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Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by <i>in vivo</i> single-molecule imaging

https://doi.org/10.1073/pnas.0806338105
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39/39 checkable references clean · checked 2026-07-23

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.

2 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 39 checked references that resolve
resolves10.1038/nature06384
Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
resolves10.1016/j.mib.2005.02.010
Protein targeting by the bacterial twin-arginine translocation (Tat) pathway
resolves10.1016/S0065-2911(03)47004-5
The Tat protein translocation pathway and its role in microbial physiology
resolves10.1016/S0092-8674(00)81149-6
A Novel and Ubiquitous System for Membrane Targeting and Secretion of Cofactor-Containing Proteins
resolves10.1093/emboj/17.13.3640
Overlapping functions of components of a bacterial Sec‐independent protein export pathway
resolves10.1074/jbc.274.51.36073
Sec-independent Protein Translocation in Escherichia coli
resolves10.1074/jbc.273.29.18003
An Essential Component of a Novel Bacterial Protein Export System with Homologues in Plastids and Mitochondria
resolves10.1074/jbc.M100682200
TatB and TatC Form a Functional and Structural Unit of the Twin-arginine Translocase from Escherichia coli
resolves10.1083/jcb.200105149
Thylakoid <b>Δ</b>pH-dependent precursor proteins bind to a cpTatC–Hcf106 complex before Tha4-dependent transport
resolves10.1016/S1097-2765(03)00398-8
Differential Interactions between a Twin-Arginine Signal Peptide and Its Translocase in Escherichia coli
resolves10.1021/bi026142i
Characterization and Membrane Assembly of the TatA Component of the<i>Escherichia</i><i>coli</i>Twin-Arginine Protein Transport System
resolves10.1016/j.jmb.2004.11.047
The Escherichia coli Twin-arginine Translocation Apparatus Incorporates a Distinct Form of TatABC Complex, Spectrum of Modular TatA Complexes and Minor TatAB Complex
resolves10.1073/pnas.0503558102
The TatA component of the twin-arginine protein transport system forms channel complexes of variable diameter
resolves10.1111/j.1742-4658.2006.05554.x
Subunit composition and <i>in vivo</i> substrate‐binding characteristics of <i>Escherichia coli</i> Tat protein complexes expressed at native levels
resolves10.1083/jcb.200202048
A twin arginine signal peptide and the pH gradient trigger reversible assembly of the thylakoid ΔpH/Tat translocase
resolves10.1093/emboj/20.10.2472
Functional reconstitution of bacterial Tat translocation in vitro
resolves10.1074/jbc.M512453200
Oligomers of Tha4 Organize at the Thylakoid Tat Translocase during Protein Transport
resolves10.1078/0944-5013-00176
An alternative model of the twin arginine translocation system
resolves10.1038/sj.emboj.7601759
Evidence for a dynamic and transient pathway through the TAT protein transport machinery
resolves10.1074/jbc.M702972200
Cysteine Scanning Mutagenesis and Disulfide Mapping Studies of the TatA Component of the Bacterial Twin Arginine Translocase
resolves10.1146/annurev.biochem.67.1.509
THE GREEN FLUORESCENT PROTEIN
resolves10.1073/pnas.0404200101
Visualization of the movement of single histidine kinase molecules in live <i>Caulobacter</i> cells
resolves10.1074/jbc.M607295200
Cysteine-scanning Mutagenesis and Disulfide Mapping Studies of the Conserved Domain of the Twin-arginine Translocase TatB Component
resolves10.1083/jcb.146.1.45
Component Specificity for the Thylakoidal Sec and Delta Ph–Dependent Protein Transport Pathways
resolves10.1074/jbc.M313187200
Dual Topology of the Escherichia coli TatA Protein
resolves10.1021/bi7005288
The TatA Subunit of<i>Escherichia coli</i>Twin-Arginine Translocase Has an N-in Topology
resolves10.1046/j.1365-2958.2003.03504.x
Role of the <i>Escherichia coli</i> Tat pathway in outer membrane integrity
resolves10.1529/biophysj.106.095265
Nonequivalence of Membrane Voltage and Ion-Gradient as Driving Forces for the Bacterial Flagellar Motor at Low Load
resolves10.1038/nature05135
Stoichiometry and turnover in single, functioning membrane protein complexes
resolves10.1021/bi047581f
Protonation, Photobleaching, and Photoactivation of Yellow Fluorescent Protein (YFP 10C):  A Unifying Mechanism
resolves10.1042/BST0340979
Blinking fluorophores: what do they tell us about protein dynamics?
resolves10.1016/S0006-3495(93)81253-0
Confined lateral diffusion of membrane receptors as studied by single particle tracking (nanovid microscopy). Effects of calcium-induced differentiation in cultured epithelial cells
resolves10.1073/pnas.0511026103
Lateral mobility of proteins in liquid membranes revisited
resolves10.1128/JB.188.10.3442-3448.2006
Diffusion of Green Fluorescent Protein in Three Cell Environments in <i>Escherichia Coli</i>
resolves10.1007/s002850100102
A model for actin-filament length distribution in a lamellipod
resolves10.1016/j.febslet.2004.05.054
Localization of the Tat translocon components in <i>Escherichia coli</i>
resolves10.1074/jbc.M413521200
Location and Mobility of Twin Arginine Translocase Subunits in the Escherichia coli Plasma Membrane
resolves10.1016/j.bbamem.2007.06.021
Structure analysis of the protein translocating channel TatA in membranes using a multi-construct approach
resolves10.1529/biophysj.103.033571
The Elasticity of Single Titin Molecules Using a Two-Bead Optical Tweezers Assay
The 2 references without a DOI — listed, not checked
no DOI — not checkedK Cline, SM Theg, The Sec and Tat protein translocation pathways in chloroplasts. The Enzymes, Molecular Machines Involved in Protein Transport Across Cellular Membranes, eds RE Dalbey, C Koehler, F Tamanoi (Elsevier, San Diego) Vol XXV, 455–485 (2007).
no DOI — not checkedDJ Gross, WW Webb, Cell surface clustering and mobility of the liganded LDL receptor measured by digital video fluorescence microscopy. Spectroscopic Membrane Probes II, ed LM Loew (CRC, Boca Raton, FL), pp. 19–45 (1988).
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.

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