
Membrane Targeting of Ribosomes and Their Release Require Distinct and Separable Functions of FtsY
resolves10.1016/j.bbamem.2010.07.025
Early targeting events during membrane protein biogenesis in Escherichia coli
resolves10.1083/jcb.200803097
To flip or not to flip: lipid–protein charge interactions are a determinant of final membrane protein topology
resolves10.1016/0022-2836(73)90037-5
In vitro exchange of ribosomal subunits between free and membrane-bound ribosomes
resolves10.1038/nsmb.1402
Signal sequence–independent membrane targeting of ribosomes containing short nascent peptides within the exit tunnel
resolves10.1091/mbc.e08-08-0886
Visualization of Distinct Entities of the SecYEG Translocon during Translocation and Integration of Bacterial Proteins
resolves10.1016/j.jmb.2009.04.061
Two Cooperating Helices Constitute the Lipid-binding Domain of the Bacterial SRP Receptor
resolves10.1128/JB.00208-09
Depletion of the Signal Recognition Particle Receptor Inactivates Ribosomes in
<i>Escherichia coli</i>
resolves10.1261/rna.1285609
Conformation of the signal recognition particle in ribosomal targeting complexes
resolves10.1083/jcb.200408188
Identification of cytoplasmic residues of Sec61p involved in ribosome binding and cotranslational translocation
resolves10.1093/emboj/20.10.2462
Projection structure and oligomeric properties of a bacterial core protein translocase
resolves10.1093/emboj/19.4.531
Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity
resolves10.1038/334173a0
Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes
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
resolves10.1371/journal.pone.0003619
Structures of the Signal Recognition Particle Receptor from the Archaeon Pyrococcus furiosus: Implications for the Targeting Step at the Membrane
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
resolves10.1093/emboj/20.9.2338
SRβ coordinates signal sequence release from SRP with ribosome binding to the translocon
resolves10.1038/nsmb.1994
Structural basis of signal-sequence recognition by the signal recognition particle
resolves10.1038/nature05326
Following the signal sequence from ribosomal tunnel exit to signal recognition particle
resolves10.1126/science.1124864
Signal Recognition Particle Receptor Exposes the Ribosomal Translocon Binding Site
resolves10.1074/jbc.C300180200
The β-Subunit of the Protein-conducting Channel of the Endoplasmic Reticulum Functions as the Guanine Nucleotide Exchange Factor for the β-Subunit of the Signal Recognition Particle Receptor
resolves10.1017/S1355838201002205
Important role of the tetraloop region of 4.5S RNA in SRP binding to its receptor FtsY
resolves10.1006/jmbi.1999.3427
Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP
resolves10.1083/jcb.200707196
An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation
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 of<i>Escherichia coli</i>
resolves10.1007/s10254-002-0002-9
Signal recognition particle-depencent protein targeting, universal to all kingdoms of life
resolves10.1111/j.1600-0854.2011.01167.x
The Bacterial SRP Receptor, SecA and the Ribosome Use Overlapping Binding Sites on the SecY Translocon
resolves10.1016/j.jmb.2005.11.039
Multi-step Assembly Pathway of the cbb3-type Cytochrome c Oxidase Complex
resolves10.1083/jcb.201004129
Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting
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
resolves10.1002/j.1460-2075.1994.tb06511.x
An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY.
resolves10.1074/jbc.M900775200
The Membrane-binding Motif of the Chloroplast Signal Recognition Particle Receptor (cpFtsY) Regulates GTPase Activity
resolves10.1128/JB.182.12.3377-3382.2000
A Mutation in
<i>secY</i>
That Causes Enhanced SecA Insertion and Impaired Late Functions in Protein Translocation
resolves10.1186/1741-7007-7-76
Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor
resolves10.1038/nsmb.1467
SRP RNA controls a conformational switch regulating the SRP–SRP receptor interaction
resolves10.1091/mbc.9.1.103
Binding of Signal Recognition Particle Gives Ribosome/Nascent Chain Complexes a Competitive Advantage in Endoplasmic Reticulum Membrane Interaction
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
resolves10.1074/jbc.M608228200
A Derivative of Lipid A Is Involved in Signal Recognition Particle/SecYEG-dependent and -independent Membrane Integrations
resolves10.1371/journal.pbio.0050322
The Signal Sequence Coding Region Promotes Nuclear Export of mRNA
resolves10.1074/jbc.M705430200
Escherichia coli Signal Recognition Particle Receptor FtsY Contains an Essential and Autonomous Membrane-binding Amphipathic Helix
resolves10.1126/science.288.5471.1640
Role of 4.5
<i>S</i>
RNA in Assembly of the Bacterial Signal Recognition Particle with Its Receptor
resolves10.1038/359744a0
The E. coli ffh gene is necessary for viability and efficient protein export
resolves10.1126/science.1701272
An
<i>E. coli</i>
Ribonucleoprotein Containing 4.5
<i>S</i>
RNA Resembles Mammalian Signal Recognition Particle
resolves10.1074/jbc.M005294200
Regulation of Ribosome Detachment from the Mammalian Endoplasmic Reticulum Membrane
resolves10.1016/S0962-8924(00)01905-X
Ribosome exchange revisited: a mechanism for translation-coupled ribosome detachment from the ER membrane
resolves10.1093/emboj/16.16.4880
Co‐translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor
resolves10.1073/pnas.0902029106
Studying membrane proteins through the eyes of the genetic code revealed a strong uracil bias in their coding mRNAs
resolves10.1093/emboj/19.8.1900
Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA
resolves10.1261/rna.721108
Signal sequence- and translation-independent mRNA localization to the endoplasmic reticulum
resolves10.1091/mbc.9.1.117
Signal Recognition Particle-dependent Targeting of Ribosomes to the Rough Endoplasmic Reticulum in the Absence and Presence of the Nascent Polypeptide-associated Complex
resolves10.1038/nature06384
Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
resolves10.1016/0092-8674(90)90454-M
E. coli 4.5S RNA is part of a ribonucleoprotein particle that has properties related to signal recognition particle
resolves10.1074/jbc.M709871200
Cardiolipin Controls the Osmotic Stress Response and the Subcellular Location of Transporter ProP in Escherichia coli
resolves10.1038/nature05182
Structure of the E. coli signal recognition particle bound to a translating ribosome
resolves10.1091/mbc.e06-05-0439
Ribosome Binding to and Dissociation from Translocation Sites of the Endoplasmic Reticulum Membrane
resolves10.1074/jbc.M004462200
The Fate of Membrane-bound Ribosomes Following the Termination of Protein Synthesis
resolves10.1083/jcb.200702018
Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation
resolves10.1021/bi9006989
Signal Recognition Particle (SRP) and SRP Receptor: A New Paradigm for Multistate Regulatory GTPases
resolves10.1371/journal.pbio.0020320
Mechanism of Association and Reciprocal Activation of Two GTPases
resolves10.1016/j.febslet.2004.11.049
Co‐translational protein targeting by the signal recognition particle
resolves10.1073/pnas.1002968107
Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting
resolves10.1016/S0092-8674(00)80669-8
Role of Sec61α in the Regulated Transfer of the Ribosome–Nascent Chain Complex from the Signal Recognition Particle to the Translocation Channel
resolves10.1083/jcb.97.6.1693
Subcellular distribution of signal recognition particle and 7SL-RNA determined with polypeptide-specific antibodies and complementary DNA probe.
resolves10.1016/j.jmb.2008.01.040
A Cleavable N-Terminal Membrane Anchor is Involved in Membrane Binding of the Escherichia coli SRP Receptor
resolves10.1016/j.bbabio.2009.02.012
Role of phospholipids in respiratory cytochrome bc1 complex catalysis and supercomplex formation
resolves10.1073/pnas.0808573106
Multiple conformational switches in a GTPase complex control co-translational protein targeting
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