Reference health
Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites
48/48 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.
1 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.
The 48 checked references that resolve
resolves10.1038/sj.embor.7400385
FtsY, the bacterial signal‐recognition particle receptor, interacts functionally and physically with the SecYEG translocon
resolves10.1038/340482a0
Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
resolves10.1016/S0021-9258(18)54245-9
Characterization of membrane-associated and soluble states of SecA protein from wild-type and SecA51(TS) mutant strains of Escherichia coli.
resolves10.1074/jbc.M509647200
A Dual Function for SecA in the Assembly of Single Spanning Membrane Proteins in Escherichia coli
resolves10.1093/emboj/19.4.531
Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity
resolves10.1021/bi9605088
Domain Interactions of the Peripheral Preprotein <i>Translocase</i> Subunit SecA
resolves10.1093/emboj/cdg418
Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase
resolves10.1016/S0092-8674(94)90582-7
SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion
resolves10.1016/j.sbi.2005.03.007
Targeting proteins to membranes: structure of the signal recognition particle
resolves10.1128/JB.186.8.2492-2494.2004
The Core<i>Escherichia coli</i>Signal Recognition Particle Receptor Contains Only the N and G Domains of FtsY
resolves10.1083/jcb.93.1.97
Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum.
resolves10.1093/emboj/20.9.2338
SRβ coordinates signal sequence release from SRP with ribosome binding to the translocon
resolves10.1083/jcb.95.2.470
Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor.
resolves10.1016/j.sbi.2005.01.013
The signal recognition particle and its interactions during protein targeting
resolves10.1126/science.1124864
Signal Recognition Particle Receptor Exposes the Ribosomal Translocon Binding Site
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
resolves10.1074/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
resolves10.1093/embo-reports/kve226
Evidence for coupling of membrane targeting and function of the signal recognition particle (SRP) receptor FtsY
resolves10.1083/jcb.150.3.689
Dissecting the Translocase and Integrase Functions of the <i>Escherichia coli</i> Secyeg Translocon
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
resolves10.1016/0014-5793(95)00997-N
The functioning of the SRP receptor FtsY in protein‐targeting in <i>E. coli</i> is correlated with its ability to bind and hydrolyse GTP
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
resolves10.1093/emboj/20.23.6724
Evidence for a novel GTPase priming step in the SRP protein targeting pathway
resolves10.1002/j.1460-2075.1994.tb06511.x
An alternative protein targeting pathway in Escherichia coli: studies on the role of FtsY.
resolves10.1083/jcb.200303143
Dual recognition of the ribosome and the signal recognition particle by the SRP receptor during protein targeting to the endoplasmic reticulum
resolves10.1093/emboj/16.21.6384
SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane
resolves10.1074/jbc.274.47.33227
A Site-specific, Membrane-dependent Cleavage Event Defines the Membrane Binding Domain of FtsY
resolves10.1074/jbc.M011331200
FtsY Binds to the Escherichia coli Inner Membrane via Interactions with Phosphatidylethanolamine and Membrane Proteins
resolves10.1083/jcb.200307067
Functional interaction of chloroplast SRP/FtsY with the ALB3 translocase in thylakoids
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.273.20.12451
A Mutation in the Escherichia coli secY Gene That Produces Distinct Effects on Inner Membrane Protein Insertion and Protein Export
resolves10.1093/emboj/16.16.4880
Co‐translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor
resolves10.1111/j.1365-2958.1996.tb02487.x
Integration of SecA protein into the <i>Escherichia coli</i> inner membrane is regulated by its amino‐terminal ATP‐binding domain
resolves10.1038/340478a0
Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP–binding domains
resolves10.1016/S0091-679X(01)65014-3
Chapter 13 Blue-native gels to isolate protein complexes from mitochondria
resolves10.1016/S0092-8674(03)00161-2
Structural Basis for the Function of the β Subunit of the Eukaryotic Signal Recognition Particle Receptor
resolves10.1074/jbc.274.42.29883
SecA Is Not Required for Signal Recognition Particle-mediated Targeting and Initial Membrane Insertion of a Nascent Inner Membrane Protein
resolves10.1371/journal.pbio.0020320
Mechanism of Association and Reciprocal Activation of Two GTPases
resolves10.1074/jbc.271.21.12394
Insertion of the Polytopic Membrane Protein MalF Is Dependent on the Bacterial Secretion Machinery
resolves10.1093/emboj/17.9.2504
The Escherichia coli SRP and SecB targeting pathways converge at the translocon
resolves10.1073/pnas.94.12.6025
The NG domain of the prokaryotic signal recognition particle receptor, FtsY, is fully functional when fused to an unrelated integral membrane polypeptide
The 1 reference without a DOI — listed, not checked
no DOI — not checked2023072907550713300_BIB35
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