Reference health

Structural Dynamics of the YidC:Ribosome Complex during Membrane Protein Biogenesis

https://doi.org/10.1016/j.celrep.2016.11.059

53/53 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.

The 53 checked references that resolve

resolves10.1107/S0907444909052925

PHENIX: a comprehensive Python-based system for macromolecular structure solution

resolves10.1038/nsmb.3086

Translational arrest by a prokaryotic signal recognition particle is mediated by RNA interactions

resolves10.1016/j.celrep.2014.09.011

Molecular Basis for the Ribosome Functioning as an L-Tryptophan Sensor

resolves10.1038/ncomms5103

Visualization of a polytopic membrane protein during SecY-mediated membrane insertion

resolves10.1016/j.str.2015.06.025

A YidC-like Protein in the Archaeal Plasma Membrane

resolves10.1016/j.bbamem.2011.05.024

Towards understanding the Tat translocation mechanism through structural and biophysical studies of the amphipathic region of TatA from Escherichia coli

resolves10.1016/j.jsb.2006.06.001

SIGNATURE: A single-particle selection system for molecular electron microscopy

resolves10.1074/jbc.M114.595082

The Role of the Strictly Conserved Positively Charged Residue Differs among the Gram-positive, Gram-negative, and Chloroplast YidC Homologs

resolves10.1074/jbc.M113.456327

Electrostatics Control Actin Filament Nucleation and Elongation Kinetics

resolves10.1146/annurev.micro.57.030502.090851

Bacterial Membrane Lipids: Where Do We Stand?

resolves10.1007/s00249-013-0925-x

Helical membrane protein conformations and their environment

resolves10.1038/nrg3414

Emerging methods in protein co-evolution

resolves10.1021/ja0393574

Directed Self-Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size

resolves10.1016/j.bbamem.2010.08.016

The Sec translocase

resolves10.1038/nature13916

Architecture and conformational switch mechanism of the ryanodine receptor

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

resolves10.1038/nsmb.2026

Cryo-EM structure of the ribosome–SecYE complex in the membrane environment

resolves10.1038/nature17964

TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action

resolves10.1074/jbc.M115.650309

Role of the Cytosolic Loop C2 and the C Terminus of YidC in Ribosome Binding and Insertion Activity

resolves10.1016/j.jsb.2006.05.004

FREALIGN: High-resolution refinement of single particle structures

resolves10.1021/ja310901f

Optimized Phospholipid Bilayer Nanodiscs Facilitate High-Resolution Structure Determination of Membrane Proteins

resolves10.1021/bi1020293

Substrate-Dependent Conformational Dynamics of the Escherichia coli Membrane Insertase YidC

resolves10.1074/jbc.M307362200

Defining the Regions of Escherichia coli YidC That Contribute to Activity

resolves10.1016/j.jmb.2013.07.042

Elucidating the Native Architecture of the YidC: Ribosome Complex

resolves10.1088/0034-4885/65/2/203

Fluorescence correlation spectroscopy: the technique and its applications

resolves10.1007/s10858-015-9905-z

Optimizing nanodiscs and bicelles for solution NMR studies of two β-barrel membrane proteins

resolves10.1038/nature13167

Structural basis of Sec-independent membrane protein insertion by YidC

resolves10.1038/srep07299

Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase

resolves10.1016/S1047-8477(03)00069-8

Accurate determination of local defocus and specimen tilt in electron microscopy

resolves10.1074/jbc.M708936200

Crystal Structure of the Major Periplasmic Domain of the Bacterial Membrane Protein Assembly Facilitator YidC

resolves10.7554/eLife.02030

Robust and accurate prediction of residue–residue interactions across protein interfaces using evolutionary information

resolves10.1146/annurev-biophys-050511-102312

Mechanisms of Sec61/SecY-Mediated Protein Translocation Across Membranes

resolves10.1146/annurev.biochem.052208.114057

Amphipols, Nanodiscs, and Fluorinated Surfactants: Three Nonconventional Approaches to Studying Membrane Proteins in Aqueous Solutions

resolves10.1038/46224

Structural changes linked to proton translocation by subunit c of the ATP synthase

resolves10.1016/S0076-6879(09)64011-8

Reconstitution of Membrane Proteins in Phospholipid Bilayer Nanodiscs

resolves10.1073/pnas.1219486110

Structural model for the protein-translocating element of the twin-arginine transport system

resolves10.1515/hsz-2012-0199

The YidC/Oxa1/Alb3 protein family: common principles and distinct features

resolves10.1038/35020586

YidC mediates membrane protein insertion in bacteria

resolves10.1016/j.jsb.2012.09.006

RELION: Implementation of a Bayesian approach to cryo-EM structure determination

resolves10.1093/emboj/19.4.542

YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase

resolves10.1016/j.ymeth.2012.12.005

Microscale thermophoresis quantifies biomolecular interactions under previously challenging conditions

resolves10.1111/mmi.12465

The <scp>C</scp>‐terminal regions of <scp>YidC</scp> from <scp>R</scp>hodopirellula baltica and <scp>O</scp>ceanicaulis alexandrii bind to ribosomes and partially substitute for <scp>SRP</scp> receptor function in <scp>E</scp>scherichia coli

resolves10.1016/j.str.2015.10.025

Residues Coevolution Guides the Systematic Identification of Alternative Functional Conformations in Proteins

resolves10.1038/nprot.2008.156

SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs

resolves10.1016/S0014-5793(03)00475-7

Snorkeling of lysine side chains in transmembrane helices: how easy can it get?

resolves10.1016/j.jsb.2006.05.009

EMAN2: An extensible image processing suite for electron microscopy

resolves10.1016/j.febslet.2004.08.069

F1F0 ATP synthase subunit c is targeted by the SRP to YidC in the E. coli inner membrane

resolves10.1083/jcb.200402100

F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis

resolves10.1016/0022-2836(88)90384-1

Electron microscopy and computer image averaging of ice-embedded large ribosomal subunits from Escherichia coli

resolves10.7554/eLife.03035

A structural model of the active ribosome-bound membrane protein insertase YidC

resolves10.1074/jbc.M111.297911

Competitive Binding of the SecA ATPase and Ribosomes to the SecYEG Translocon

resolves10.1128/JB.00792-13

Interaction of Streptococcus mutans YidC1 and YidC2 with Translating and Nontranslating Ribosomes

resolves10.1074/jbc.M804344200

The Conserved Third Transmembrane Segment of YidC Contacts Nascent Escherichia coli Inner Membrane Proteins

What this badge says. CiteStamped means the CHECKABLE references of this work were clean at the dated check: each resolved to a known work in a public registry, and none carried a retraction notice at that time. It says nothing about the quality, findings, or importance of the work itself, and nothing about references deposited without a DOI.

checked 2026-07-22 — re-checked daily as this page is visited; titles and statuses come from Crossref and DataCite and are not part of the signed record

view as graph · paper page

Embed this badge

Both snippets point at the live badge image and link back to this page. The badge re-renders from the daily check, so an embed never goes stale by more than a day of visits.

<a href="https://citestamp.com/citestamped/10.1016/j.celrep.2016.11.059"><img src="https://citestamp.com/citestamped/10.1016/j.celrep.2016.11.059/badge.svg" alt="CiteStamped reference-health badge" width="460" height="64"></a>

[![CiteStamped reference-health badge](https://citestamp.com/citestamped/10.1016/j.celrep.2016.11.059/badge.svg)](https://citestamp.com/citestamped/10.1016/j.celrep.2016.11.059)