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YidC and Oxa1 Form Dimeric Insertion Pores on the Translating Ribosome

https://doi.org/10.1016/j.molcel.2009.04.019
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59/59 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.

1 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 59 checked references that resolve
resolves10.1093/embo-reports/kve154
YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids
resolves10.1093/emboj/21.5.995
The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure
resolves10.1006/jmbi.1994.1363
OXA1, a Saccharomyces cerevisiae Nuclear Gene whose Sequence is Conserved form Prokaryotes to Eukaryotes Controls Cytochrome Oxidase Biogenesis
resolves10.1038/nature00827
Three-dimensional structure of the bacterial protein-translocation complex SecYEG
resolves10.1016/0092-8674(90)90111-Q
The purified E. coli integral membrane protein is sufficient for reconstitution of SecA-dependent precursor protein translocation
resolves10.1074/jbc.M110644200
Direct Interaction of YidC with the Sec-independent Pf3 Coat Protein during Its Membrane Protein Insertion
resolves10.1128/JB.01366-07
Functional Overlap but Lack of Complete Cross-Complementation of <i>Streptococcus mutans</i> and <i>Escherichia coli</i> YidC Orthologs
resolves10.1007/BF00234937
How proteins cross the bacterial cytoplasmic membrane
resolves10.1017/S0033583500004297
Cryo-electron microscopy of vitrified specimens
resolves10.1016/j.jmb.2006.10.083
The Mechanosensitive Channel Protein MscL Is Targeted by the SRP to The Novel YidC Membrane Insertion Pathway of Escherichia coli
resolves10.1073/pnas.96.11.6020
Chemistry for the analysis of protein–protein interactions: Rapid and efficient cross-linking triggered by long wavelength light
resolves10.1006/jsbi.1996.0030
SPIDER and WEB: Processing and Visualization of Images in 3D Electron Microscopy and Related Fields
resolves10.1074/jbc.M403229200
Targeting and Translocation of Two Lipoproteins in Escherichia coli via the SRP/Sec/YidC Pathway
resolves10.1002/pro.5560051229
<i>Saccharomyces cerevisiae</i> mitochondria lack a bacterial‐type Sec machinery
resolves10.1093/emboj/cdg624
Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the C‐terminal region of Oxa1
resolves10.1091/mbc.e06-10-0925
Oxa1 Directly Interacts with Atp9 and Mediates Its Assembly into the Mitochondrial F <sub>1</sub> F <sub>o</sub> -ATP Synthase Complex
resolves10.1074/jbc.M110857200
Chloroplast YidC Homolog Albino3 Can Functionally Complement the Bacterial YidC Depletion Strain and Promote Membrane Insertion of Both Bacterial and Chloroplast Thylakoid Proteins
resolves10.1074/jbc.M307362200
Defining the Regions of Escherichia coli YidC That Contribute to Activity
resolves10.1146/annurev.biochem.70.1.755
The Signal Recognition Particle
resolves10.1016/S0074-7696(06)59003-5
YidC as an Essential and Multifunctional Component in Membrane Protein Assembly
resolves10.1016/j.febslet.2008.10.044
The Pf3 coat protein contacts TM1 and TM3 of YidC during membrane biogenesis
resolves10.1016/j.jsb.2008.05.007
Exploration of parameters in cryo-EM leading to an improved density map of the E. coli ribosome
resolves10.1016/j.jmb.2007.10.089
Projection Structure of yidC: A Conserved Mediator of Membrane Protein Assembly
resolves10.1016/S0014-5793(01)02616-3
YidC/Oxa1p/Alb3: evolutionarily conserved mediators of membrane protein assembly
resolves10.1146/annurev.micro.59.030804.121246
BIOGENESIS OF INNER MEMBRANE PROTEINS IN <i>ESCHERICHIA COLI</i>
resolves10.1016/j.molcel.2007.10.034
Ribosome Binding of a Single Copy of the SecY Complex: Implications for Protein Translocation
resolves10.1038/emboj.2008.89
Molecular mechanism and structure of Trigger Factor bound to the translating ribosome
resolves10.1038/nature04133
Structure of the E. coli protein-conducting channel bound to a translating ribosome
resolves10.1083/jcb.200402067
Role of YidC in folding of polytopic membrane proteins
resolves10.1016/S0092-8674(02)00649-9
The Ribosomal Exit Tunnel Functions as a Discriminating Gate
resolves10.1046/j.1365-2958.2002.02972.x
SecDFyajC forms a heterotetrameric complex with YidC
resolves10.1074/jbc.M708936200
Crystal Structure of the Major Periplasmic Domain of the Bacterial Membrane Protein Assembly Facilitator YidC
resolves10.1016/j.cell.2007.02.036
Protein Translocation Is Mediated by Oligomers of the SecY Complex with One SecY Copy Forming the Channel
resolves10.1002/jcc.20084
UCSF Chimera—A visualization system for exploratory research and analysis
resolves10.1038/nature06384
Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
resolves10.1111/j.1742-4658.2008.06588.x
Protein transport across the endoplasmic reticulum membrane
resolves10.1074/jbc.M710493200
The Crystal Structure of the Periplasmic Domain of the Escherichia coli Membrane Protein Insertase YidC Contains a Substrate Binding Cleft
resolves10.1038/35020586
YidC mediates membrane protein insertion in bacteria
resolves10.1016/S1047-8477(03)00072-8
Automatic CTF correction for single particles based upon multivariate statistical analysis of individual power spectra
resolves10.1016/j.jsb.2007.01.005
Generation of ribosome nascent chain complexes for structural and functional studies
resolves10.1038/nature05182
Structure of the E. coli signal recognition particle bound to a translating ribosome
resolves10.1126/science.1117230
Structures of the Bacterial Ribosome at 3.5 Å Resolution
resolves10.1093/emboj/19.4.542
YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase
resolves10.1038/sj.emboj.7600063
Escherichia coli YidC is a membrane insertase for Sec‐independent proteins
resolves10.1093/emboj/cdg623
Ribosome binding to the Oxa1 complex facilitates co‐translational protein insertion in mitochondria
resolves10.1093/embo-reports/kve108
Sec‐dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC
resolves10.1074/jbc.M200311200
Targeting, Insertion, and Localization of Escherichia coli YidC
resolves10.1093/emboj/cdf326
Cryo‐EM reveals an active role for aminoacyl‐tRNA in the accommodation process
resolves10.1074/jbc.M414094200
The Sec-independent Function of Escherichia coli YidC Is Evolutionary-conserved and Essential
resolves10.1111/j.1742-4658.2007.06094.x
<i>Saccharomyces cerevisiae</i> Cox18 complements the essential Sec‐independent function of <i>Escherichia coli</i> YidC
resolves10.1016/j.febslet.2008.02.082
Detection of cross‐links between FtsH, YidC, HflK/C suggests a linked role for these proteins in quality control upon insertion of bacterial inner membrane proteins
resolves10.1038/nature02218
X-ray structure of a protein-conducting channel
resolves10.1093/embo-reports/kve106
Reconstitution of Sec‐dependent membrane protein insertion: nascent FtsQ interacts with YidC in a SecYEG‐dependent manner
resolves10.1073/pnas.0636761100
A conserved function of YidC in the biogenesis of respiratory chain complexes
resolves10.1083/jcb.200402100
F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis
resolves10.1006/jsbi.1996.0004
A New Generation of the IMAGIC Image Processing System
resolves10.1093/nar/gkh026
DSDBASE: a consortium of native and modelled disulphide bonds in proteins
resolves10.1074/jbc.M804344200
The Conserved Third Transmembrane Segment of YidC Contacts Nascent Escherichia coli Inner Membrane Proteins
resolves10.1128/JB.01365-07
Isolation of Cold-Sensitive <i>yidC</i> Mutants Provides Insights into the Substrate Profile of the YidC Insertase and the Importance of Transmembrane 3 in YidC Function
The 1 reference without a DOI — listed, not checked
no DOI — not checkedUse of multivariate statistics in analysing the images of biological macromolecules
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