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 51 checked references that resolve
resolves10.7554/eLife.13065Spatial organization shapes the turnover of a bacterial transcriptome
resolves10.1091/mbc.E13-01-0038Translation- and SRP-independent mRNA targeting to the endoplasmic reticulum in the yeast <i>Saccharomyces cerevisiae</i>
resolves10.1038/nrg2695Prokaryotic transcriptomics: a new view on regulation, physiology and pathogenicity
resolves10.1073/pnas.0902029106Studying membrane proteins through the eyes of the genetic code revealed a strong uracil bias in their coding mRNAs
resolves10.1371/journal.pone.0134413Model Uracil-Rich RNAs and Membrane Protein mRNAs Interact Specifically with Cold Shock Proteins in Escherichia coli
resolves10.1016/S0301-4622(02)00021-2Formation of 70S ribosomes: large activation energy is required for the adaptation of exclusively the small ribosomal subunit
resolves10.1093/emboj/19.8.1900Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA
resolves10.1074/jbc.272.4.2053FtsY, the Prokaryotic Signal Recognition Particle Receptor Homologue, Is Essential for Biogenesis of Membrane Proteins
resolves10.1073/pnas.080077197Association 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.200204144Accumulation of endoplasmic membranes and novel membrane-bound ribosome–signal recognition particle receptor complexes in<i>Escherichia coli</i>
resolves10.1074/jbc.M110.140921Genetic Evidence for Functional Interaction of the Escherichia coli Signal Recognition Particle Receptor with Acidic Lipids in Vivo
resolves10.1128/JB.00208-09Depletion of the Signal Recognition Particle Receptor Inactivates Ribosomes in
<i>Escherichia coli</i>
resolves10.1038/nsmb1150Structural analysis of kasugamycin inhibition of translation
resolves10.1242/jcs.166116Co-translational membrane association of the <i>Escherichia coli</i> SRP receptor
resolves10.1073/pnas.97.14.7784<i>Escherichia coli</i>
CspA-family RNA chaperones are transcription antiterminators
resolves10.1128/JB.183.4.1205-1214.2001Role of CspC and CspE in Regulation of Expression of RpoS and UspA, the Stress Response Proteins in
<i>Escherichia coli</i>
resolves10.1038/msb4100050Construction of Escherichia coli K‐12 in‐frame, single‐gene knockout mutants: the Keio collection
resolves10.1093/nar/25.6.1203Independent 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.2013.133Selective ribosome profiling as a tool for studying the interaction of chaperones and targeting factors with nascent polypeptide chains and ribosomes
resolves10.1093/nar/gki027PSORTdb: a protein subcellular localization database for bacteria
resolves10.1093/bioinformatics/bti057PSORTb v.2.0: Expanded prediction of bacterial protein subcellular localization and insights gained from comparative proteome analysis
resolves10.1038/nprot.2008.211Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
resolves10.1093/nar/gkn923Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists
resolves10.1016/j.jmb.2006.05.044T-rich DNA Single Strands Bind to a Preformed Site on the Bacterial Cold Shock Protein Bs-CspB
resolves10.1093/nar/gkm040Sequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approach
resolves10.1261/rna.02809212RNA 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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