Reference health
Compensating complete loss of signal recognition particle during co-translational protein targeting by the translation speed and accuracy
68/68 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 68 checked references that resolve
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Signal Recognition Particle: An Essential Protein-Targeting Machine
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Physiological Basis for Conservation of the Signal Recognition Particle Targeting Pathway in
<i>Escherichia coli</i>
resolves10.1073/pnas.90.11.5229
Functional substitution of the signal recognition particle 54-kDa subunit by its Escherichia coli homolog.
resolves10.1038/nsmb.1402
Signal sequence–independent membrane targeting of ribosomes containing short nascent peptides within the exit tunnel
resolves10.1038/s41467-017-01492-6
A conformational switch in initiation factor 2 controls the fidelity of translation initiation in bacteria
resolves10.1021/pr050300l
Normalization Approaches for Removing Systematic Biases Associated with Mass Spectrometry and Label-Free Proteomics
resolves10.1038/nature19309
Cotranslational signal-independent SRP preloading during membrane targeting
resolves10.1038/nmeth735
Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase
resolves10.1128/mBio.02375-17
Slowdown of Translational Elongation in
<i>Escherichia coli</i>
under Hyperosmotic Stress
resolves10.1038/nmicrobiol.2016.231
Reduction of translating ribosomes enables Escherichia coli to maintain elongation rates during slow growth
resolves10.1016/j.sbi.2005.03.007
Targeting proteins to membranes: structure of the signal recognition particle
resolves10.1074/jbc.M300173200
Signal Recognition Particle Binds to Ribosome-bound Signal Sequences with Fluorescence-detected Subnanomolar Affinity That Does Not Diminish as the Nascent Chain Lengthens
resolves10.7554/eLife.03440
mRNA-programmed translation pauses in the targeting of E. coli membrane proteins
resolves10.1016/S0021-9258(17)36095-7
Structure and expression of the gene locus encoding the phosphatidylglycerophosphate synthase of Escherichia coli.
resolves10.1128/JB.01146-06
Membrane Composition Changes and Physiological Adaptation by<i>Streptococcus mutans</i>Signal Recognition Particle Pathway Mutants
resolves10.1016/0092-8674(88)90057-8
A novel role for cAMP in the control of the activity of the E. coli chromosome replication initiator protein, DnaA
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Biotinylation in vivo as a sensitive indicator of protein secretion and membrane protein insertion
resolves10.1186/s12014-018-9201-5
Comparison of iTRAQ and SWATH in a clinical study with multiple time points
resolves10.1128/JB.182.2.371-376.2000
Viability of an
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Null Mutant Lacking Detectable Phosphatidylglycerol and Cardiolipin
resolves10.1128/JB.183.8.2543-2552.2001
Characterization of the
<i>sat</i>
Operon in
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Suppression of growth and protein secretion defects in Escherichia coli secA mutants by decreasing protein synthesis
resolves10.1073/pnas.051484198
The targeting pathway of
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presecretory and integral membrane proteins is specified by the hydrophobicity of the targeting signal
resolves10.1073/pnas.1520337112
Initiation factor 2 stabilizes the ribosome in a semirotated conformation
resolves10.1109/TCBB.2012.120
On the Steady-State Distribution in the Homogeneous Ribosome Flow Model
resolves10.1093/emboj/19.15.4164
Elongation arrest is a physiologically important function of signal recognition particle
resolves10.1038/nmicrobiol.2017.117
Translational fidelity and mistranslation in the cellular response to stress
resolves10.1091/mbc.12.3.577
Multifaceted Physiological Response Allows Yeast to Adapt to the Loss of the Signal Recognition Particle-dependent Protein-targeting Pathway
resolves10.1111/j.1432-1033.1977.tb11223.x
The Effect of Initiation Factor IF‐1 on the Dissociation of 70‐S Ribosomes of <i>Escherichia coli</i>
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
resolves10.1083/jcb.134.2.269
Signal sequences specify the targeting route to the endoplasmic reticulum membrane.
resolves10.1093/nar/25.6.1185
Decoding fidelity at the ribosomal A and P sites: influence of mutations in three different regions of the decoding domain in 16S rRNA
resolves10.1038/359744a0
The E. coli ffh gene is necessary for viability and efficient protein export
resolves10.1080/09687860400026348
Signal recognition particles in chloroplasts, bacteria, yeast and mammals (Review)
resolves10.1093/emboj/16.16.4880
Co‐translational protein targeting catalyzed by the Escherichia coli signal recognition particle and its receptor
resolves10.1016/j.celrep.2017.06.028
Post-termination Ribosome Intermediate Acts as the Gateway to Ribosome Recycling
resolves10.1128/JB.187.5.1632-1638.2005
Transcriptional Polarity in rRNA Operons of
<i>Escherichia coli nusA</i>
and
<i>nusB</i>
Mutant Strains
resolves10.1073/pnas.1817299116
Protein synthesis rates and ribosome occupancies reveal determinants of translation elongation rates
resolves10.1126/science.1192588
Interdependence of Cell Growth and Gene Expression: Origins and Consequences
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
resolves10.1016/j.jmb.2009.12.042
Slowing Bacterial Translation Speed Enhances Eukaryotic Protein Folding Efficiency
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
resolves10.1083/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.cellbio.10.1.87
Signal Sequence Recognition and Protein Targeting to the Endoplasmic Reticulum Membrane
resolves10.1074/jbc.M109.081935
Consequences of Depletion of the Signal Recognition Particle in Escherichia coli
resolves10.1021/ac300006b
Consecutive Proteolytic Digestion in an Enzyme Reactor Increases Depth of Proteomic and Phosphoproteomic Analysis
resolves10.1534/g3.116.032227
Depletion of Shine-Dalgarno Sequences Within Bacterial Coding Regions Is Expression Dependent
resolves10.1109/TCBB.2013.120
Explicit Expression for the Steady-State Translation Rate in the Infinite-Dimensional Homogeneous Ribosome Flow Model
resolves10.1109/TCBB.2014.2330621
Maximizing Protein Translation Rate in the Ribosome Flow Model: The Homogeneous Case
resolves10.1016/S0079-6603(08)60256-1
Diverse Mechanisms for Regulating Ribosomal Protein Synthesis in Escherichia coli
resolves10.1074/jbc.M111.325001
Translation Elongation Regulates Substrate Selection by the Signal Recognition Particle
resolves10.1074/mcp.M111.011585
Novel Proteomic Tools Reveal Essential Roles of SRP and Importance of Proper Membrane Protein Biogenesis
resolves10.1146/annurev-biophys-051013-022653
Fidelity of Cotranslational Protein Targeting by the Signal Recognition Particle
resolves10.1093/nar/gkw698
Real time determination of bacterial<i>in vivo</i>ribosome translation elongation speed based on LacZα complementation system
The 5 references without a DOI — listed, not checked
no DOI — not checkedContributions of the N- and C-Terminal Domains of Initiation Factor 3 to Its Functions in the Fidelity of Initiation and Antiassociation of the Ribosomal Subunits
no DOI — not checkedAutogenous and post-transcriptional regulation of RNA polymerase synthesis
no DOI — not checkedMiller, J.H. (1972). Experiments in molecular Genetucs (Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory Press).
no DOI — not checkedThe affinity of signal recognition particle for presecretory proteins is dependent on nascent chain length
no DOI — not checkedSignal Recognition Particle Suppressor Screening Reveals the Regulation of Membrane Protein Targeting by the Translation Rate
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