The DOI matches its Crossref record; 91 of the 91 references it cites were found in a registry or an index.
Direct stochastic optical reconstruction microscopy with standard fluorescent probes
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Imaging Intracellular Fluorescent Proteins at Nanometer Resolution
Betzig, E., Patterson, G. H., Sougrat, R., Lindwasser, O. W., Olenych, S., Bonifacino, J. S., Davidson, M. W., Lippincott-Schwartz, J., & Hess, H. F. (2006) · Science · doi:10.1126/science.1127344 · Cited by 8,772
Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
Rust, M. J., Bates, M., & Zhuang, X. (2006) · Nature Methods · doi:10.1038/nmeth929 · Cited by 8,078
Quantum Dots for Live Cells, in Vivo Imaging, and Diagnostics
Michalet, X., Pinaud, F. F., Bentolila, L. A., Tsay, J. M., Doose, S., Li, J. J., Sundaresan, G., Wu, A. M., Gambhir, S. S., & Weiss, S. (2005) · Science · doi:10.1126/science.1104274 · Cited by 7,790
Hell, S. W., & Wichmann, J. (1994) · Optics Letters · doi:10.1364/ol.19.000780 · Cited by 6,065
Communication In The Presence Of Noise
Shannon, C. E. (1998) · Proceedings of the IEEE · doi:10.1109/jproc.1998.659497 · Cited by 4,804
Principles of Optics: Electromagnetic Theory of Propagation, Interference and Diffraction of Light
Born, M., Wolf, E., & Hecht, E. (2000) · Physics Today · doi:10.1063/1.1325200 · Cited by 4,078
Gustafsson, M. G. L. (2000) · Journal of Microscopy · doi:10.1046/j.1365-2818.2000.00710.x · Cited by 3,786
Ultra-High Resolution Imaging by Fluorescence Photoactivation Localization Microscopy
Hess, S. T., Girirajan, T. P. K., & Mason, M. D. (2006) · Biophysical Journal · doi:10.1529/biophysj.106.091116 · Cited by 3,605
Hell, S. W. (2007) · Science · doi:10.1126/science.1137395 · Cited by 2,967
Three-Dimensional Super-Resolution Imaging by Stochastic Optical Reconstruction Microscopy
Huang, B., Wang, W., Bates, M., & Zhuang, X. (2008) · Science · doi:10.1126/science.1153529 · Cited by 2,796
Beiträge zur Theorie des Mikroskops und der mikroskopischen Wahrnehmung
Abbe, E. (1873) · Archiv für Mikroskopische Anatomie · doi:10.1007/bf02956173 · Cited by 2,724
HaloTag: A Novel Protein Labeling Technology for Cell Imaging and Protein Analysis
Los, G. V., Encell, L. P., McDougall, M. G., Hartzell, D. D., Karassina, N., Zimprich, C., Wood, M. G., Learish, R., Ohana, R. F., Urh, M., et al. (2008) · ACS Chemical Biology · doi:10.1021/cb800025k · Cited by 2,624
Precise Nanometer Localization Analysis for Individual Fluorescent Probes
Thompson, R. E., Larson, D. R., & Webb, W. W. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75618-x · Cited by 2,320
Crystal Structure of the Aequorea victoria Green Fluorescent Protein
Ormö, M., Cubitt, A. B., Kallio, K., Gross, L. A., Tsien, R. Y., & Remington, S. J. (1996) · Science · doi:10.1126/science.273.5280.1392 · Cited by 2,242
Lifeact: a versatile marker to visualize F-actin
Riedl, J., Crevenna, A. H., Kessenbrock, K., Yu, J. H., Neukirchen, D., Bista, M., Bradke, F., Jenne, D., Holak, T. A., Werb, Z., et al. (2008) · Nature Methods · doi:10.1038/nmeth.1220 · Cited by 2,189
Reduction potentials of one-electron couples involving free radicals in aqueous solution
Wardman, P. (1989) · Journal of Physical and Chemical Reference Data · doi:10.1063/1.555843 · Cited by 2,123
Efficient Non-Maximum Suppression
Neubeck, A., & Van Gool, L. (2006) · 18th International Conference on Pattern Recognition (ICPR'06) · doi:10.1109/icpr.2006.479 · Cited by 2,118
Creating new fluorescent probes for cell biology
Zhang, J., Campbell, R. E., Ting, A. Y., & Tsien, R. Y. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm976 · Cited by 1,981
A general method for the covalent labeling of fusion proteins with small molecules in vivo
Keppler, A., Gendreizig, S., Gronemeyer, T., Pick, H., Vogel, H., & Johnsson, K. (2003) · Nature Biotechnology · doi:10.1038/nbt765 · Cited by 1,956
Subdiffraction‐Resolution Fluorescence Imaging with Conventional Fluorescent Probes
Heilemann, M., van de Linde, S., Schüttpelz, M., Kasper, R., Seefeldt, B., Mukherjee, A., Tinnefeld, P., & Sauer, M. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200802376 · Cited by 1,866
Self-citationMyosin V Walks Hand-Over-Hand: Single Fluorophore Imaging with 1.5-nm Localization
Yildiz, A., Forkey, J. N., McKinney, S. A., Ha, T., Goldman, Y. E., & Selvin, P. R. (2003) · Science · doi:10.1126/science.1084398 · Cited by 1,837
Near-Field Optics: Microscopy, Spectroscopy, and Surface Modification Beyond the Diffraction Limit
Betzig, E., & Trautman, J. K. (1992) · Science · doi:10.1126/science.257.5067.189 · Cited by 1,808
Glutathione and its role in cellular functions
Sies, H. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00177-x · Cited by 1,735
Super-resolution fluorescence microscopy
Huang, B., Bates, M., & Zhuang, X. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061906.092014 · Cited by 1,657
Specific Covalent Labeling of Recombinant Protein Molecules Inside Live Cells
Griffin, B. A., Adams, S. R., & Tsien, R. Y. (1998) · Science · doi:10.1126/science.281.5374.269 · Cited by 1,549
Highly inclined thin illumination enables clear single-molecule imaging in cells
Tokunaga, M., Imamoto, N., & Sakata-Sogawa, K. (2008) · Nature Methods · doi:10.1038/nmeth1171 · Cited by 1,305
High-density mapping of single-molecule trajectories with photoactivated localization microscopy
Manley, S., Gillette, J. M., Patterson, G. H., Shroff, H., Hess, H. F., Betzig, E., & Lippincott-Schwartz, J. (2008) · Nature Methods · doi:10.1038/nmeth.1176 · Cited by 1,199
Fast, background-free, 3D super-resolution optical fluctuation imaging (SOFI)
Dertinger, T., Colyer, R., Iyer, G., Weiss, S., & Enderlein, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0907866106 · Cited by 1,130
Pavani, S. R. P., Thompson, M. A., Biteen, J. S., Lord, S. J., Liu, N., Twieg, R. J., Piestun, R., & Moerner, W. E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900245106 · Cited by 1,040
Improving the photostability of bright monomeric orange and red fluorescent proteins
Shaner, N. C., Lin, M. Z., McKeown, M. R., Steinbach, P. A., Hazelwood, K. L., Davidson, M. W., & Tsien, R. Y. (2008) · Nature Methods · doi:10.1038/nmeth.1209 · Cited by 1,009
Development and Use of Fluorescent Protein Markers in Living Cells
Lippincott-Schwartz, J., & Patterson, G. H. (2003) · Science · doi:10.1126/science.1082520 · Cited by 992
Microscopy and its focal switch
Hell, S. W. (2009) · Nature Methods · doi:10.1038/nmeth.1291 · Cited by 986
Interferometric fluorescent super-resolution microscopy resolves 3D cellular ultrastructure
Shtengel, G., Galbraith, J. A., Galbraith, C. G., Lippincott-Schwartz, J., Gillette, J. M., Manley, S., Sougrat, R., Waterman, C. M., Kanchanawong, P., Davidson, M. W., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0813131106 · Cited by 888
Live-cell photoactivated localization microscopy of nanoscale adhesion dynamics
Shroff, H., Galbraith, C. G., Galbraith, J. A., & Betzig, E. (2008) · Nature Methods · doi:10.1038/nmeth.1202 · Cited by 873
Three-dimensional sub–100 nm resolution fluorescence microscopy of thick samples
Juette, M. F., Gould, T. J., Lessard, M. D., Mlodzianoski, M. J., Nagpure, B. S., Bennett, B. T., Hess, S. T., & Bewersdorf, J. (2008) · Nature Methods · doi:10.1038/nmeth.1211 · Cited by 812
Fluorescence nanoscopy by ground-state depletion and single-molecule return
Fölling, J., Bossi, M., Bock, H., Medda, R., Wurm, C. A., Hein, B., Jakobs, S., Eggeling, C., & Hell, S. W. (2008) · Nature Methods · doi:10.1038/nmeth.1257 · Cited by 758
Super-resolution video microscopy of live cells by structured illumination
Kner, P., Chhun, B. B., Griffis, E. R., Winoto, L., & Gustafsson, M. G. L. (2009) · Nature Methods · doi:10.1038/nmeth.1324 · Cited by 734
Nonblinking and long-lasting single-molecule fluorescence imaging
Rasnik, I., McKinney, S. A., & Ha, T. (2006) · Nature Methods · doi:10.1038/nmeth934 · Cited by 702
A Reducing and Oxidizing System Minimizes Photobleaching and Blinking of Fluorescent Dyes
Vogelsang, J., Kasper, R., Steinhauer, C., Person, B., Heilemann, M., Sauer, M., & Tinnefeld, P. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200801518 · Cited by 618
Self-citationDoose, S., Neuweiler, H., & Sauer, M. (2009) · ChemPhysChem · doi:10.1002/cphc.200900238 · Cited by 523
Self-citationProposed method for molecular optical imaging
Betzig, E. (1995) · Optics Letters · doi:10.1364/ol.20.000237 · Cited by 444
Labeling of fusion proteins with synthetic fluorophores in live cells
Keppler, A., Pick, H., Arrivoli, C., Vogel, H., & Johnsson, K. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401923101 · Cited by 440
Hell, S., & Stelzer, E. H. K. (1992) · Optics Communications · doi:10.1016/0030-4018(92)90185-t · Cited by 415
Super‐Resolution Imaging with Small Organic Fluorophores
Heilemann, M., van de Linde, S., Mukherjee, A., & Sauer, M. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200902073 · Cited by 405
Self-citationYaroslavsky, L. P. (1985) · Springer Series in Information Sciences · doi:10.1007/978-3-642-81929-2 · Cited by 382
Photoswitching Mechanism of Cyanine Dyes
Dempsey, G. T., Bates, M., Kowtoniuk, W. E., Liu, D. R., Tsien, R. Y., & Zhuang, X. (2009) · Journal of the American Chemical Society · doi:10.1021/ja904588g · Cited by 380
Position measurement with a resolution and noise-limited instrument
Bobroff, N. (1986) · Review of Scientific Instruments · doi:10.1063/1.1138619 · Cited by 375
Hess, S. T., Gould, T. J., Gudheti, M. V., Maas, S. A., Mills, K. D., & Zimmerberg, J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0708066104 · Cited by 373
Superresolution by localization of quantum dots using blinking statistics
Lidke, K. A., Rieger, B., Jovin, T. M., & Heintzmann, R. (2005) · Optics Express · doi:10.1364/opex.13.007052 · Cited by 361
Live-cell super-resolution imaging with trimethoprim conjugates
Wombacher, R., Heidbreder, M., van de Linde, S., Sheetz, M. P., Heilemann, M., Cornish, V. W., & Sauer, M. (2010) · Nature Methods · doi:10.1038/nmeth.1489 · Cited by 337
Self-citationIn vivo protein labeling with trimethoprim conjugates: a flexible chemical tag
Miller, L. W., Cai, Y., Sheetz, M. P., & Cornish, V. W. (2005) · Nature Methods · doi:10.1038/nmeth749 · Cited by 323
Nanometer-localized multiple single-molecule fluorescence microscopy
Qu, X., Wu, D., Mets, L., & Scherer, N. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402155101 · Cited by 304
Photochromic Rhodamines Provide Nanoscopy with Optical Sectioning
Fölling, J., Belov, V., Kunetsky, R., Medda, R., Schönle, A., Egner, A., Eggeling, C., Bossi, M., & Hell, S. W. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200702167 · Cited by 291
Ultrahigh-resolution multicolor colocalization of single fluorescent probes
Lacoste, T. D., Michalet, X., Pinaud, F., Chemla, D. S., Alivisatos, A. P., & Weiss, S. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170286097 · Cited by 285
Vogelsang, J., Cordes, T., Forthmann, C., Steinhauer, C., & Tinnefeld, P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811875106 · Cited by 280
PALM imaging and cluster analysis of protein heterogeneity at the cell surface
Owen, D. M., Rentero, C., Rossy, J., Magenau, A., Williamson, D., Rodriguez, M., & Gaus, K. (2010) · Journal of Biophotonics · doi:10.1002/jbio.200900089 · Cited by 257
Heilemann, M., Dedecker, P., Hofkens, J., & Sauer, M. (2009) · Laser & Photonics Review · doi:10.1002/lpor.200810043 · Cited by 256
Self-citationMulticolor Far-Field Fluorescence Nanoscopy through Isolated Detection of Distinct Molecular Species
Bossi, M., Fölling, J., Belov, V. N., Boyarskiy, V. P., Medda, R., Egner, A., Eggeling, C., Schönle, A., & Hell, S. W. (2008) · Nano Letters · doi:10.1021/nl801471d · Cited by 253
Live-cell dSTORM with SNAP-tag fusion proteins
Klein, T., Löschberger, A., Proppert, S., Wolter, S., van de Linde, S., & Sauer, M. (2011) · Nature Methods · doi:10.1038/nmeth0111-7b · Cited by 250
Self-citationReal‐time computation of subdiffraction‐resolution fluorescence images
WOLTER, S., SCHÜTTPELZ, M., TSCHEREPANOW, M., VAN DE LINDE, S., HEILEMANN, M., & SAUER, M. (2010) · Journal of Microscopy · doi:10.1111/j.1365-2818.2009.03287.x · Cited by 219
Self-citationA Photoactivatable Push−Pull Fluorophore for Single-Molecule Imaging in Live Cells
Lord, S. J., Conley, N. R., Lee, H.-L. D., Samuel, R., Liu, N., Twieg, R. J., & Moerner, W. E. (2008) · Journal of the American Chemical Society · doi:10.1021/ja802883k · Cited by 216
Lighting up cells: labelling proteins with fluorophores.
Miyawaki, A., Sakaue-Sawano, A., & Kogure, T. (2003) · PubMed · Cited by 211
Photoinduced formation of reversible dye radicals and their impact on super-resolution imaging
van de Linde, S., Krstić, I., Prisner, T., Doose, S., Heilemann, M., & Sauer, M. (2011) · Photochemical & Photobiological Sciences · doi:10.1039/c0pp00317d · Cited by 211
Self-citationSuperresolution Microscopy on the Basis of Engineered Dark States
Steinhauer, C., Forthmann, C., Vogelsang, J., & Tinnefeld, P. (2008) · Journal of the American Chemical Society · doi:10.1021/ja806590m · Cited by 200
Make them Blink: Probes for Super‐Resolution Microscopy
Vogelsang, J., Steinhauer, C., Forthmann, C., Stein, I. H., Person‐Skegro, B., Cordes, T., & Tinnefeld, P. (2010) · ChemPhysChem · doi:10.1002/cphc.201000189 · Cited by 199
Imaging biological structures with fluorescence photoactivation localization microscopy
Gould, T. J., Verkhusha, V. V., & Hess, S. T. (2009) · Nature Protocols · doi:10.1038/nprot.2008.246 · Cited by 194
Lee, H.-L. D., Lord, S. J., Iwanaga, S., Zhan, K., Xie, H., Williams, J. C., Wang, H., Bowman, G. R., Goley, E. D., Shapiro, L., et al. (2010) · Journal of the American Chemical Society · doi:10.1021/ja1044192 · Cited by 175
SPDM: light microscopy with single-molecule resolution at the nanoscale
Lemmer, P., Gunkel, M., Baddeley, D., Kaufmann, R., Urich, A., Weiland, Y., Reymann, J., Müller, P., Hausmann, M., & Cremer, C. (2008) · Applied Physics B · doi:10.1007/s00340-008-3152-x · Cited by 174
Fluorescent proteins: a cell biologist's user guide
Snapp, E. L. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.08.002 · Cited by 171
A Stroboscopic Approach for Fast Photoactivation−Localization Microscopy with Dronpa Mutants
Flors, C., Hotta, J., Uji‐i, H., Dedecker, P., Ando, R., Mizuno, H., Miyawaki, A., & Hofkens, J. (2007) · Journal of the American Chemical Society · doi:10.1021/ja074704l · Cited by 158
Selective chemical labeling of proteins in living cells
Miller, L. W., & Cornish, V. W. (2005) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2004.12.007 · Cited by 140
van de Linde, S., Wolter, S., Heilemann, M., & Sauer, M. (2010) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2010.02.010 · Cited by 133
Self-citationAdvances in the speed and resolution of light microscopy
Ji, N., Shroff, H., Zhong, H., & Betzig, E. (2008) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2009.03.009 · Cited by 132
Fluorescence microscopy beyond the diffraction limit
Heilemann, M. (2010) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2010.03.012 · Cited by 126
Self-citationAn In Vivo Covalent TMP-Tag Based on Proximity-Induced Reactivity
Gallagher, S. S., Sable, J. E., Sheetz, M. P., & Cornish, V. W. (2009) · ACS Chemical Biology · doi:10.1021/cb900062k · Cited by 126
Multicolor photoswitching microscopy for subdiffraction-resolution fluorescence imaging
van de Linde, S., Endesfelder, U., Mukherjee, A., Schüttpelz, M., Wiebusch, G., Wolter, S., Heilemann, M., & Sauer, M. (2009) · Photochemical & Photobiological Sciences · doi:10.1039/b822533h · Cited by 124
Self-citationHigh-Resolution Colocalization of Single Dye Molecules by Fluorescence Lifetime Imaging Microscopy
Heilemann, M., Herten, D., Heintzmann, R., Cremer, C. G., Müller, C., Tinnefeld, P., Weston, K. D., Wolfrum, J., & Sauer, M. (2002) · Analytical Chemistry · doi:10.1021/ac025576g · Cited by 117
Self-citationSuper‐Resolution Imaging of DNA Labelled with Intercalating Dyes
Flors, C., Ravarani, C. N. J., & Dryden, D. T. F. (2009) · ChemPhysChem · doi:10.1002/cphc.200900384 · Cited by 111
Photoswitching microscopy with standard fluorophores
van de Linde, S., Kasper, R. T., Heilemann, M., & Sauer, M. (2008) · Applied Physics B · doi:10.1007/s00340-008-3250-9 · Cited by 111
Self-citationLight-Induced Dark States of Organic Fluochromes Enable 30 nm Resolution Imaging in Standard Media
Baddeley, D., Jayasinghe, I., Cremer, C. G., et al. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2008.11.002 · Cited by 110
van de Linde, S., Sauer, M., & Heilemann, M. (2008) · Journal of Structural Biology · doi:10.1016/j.jsb.2008.08.002 · Cited by 107
Self-citationFluorescent Proteins for Photoactivation Experiments
Lippincott‐Schwartz, J., & Patterson, G. H. (2008) · Methods in cell biology · doi:10.1016/s0091-679x(08)85003-0 · Cited by 97
Madej, E., & Wardman, P. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.03.002 · Cited by 87
Dual color localization microscopy of cellular nanostructures
Gunkel, M., Erdel, F., Rippe, K., Lemmer, P., Kaufmann, R., Hörmann, C., Amberger, R., & Cremer, C. G. (2009) · Biotechnology Journal · doi:10.1002/biot.200900005 · Cited by 86
Kinetics of oxidation of aliphatic and aromatic thiols by myeloperoxidase compounds I and II
Burner, U., Jantschko, W., & Obinger, C. (1999) · FEBS Letters · doi:10.1016/s0014-5793(98)01727-x · Cited by 83
Resolving Single-Molecule Assembled Patterns with Superresolution Blink-Microscopy
Cordes, T., Strackharn, M., Ståhl, S., Summerer, W., Steinhauer, C., Forthmann, C., Puchner, E. M., Vogelsang, J., Gaub, H. E., & Tinnefeld, P. (2009) · Nano Letters · doi:10.1021/nl903730r · Cited by 76
Photoactivated Localization Microscopy (PALM) of Adhesion Complexes
Shroff, H., White, H., & Betzig, E. (2008) · Current Protocols in Cell Biology · doi:10.1002/0471143030.cb0421s41 · Cited by 70
Near-isotropic 3D optical nanoscopy with photon-limited chromophores
Tang, J., Akerboom, J., Vaziri, A., Looger, L. L., & Shank, C. V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004899107 · Cited by 70
Burner, U., & Obinger, C. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00713-8 · Cited by 64
Automatic fluorescent tag localization II: improvement in super‐resolution by relative tracking
Thomann, D., Dorn, J. F., Sorger, P. K., & Danuser, G. M. (2003) · Journal of Microscopy · doi:10.1046/j.1365-2818.2003.01223.x · Cited by 59
Subdiffraction‐Resolution Fluorescence Microscopy of Myosin–Actin Motility
Endesfelder, U., van de Linde, S., Wolter, S., Sauer, M., & Heilemann, M. (2010) · ChemPhysChem · doi:10.1002/cphc.200900944 · Cited by 40
Self-citation
Cited by
BODIPY-based probes for the fluorescence imaging of biomolecules in living cells
Kowada, T., Maeda, H., & Kikuchi, K. (2015) · Chemical Society Reviews · doi:10.1039/c5cs00030k · Cited by 1,381
Evaluation of fluorophores for optimal performance in localization-based super-resolution imaging
Dempsey, G. T., Vaughan, J. C., Chen, K. H., Bates, M., & Zhuang, X. (2011) · Nature Methods · doi:10.1038/nmeth.1768 · Cited by 1,369
A trans-synaptic nanocolumn aligns neurotransmitter release to receptors
Tang, A.-H., Chen, H., Li, T. P., Metzbower, S. R., MacGillavry, H. D., & Blanpied, T. A. (2016) · Nature · doi:10.1038/nature19058 · Cited by 677
Nair, D., Hosy, E., Petersen, J. D., Constals, A., Giannone, G., Choquet, D., & Sibarita, J.-B. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.2381-12.2013 · Cited by 617
Tang, J., Kong, B., Wu, H., Xu, M., Wang, Y., Wang, Y., Zhao, D., & Zheng, G. (2013) · Advanced Materials · doi:10.1002/adma.201303124 · Cited by 567
Metadata
- Authors
- van de Linde, S., Löschberger, A., Klein, T., Heidbreder, M., Wolter, S., Heilemann, M., & Sauer, M.
- Venue
- Nature Protocols
- Published
- 2011-06-16
- Volume
- 6
- Issue
- 7
- Pages
- 991-1009
- ISSN
- 1750-2799 (ISSN-L)
- 1754-2189
- OpenAlex
- W2087850846
- Cited by
- 1,071
- References
- 91
- FWCI
- 30.72
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
