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Millisecond single-molecule localization microscopy combined with convolution analysis and automated image segmentation to determine protein concentrations in complexly structured, functional cells, one cell at a time

https://doi.org/10.1039/c5fd00077g
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47/47 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.

4 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 47 checked references that resolve
resolves10.1016/j.cell.2009.05.051
Full Dynamic Range Proteome Analysis of S. cerevisiae by Targeted Proteomics
resolves10.2144/000112803
Affinity as a Tool in Life Science
resolves10.1002/1615-9861(200204)2:4<383::AID-PROT383>3.0.CO;2-E
Zeptosens' protein microarrays: A novel high performance microarray platform for low abundance protein analysis
resolves10.1038/nature02046
Global analysis of protein expression in yeast
resolves10.1038/nature01511
Mass spectrometry-based proteomics
resolves10.1038/nature01107
A proteomic view of the Plasmodium falciparum life cycle
resolves10.1038/nature04785
Single-cell proteomic analysis of S. cerevisiae reveals the architecture of biological noise
resolves10.1126/science.1188308
Quantifying <i>E. coli</i> Proteome and Transcriptome with Single-Molecule Sensitivity in Single Cells
resolves10.1128/MCB.14.3.1979
Importance of a flanking AT-rich region in target site recognition by the GC box-binding zinc finger protein MIG1.
resolves10.1002/j.1460-2075.1991.tb04901.x
Control of yeast GAL genes by MIG1 repressor: a transcriptional cascade in the glucose response.
resolves10.1099/00221287-144-1-13
Glucose control in Saccharomyces cerevisiae: the role of MIG1 in metabolic functions
resolves10.1111/j.1742-4658.2011.08315.x
The AMPK/SNF1/SnRK1 fuel gauge and energy regulator: structure, function and regulation
resolves10.1534/genetics.111.135731
Nutritional Control of Growth and Development in Yeast
resolves10.1091/mbc.8.8.1603
Regulated nuclear translocation of the Mig1 glucose repressor.
resolves10.1074/jbc.M114.547976
Yeast AMP-activated Protein Kinase Monitors Glucose Concentration Changes and Absolute Glucose Levels
resolves10.1073/pnas.92.8.3132
Repression by SSN6-TUP1 is directed by MIG1, a repressor/activator protein.
resolves10.1016/S0014-5793(99)00725-5
The SNF1 kinase complex from <i>Saccharomyces cerevisiae</i> phosphorylates the transcriptional repressor protein Mig1p in vitro at four sites within or near regulatory domain 1
resolves10.1128/MCB.16.3.753
Functional Domains in the Mig1 Repressor
resolves10.1046/j.1432-1327.1998.2520162.x
Negative control of the Mig1p repressor by Snf1p‐dependent phosphorylation in the absence of glucose
resolves10.1093/nar/27.5.1350
Binding of the glucose-dependent Mig1p repressor to the GAL1 and GAL4 promoters in vivo: regulationby glucose and chromatin structure
resolves10.1016/S0960-9822(99)80503-X
The nuclear exportin Msn5 is required for nuclear export of the Mig1 glucose repressor of Saccharomyces cerevisiae
resolves10.1039/b907837a
Millisecond timescale slimfield imaging and automated quantification of single fluorescent protein molecules for use in probing complex biological processes
resolves10.1098/rsob.150019
From<i>Animaculum</i>to single molecules: 300 years of the light microscope
resolves10.1126/science.1185757
Stoichiometry and Architecture of Active DNA Replication Machinery in <i>Escherichia coli</i>
resolves10.1042/BST20140253
Probing DNA interactions with proteins using a single-molecule toolbox: inside the cell, in a test tube and in a computer
resolves10.1016/j.ymeth.2015.01.010
Superresolution imaging of single DNA molecules using stochastic photoblinking of minor groove and intercalating dyes
resolves10.1038/nmeth.1955
Segregation of molecules at cell division reveals native protein localization
resolves10.1038/nature05135
Stoichiometry and turnover in single, functioning membrane protein complexes
resolves10.1073/pnas.0806338105
Variable stoichiometry of the TatA component of the twin-arginine protein transport system observed by <i>in vivo</i> single-molecule imaging
resolves10.1364/JOSA.59.001314
Properties of a Defocused Optical System*
resolves10.1098/rspa.1955.0158
The frequency response of a defocused optical system
resolves10.1364/OL.28.000801
Phase retrieval for high-numerical-aperture optical systems
resolves10.1529/biophysj.105.071332
Fluorescence Measurement of Intracellular Sodium Concentration in Single Escherichia coli Cells
resolves10.1016/S0006-3495(02)75618-X
Precise Nanometer Localization Analysis for Individual Fluorescent Probes
resolves10.1529/biophysj.103.033571
The Elasticity of Single Titin Molecules Using a Two-Bead Optical Tweezers Assay
resolves10.1016/S0014-5793(02)03857-7
The elasticity of single kettin molecules using a two‐bead laser‐tweezers assay
resolves10.1039/C4CP00219A
Analytical tools for single-molecule fluorescence imaging in cellulo
resolves10.1529/biophysj.106.095265
Nonequivalence of Membrane Voltage and Ion-Gradient as Driving Forces for the Bacterial Flagellar Motor at Low Load
resolves10.1016/j.jsb.2006.02.017
Mechanical properties of cardiac titin’s N2B-region by single-molecule atomic force spectroscopy
resolves10.1042/BST0361032
Are <i>Escherichia coli</i> OXPHOS complexes concentrated in specialized zones within the plasma membrane?
resolves10.1098/rsob.120090
Experimental approaches for addressing fundamental biological questions in living, functioning cells with single molecule precision
resolves10.4161/cib.3.5.12657
Shining the spotlight on functional molecular complexes
resolves10.3390/ijms12042518
Functioning Nanomachines Seen in Real-Time in Living Bacteria Using Single-Molecule and Super-Resolution Fluorescence Imaging
resolves10.1088/0031-9155/49/16/009
Multiple sources of passive stress relaxation in muscle fibres
resolves10.1098/rstb.2012.0248
The physics of life: one molecule at a time
resolves10.1016/j.bbabio.2014.01.020
Single-molecule in vivo imaging of bacterial respiratory complexes indicates delocalized oxidative phosphorylation
resolves10.1126/science.1227126
In Vivo Architecture and Action of Bacterial Structural Maintenance of Chromosome Proteins
The 4 references without a DOI — listed, not checked
no DOI — not checkedP. Pankajakshan , L.Blanc-Feraud, J.-C.Olivo-Marin and J.Zerubia, in 2008 5th IEEE International Symposium on Biomedical Imaging: From Nano to Macro, IEEE, 2008, pp. 740–743
no DOI — not checkedQ. Xue and M. C.Leake, Proc. - 2009 IEEE Int. Symp. Biomed. Imaging From Nano to Macro, ISBI 2009, 2009, pp. 1158–1161
no DOI — not checkedQ. Xue , N. S.Jones and M. C.Leake, 2010 7th IEEE Int. Symp. Biomed. Imaging From Nano to Macro, ISBI 2010-Proc., 2010, pp. 161–164
no DOI — not checkedC5FD00077G-(cit42)/*[position()=1]
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