Reference health
Global profiling of SRP interaction with nascent polypeptides
1 of 35 checkable references need attention · checked 2026-07-22
At the dated check, the references listed below either did not resolve in Crossref or DataCite, or carried a retraction notice. Each one is shown with the registry record that put it there.
References needing attention
does not resolve to a known work10.1128/MMBR.57.1.50-108.1993
The 34 checked references that resolve
resolves10.1146/annurev-biochem-072711-164732
Signal Recognition Particle: An Essential Protein-Targeting Machine
resolves10.1146/annurev.biochem.77.061606.160747
Protein Translocation Across the Bacterial Cytoplasmic Membrane
resolves10.1016/j.cell.2011.10.044
Selective Ribosome Profiling Reveals the Cotranslational Chaperone Action of Trigger Factor In Vivo
resolves10.1016/j.cell.2013.02.003
A Network of Cytosolic Factors Targets SRP-Independent Proteins to the Endoplasmic Reticulum
resolves10.1016/S0021-9258(18)35769-7
Structural requirements for transport of preprocecropinA and related presecretory proteins into mammalian microsomes.
resolves10.1371/journal.pbio.1001100
Defining the Specificity of Cotranslationally Acting Chaperones by Systematic Analysis of mRNAs Associated with Ribosome-Nascent Chain Complexes
resolves10.1016/j.bbamcr.2013.11.007
Chaperone networking facilitates protein targeting to the bacterial cytoplasmic membrane
resolves10.1099/00221287-139-1-95
Immunogold localization of the DnaK heat shock protein in Escherichia coli cells
resolves10.1111/j.1365-2958.1996.tb02646.x
A novel DnaJ‐like protein in Escherichia coli inserts into the cytoplasmic membrane with a Type III topology
resolves10.1126/science.1186743
Sequential Checkpoints Govern Substrate Selection During Cotranslational Protein Targeting
resolves10.1101/gad.1259505
SecM facilitates translocase function of SecA by localizing its biosynthesis
resolves10.1371/journal.pbio.1001735
Heat Shock Transcription Factor σ32 Co-opts the Signal Recognition Particle to Regulate Protein Homeostasis in E. coli
resolves10.1038/nsmb.1402
Signal sequence–independent membrane targeting of ribosomes containing short nascent peptides within the exit tunnel
resolves10.1006/jmbi.2000.4315
Predicting transmembrane protein topology with a hidden markov model: application to complete genomes11Edited by F. Cohen
resolves10.7554/eLife.03440
mRNA-programmed translation pauses in the targeting of E. coli membrane proteins
resolves10.1074/jbc.271.11.6423
Reinitiation of Protein Translocation across the Endoplasmic Reticulum Membrane for the Topogenesis of Multispanning Membrane Proteins
resolves10.1038/ncomms5103
Visualization of a polytopic membrane protein during SecY-mediated membrane insertion
resolves10.1038/nature06387
Molecular code for transmembrane-helix recognition by the Sec61 translocon
resolves10.1073/pnas.051484198
The targeting pathway of
<i>Escherichia coli</i>
presecretory and integral membrane proteins is specified by the hydrophobicity of the targeting signal
resolves10.1016/j.bbamcr.2010.01.017
Structure and function of the molecular chaperone Trigger Factor
resolves10.1073/pnas.1422594112
Regulation by a chaperone improves substrate selectivity during cotranslational protein targeting
resolves10.1038/ncomms5180
Interplay between trigger factor and other protein biogenesis factors on the ribosome
resolves10.1016/j.cell.2009.07.030
Detecting Folding Intermediates of a Protein as It Passes through the Bacterial Translocation Channel
resolves10.3109/09687689509027509
SecA-dependence of the translocation of a large periplasmic loop in the<i>Escherichia coli</i>MalF inner membrane protein is a function of sequence context
resolves10.1126/science.aaa5335
The principle of antagonism ensures protein targeting specificity at the endoplasmic reticulum
resolves10.1016/0022-2836(76)90119-4
Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu
resolves10.1128/JB.186.12.3777-3784.2004
Functional Dissection of
<i>Escherichia coli</i>
Trigger Factor: Unraveling the Function of Individual Domains
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
resolves10.1038/nature03216
Recognition of transmembrane helices by the endoplasmic reticulum translocon
resolves10.1016/j.febslet.2009.06.041
Large‐scale purification of ribosome‐nascent chain complexes for biochemical and structural studies
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