Reference health
New prospects in studying the bacterial signal recognition particle pathway
114/114 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.
5 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 114 checked references that resolve
resolves10.1016/s1369-5274(99)80003-4
Type III machines of Gram-negative pathogens: injecting virulence factors into host cells and more
resolves10.1038/381248a0
Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting
resolves10.1083/jcb.146.4.723
The Ribosome Regulates the Gtpase of the β-Subunit of the Signal Recognition Particle Receptor
resolves10.1126/science.287.5456.1232
Crystal Structure of the Ribonucleoprotein Core of the Signal Recognition Particle
resolves10.1093/emboj/19.1.134
Discrimination between SRP‐ and SecA/SecB‐dependent substrates involves selective recognition of nascent chains by SRP and trigger factor
resolves10.1038/73265
resolves10.1038/340482a0
Model for signal sequence recognition from amino-acid sequence of 54K subunit of signal recognition particle
resolves10.1073/pnas.90.11.5229
Functional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homolog.
resolves10.1016/0166-6851(93)90198-7
Identification of a tRNA-like molecule that copurifies with the 7SL RNA of Trypanosoma brucei
resolves10.1083/jcb.67.3.835
Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma.
resolves10.1083/jcb.67.3.852
Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components.
resolves10.1074/jbc.271.36.22256
Chaperonin-promoted Post-translational Membrane Insertion of a Multispanning Membrane Protein Lactose Permease
resolves10.1242/jcs.109.11.2601
The signal recognition particle and related small cytoplasmic ribonucleoprotein particles
resolves10.1016/0092-8674(87)90620-9
Mutations in the gene for EF-G reduce the requirement for 4.5S RNA in the growth of E. coli
resolves10.1016/0022-2836(84)90237-7
The 4.5 S RNA gene of Escherichia coli is essential for cell growth
resolves10.1515/BC.1999.021
New Insights into Signal Recognition and Elongation Arrest Activities of the Signal Recognition Particle
resolves10.1006/bbrc.1996.1582
Bacillus subtilisFfh, A Homologue of Mammalian SRP54, Can Intrinsically Bind to the Precursors of Secretory Proteins
resolves10.1093/oxfordjournals.jbchem.a022252
Enhancing Effect of Bacillus subtilis Ffh, a Homologue of the SRP54 Subunit of the Mammalian Signal Recognition Particle, on the Binding of Sec A to Precursors of Secretory Proteins In Vitro
resolves10.1074/jbc.274.29.20068
The Signal Recognition Particle-targeting Pathway Does Not Necessarily Deliver Proteins to the Sec-translocase inEscherichia coli
resolves10.1016/S0167-4838(98)00045-4
Binding of GTP and GDP induces a significant conformational change in the GTPase domain of Ffh, a bacterial homologue of the SRP 54 kDa subunit
resolves10.1038/11572
resolves10.1016/s0014-5793(96)01354-3
Assembly of a cytoplasmic membrane protein in <i>Escherichia coli</i> is dependent on the signal recognition particle
resolves10.1007/BF00327204
The Escherichia coli cell division proteins FtsY, FtsE and FtsX are inner membrane-associated
resolves10.1099/13500872-145-2-357
Streptococcus mutans ffh, a gene encoding a homologue of the 54 kDa subunit of the signal recognition particle, is involved in resistance to acid stress
resolves10.1002/j.1460-2075.1995.tb00235.x
A complex of the signal sequence binding protein and the SRP RNA promotes translocation of nascent proteins.
resolves10.1073/pnas.080077197
Association of
<i>Escherichia coli</i>
ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle
resolves10.1021/bi981523a
Interaction of Guanine Nucleotides with the Signal Recognition Particle from <i>Escherichia coli</i>
resolves10.1006/jmbi.1999.3427
Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP
resolves10.1128/jb.176.23.7148-7154.1994
Concentrations of 4.5S RNA and Ffh protein in Escherichia coli: the stability of Ffh protein is dependent on the concentration of 4.5S RNA
resolves10.1016/S0969-2126(00)00137-4
Crystal structure of the Ffh and EF-G binding sites in the conserved domain IV of Escherichia coli 4.5S RNA
resolves10.1007/BF00425687
Molecular cloning and nucleotide sequence of the HU-1 gene of Escherichia coli
resolves10.1016/S0092-8674(00)81418-X
Crystal Structure of the Signal Sequence Binding Subunit of the Signal Recognition Particle
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>
resolves10.1074/jbc.271.22.13140
Identification of a Region of Bacillus subtilis Ffh, a Homologue of Mammalian SRP54 Protein, That Is Essential for Binding to Small Cytoplasmic RNA
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/s0378-1119(97)00425-3
A GTP-binding protein of Mycoplasma hominis: a small sized homolog to the signal recognition particle receptor FtsY
resolves10.1016/0014-5793(78)80535-3
The amino‐ and carboxy‐terminal amino acid sequences of protein HU from <i>Escherichia coli</i>
resolves10.1093/emboj/19.4.531
Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity
resolves10.1016/S0021-9258(19)61528-0
Nucleotide-dependent Binding of the GTPase Domain of the Signal Recognition Particle Receptor β-Subunit to the α-Subunit
resolves10.1111/j.1365-2958.1994.tb00284.x
Mammalian and <i>Escherichia coli</i> signal recognition particles
resolves10.1038/359741a0
Signal-sequence recognition by an Escherichia coli ribonucleoprotein complex
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.1432-1033.1995.766_3.x
The Functional Integration of a Polytopic Membrane Protein of <i>Escherichia coli</i> is Dependent on the Bacterial Signal‐Recognition Particle
resolves10.1046/j.1365-2958.1997.3551729.x
Ffh and FtsY in a <i>Mycoplasma mycoides</i> signal‐recognition particle pathway: SRP RNA and M domain of Ffh are not required for stimulation of GTPase activity <i>in vitro</i>
resolves10.1093/emboj/19.15.4164
Elongation arrest is a physiologically important function of signal recognition particle
resolves10.1038/367657a0
Interaction of E. coli Ffh/4.5S ribonucleoprotein and FtsY mimics that of mammalian signal recognition particle and its receptor
resolves10.1016/S0092-8674(00)80248-2
Switching the Model: A Concerted Mechanism for GTPases in Protein Targeting
resolves10.1074/jbc.274.47.33227
A Site-specific, Membrane-dependent Cleavage Event Defines the Membrane Binding Domain of FtsY
resolves10.1038/385365a0
Crystal structure of the NG domain from the signal-recognition particle receptor FtsY
resolves10.1016/S0969-2126(00)00131-3
The crystal structure of the conserved GTPase of SRP54 from the archaeon Acidianus ambivalens and its comparison with related structures suggests a model for the SRP–SRP receptor complex
resolves10.1073/pnas.94.21.11339
The signal recognition particle receptor of
<i>Escherichia coli</i>
(FtsY) has a nucleotide exchange factor built into the GTPase domain
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
resolves10.1006/bbrc.1994.1385
The Bacillus subtilis SRP54 Homologue, Ffh, Has an Intrinsic GTPase Activity and Forms a Ribonucleoprotein Complex with Small Cytoplasmic RNA in Vivo
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
resolves10.1128/JB.181.15.4561-4567.1999
The Structure of Multiple Polypeptide Domains Determines the Signal Recognition Particle Targeting Requirement of
<i>Escherichia coli</i>
Inner Membrane Proteins
resolves10.1016/0378-1119(96)00181-3
The effect of Srb, a homologue of the mammalian SRP receptor α-subunit, on Bacillus subtilis growth and protein translocation
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
resolves10.1016/0092-8674(88)90003-7
Human SRP RNA and E. coli 4.5S RNA contain a highly homologous structural domain
resolves10.1126/science.1701272
An
<i>E. coli</i>
Ribonucleoprotein Containing 4.5
<i>S</i>
RNA Resembles Mammalian Signal Recognition Particle
resolves10.1126/science.7660124
Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases
resolves10.1093/emboj/16.16.4880
Co‐translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor
resolves10.1016/0076-6879(83)97120-3
[7] Preparation of free and membrane-bound polysomes from Escherichia coli
resolves10.1016/S0092-8674(00)80253-6
Empty Site Forms of the SRP54 and SRα GTPases Mediate Targeting of Ribosome–Nascent Chain Complexes to the Endoplasmic Reticulum
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
resolves10.1038/340478a0
Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP–binding domains
resolves10.1016/S0167-4781(96)00236-9
Identification of a gene in the euryarchaeal Thermococcus species AN1 encoding a protein homologous to the alpha subunit of the eukaryal signal recognition particle (SRP) receptor
resolves10.1016/0167-4889(95)00034-P
The GTPase activity of the Escherichia coli Ffh protein is important for normal growth
resolves10.1038/10683
resolves10.1073/pnas.95.17.10312
A novel signal recognition particle targets light-harvesting proteins to the thylakoid membranes
resolves10.1093/emboj/19.4.542
YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase
resolves10.1074/jbc.M004462200
The Fate of Membrane-bound Ribosomes Following the Termination of Protein Synthesis
resolves10.1074/jbc.272.4.2053
FtsY, the Prokaryotic Signal Recognition Particle Receptor Homologue, Is Essential for Biogenesis of Membrane Proteins
resolves10.1074/jbc.271.22.13162
Identification of Protein Synthesis Elongation Factor G as a 4.5 S RNA-binding Protein in Escherichia coli
resolves10.1083/jcb.100.6.1913
Elongation arrest is not a prerequisite for secretory protein translocation across the microsomal membrane.
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
resolves10.1128/MCB.11.8.3949
Binding sites of the 9- and 14-kilodalton heterodimeric protein subunit of the signal recognition particle (SRP) are contained exclusively in the Alu domain of SRP RNA and contain a sequence motif that is conserved in evolution.
resolves10.1093/nar/16.15.7740
Common structural features between eukaryotic 7SL RNAs, eubacterial 4.5S RNA and scRNA and archaebacterial 7S RNA
resolves10.1016/s0378-1097(99)00498-x
Analysis of Escherichia coli 4.5S RNA binding affinity to Ffh and EF-G
resolves10.1016/0076-6879(83)97119-7
[6] Synthesis of proteins by membrane-associated polysomes and free polysomes
resolves10.1111/j.1432-1033.1997.00575.x
Identification of a Region Required for Binding to Presecretory Protein in <i>Bacillus Subtilis</i> Ffh, A Homologue of the 54‐kDa Subunit of Mammalian Signal Recognition Particle
resolves10.1093/nar/25.10.1920
A truncation in the 14 kDa protein of the signal recognition particle leads to tertiary structure changes in the RNA and abolishes the elongation arrest activity of the particle
resolves10.1073/pnas.090087297
A mutant hunt for defects in membrane protein assembly yields mutations affecting the bacterial signal recognition particle and Sec machinery
resolves10.1016/S0092-8674(00)81839-5
The E. coli Signal Recognition Particle Is Required for the Insertion of a Subset of Inner Membrane Proteins
resolves10.1002/j.1460-2075.1995.tb00236.x
Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.
resolves10.1093/emboj/17.9.2504
The Escherichia coli SRP and SecB targeting pathways converge at the translocon
resolves10.1083/jcb.91.2.551
Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein.
resolves10.1083/jcb.91.2.557
Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes.
resolves10.1146/annurev.cb.10.110194.000511
Signal Sequence Recognition and Protein Targeting to the Endoplasmic Reticulum Membrane
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.109.6.2617
Signal recognition particle mediates a transient elongation arrest of preprolactin in reticulocyte lysate.
resolves10.1093/nar/20.22.5919
Evolutionary conserved nucleotides within the<i>E.coli</i>4.5S RNA are required for association with P48<i>in vitro</i>and for optimal function<i>in vivo</i>
resolves10.1002/j.1460-2075.1996.tb00345.x
The signal recognition particle receptor alpha subunit assembles co‐translationally on the endoplasmic reticulum membrane during an mRNA‐encoded translation pause in vitro.
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
resolves10.1016/S1097-2765(00)80009-X
Domain Interactions in E. coli SRP: Stabilization of M Domain by RNA Is Required for Effective Signal Sequence Modulation of NG Domain
The 5 references without a DOI — listed, not checked
no DOI — not checkedPutative integral membrane SRP receptors
no DOI — not checked4.5S RNA: does form predict function?
no DOI — not checkedStructure of 4.5S RNA in the signal recognition particle of Escherichia coli as studied by enzymatic and chemical probing
no DOI — not checkedResponse to ‘sequence‐gazing?’
no DOI — not checkedSignal recognition and protein targeting to the endoplasmic reticulum membrane
What this badge says. CiteStamped means the CHECKABLE references of this
work were clean at the dated check: each resolved to a known work in a public registry, and none
carried a retraction notice at that time. It says nothing about the quality, findings,
or importance of the work itself, and nothing about references deposited without a DOI.
checked 2026-07-22 — re-checked daily as this page is visited; titles and statuses come from Crossref and DataCite and are not part of the signed record
Embed this badge
Both snippets point at the live badge image and link back to this page. The badge re-renders from the daily check, so an embed never goes stale by more than a day of visits.
<a href="https://citestamp.com/citestamped/10.1046/j.1365-2958.2000.02198.x"><img src="https://citestamp.com/citestamped/10.1046/j.1365-2958.2000.02198.x/badge.svg" alt="CiteStamped reference-health badge" width="460" height="64"></a>
[](https://citestamp.com/citestamped/10.1046/j.1365-2958.2000.02198.x)