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Evidence for a cytoplasmic pool of ribosome-free mRNAs encoding inner membrane proteins in Escherichia coli

https://doi.org/10.1371/journal.pone.0183862
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51/51 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.

4 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 51 checked references that resolve
resolves10.1016/j.cbpa.2015.09.016
Dynamics of co-translational protein targeting
resolves10.1016/j.jmb.2016.03.022
Protein Elongation, Co-translational Folding and Targeting
resolves10.7554/eLife.13065
Spatial organization shapes the turnover of a bacterial transcriptome
resolves10.1016/j.tibs.2011.09.004
Is there a twist in the Escherichia coli signal recognition particle pathway?
resolves10.1371/journal.pbio.1001336
p180 Promotes the Ribosome-Independent Localization of a Subset of mRNA to the Endoplasmic Reticulum
resolves10.1016/j.tig.2014.07.002
mRNA transport meets membrane traffic
resolves10.1091/mbc.E13-01-0038
Translation- and SRP-independent mRNA targeting to the endoplasmic reticulum in the yeast <i>Saccharomyces cerevisiae</i>
resolves10.1126/science.1195691
Translation-Independent Localization of mRNA in <i>E. coli</i>
resolves10.1016/j.tcb.2007.11.005
Message on the web: mRNA and ER co-trafficking
resolves10.1016/S0378-1119(01)00674-6
Structural and functional features of eukaryotic mRNA untranslated regions
resolves10.1038/nrg2695
Prokaryotic transcriptomics: a new view on regulation, physiology and pathogenicity
resolves10.1126/science.aad9822
Term-seq reveals abundant ribo-regulation of antibiotics resistance in bacteria
resolves10.1073/pnas.0902029106
Studying membrane proteins through the eyes of the genetic code revealed a strong uracil bias in their coding mRNAs
resolves10.1371/journal.pone.0134413
Model Uracil-Rich RNAs and Membrane Protein mRNAs Interact Specifically with Cold Shock Proteins in Escherichia coli
resolves10.1016/S0301-4622(02)00021-2
Formation of 70S ribosomes: large activation energy is required for the adaptation of exclusively the small ribosomal subunit
resolves10.1093/emboj/19.8.1900
Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA
resolves10.1016/S0079-6603(08)00805-2
Chapter 5 The Role of 3′–5′ Exoribonucleases in RNA Degradation
resolves10.1016/S0079-6603(08)00803-9
Chapter 3 Endonucleolytic Initiation of mRNA Decay in Escherichia coli
resolves10.1016/j.bbamem.2010.07.025
Early targeting events during membrane protein biogenesis in Escherichia coli
resolves10.1016/j.bbamcr.2013.02.021
Co-translational targeting and translocation of proteins to the endoplasmic reticulum
resolves10.1074/jbc.272.4.2053
FtsY, the Prokaryotic Signal Recognition Particle Receptor Homologue, Is Essential for Biogenesis of Membrane Proteins
resolves10.1371/journal.pone.0009130
Membrane Protein Biogenesis in Ffh- or FtsY-Depleted Escherichia coli
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
resolves10.1083/jcb.200204144
Accumulation of endoplasmic membranes and novel membrane-bound ribosome–signal recognition particle receptor complexes in<i>Escherichia coli</i>
resolves10.1074/jbc.M110.140921
Genetic Evidence for Functional Interaction of the Escherichia coli Signal Recognition Particle Receptor with Acidic Lipids in Vivo
resolves10.1074/jbc.M109.081935
Consequences of Depletion of the Signal Recognition Particle in Escherichia coli
resolves10.1128/JB.00208-09
Depletion of the Signal Recognition Particle Receptor Inactivates Ribosomes in <i>Escherichia coli</i>
resolves10.1038/nsmb1150
Structural analysis of kasugamycin inhibition of translation
resolves10.1371/journal.pone.0168143
Effects of Kasugamycin on the Translatome of Escherichia coli
resolves10.1099/mic.0.052209-0
Bacterial adaptation to cold
resolves10.1007/s00018-007-6388-4
Structure and function of bacterial cold shock proteins
resolves10.1074/jbc.272.1.196
CspA, the Major Cold-shock Protein of Escherichia coli, Is an RNA Chaperone
resolves10.1046/j.1365-2958.2000.02198.x
New prospects in studying the bacterial signal recognition particle pathway
resolves10.1242/jcs.166116
Co-translational membrane association of the <i>Escherichia coli</i> SRP receptor
resolves10.1093/nar/gki859
Nucleic acid melting by Escherichia coli CspE
resolves10.4161/rna.7.6.13482
RNA remodeling and gene regulation by cold shock proteins
resolves10.1111/j.1758-2229.2012.00358.x
Resistance to environmental stress requires the RNA chaperones CspC and CspE
resolves10.1046/j.1365-2958.1999.01541.x
Sequence‐selective interactions with RNA by CspB, CspC and CspE, members of the CspA family of <i>Escherichia coli</i>
resolves10.1073/pnas.97.14.7784
<i>Escherichia coli</i> CspA-family RNA chaperones are transcription antiterminators
resolves10.1002/wrna.1200
<scp>YB</scp>‐1 protein: functions and regulation
resolves10.1128/JB.183.4.1205-1214.2001
Role of CspC and CspE in Regulation of Expression of RpoS and UspA, the Stress Response Proteins in <i>Escherichia coli</i>
resolves10.1038/msb4100050
Construction of Escherichia coli K‐12 in‐frame, single‐gene knockout mutants: the Keio collection
resolves10.1093/nar/25.6.1203
Independent and tight regulation of transcriptional units in Escherichia coli via the LacR/O, the TetR/O and AraC/I1-I2 regulatory elements
resolves10.1038/nprot.2013.133
Selective ribosome profiling as a tool for studying the interaction of chaperones and targeting factors with nascent polypeptide chains and ribosomes
resolves10.1093/nar/gki027
PSORTdb: a protein subcellular localization database for bacteria
resolves10.1093/bioinformatics/bti057
PSORTb v.2.0: Expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis
resolves10.1038/nprot.2008.211
Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
resolves10.1093/nar/gkn923
Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists
resolves10.1016/j.jmb.2006.05.044
T-rich DNA Single Strands Bind to a Preformed Site on the Bacterial Cold Shock Protein Bs-CspB
resolves10.1093/nar/gkm040
Sequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approach
resolves10.1261/rna.02809212
RNA single strands bind to a conserved surface of the major cold shock protein in crystals and solution
The 4 references without a DOI — listed, not checked
no DOI — not checkedStructural Basis for Conserved Regulation and Adaptation of the Signal Recognition Particle Targeting Complex
no DOI — not checkedThe Sec translocase
no DOI — not checkedInsights into the Stress Response Triggered by Kasugamycin in Escherichia coli
no DOI — not checkedVon Konig K. Charakterisierung der Oligonucleotidbindung durch das Kalteschockprotein aus Thermotoga maritima. [dissertation, Universitat Regensburg, Germany]2003.
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