The DOI matches its Crossref record.
Dynasore, a Cell-Permeable Inhibitor of Dynamin
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Dynasore is a non-competitive small molecule dynamin inhibitor.
“Dynasore, a non-competitive small molecule dynamin inhibitor [50].”
From Neurodegenerative disease-associated microRNAs acting as signaling molecules modulate CNS neuron structure and viability (2025) · cites this paper as [50]
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
No references could be resolved yet.
Research works printed but not linked: 55
- Abazeed, 2005, Cell-free transport from the trans-golgi network to late endosome requires factors involved in formation and consumption of clathrin-coated vesicles, J. Biol. Chem., 280, 4442, 10.1074/jbc.M412553200 · DOI
- Altschuler, 1998, Redundant and distinct functions for dynamin-1 and dynamin-2 isoforms, J. Cell Biol., 143, 1871, 10.1083/jcb.143.7.1871 · DOI
- Barylko, 1998, Synergistic activation of dynamin GTPase by Grb2 and phosphoinositides, J. Biol. Chem., 273, 3791, 10.1074/jbc.273.6.3791 · DOI
- Cao, 2005, Actin and Arf1-dependent recruitment of a cortactin-dynamin complex to the Golgi regulates post-Golgi transport, Nat. Cell Biol., 7, 483, 10.1038/ncb1246 · DOI · Paper page
- Chen, 2004, The stalk region of dynamin drives the constriction of dynamin tubes, Nat. Struct. Mol. Biol., 11, 574, 10.1038/nsmb762 · DOI
- Cogan, 1999, A robotics-based automated assay for inorganic and organic phosphates, Anal. Biochem., 271, 29, 10.1006/abio.1999.4100 · DOI
- Damke, 1994, Induction of mutant dynamin specifically blocks endocytic coated vesicle formation, J. Cell Biol., 127, 915, 10.1083/jcb.127.4.915 · DOI
- Damke, 1995, Clathrin-independent pinocytosis is induced in cells overexpressing a temperature-sensitive mutant of dynamin, J. Cell Biol., 131, 69, 10.1083/jcb.131.1.69 · DOI
- Damke, 1995, Tightly regulated and inducible expression of dominant interfering dynamin mutant in stably transformed HeLa cells, Methods Enzymol., 257, 209, 10.1016/S0076-6879(95)57026-8 · DOI
- Damke, 2001, Dynamin GTPase domain mutants block endocytic vesicle formation at morphologically distinct stages, Mol. Biol. Cell, 12, 2578, 10.1091/mbc.12.9.2578 · DOI
- Danino, 2001, Dynamin family of mechanoenzymes, Curr. Opin. Cell Biol., 13, 454, 10.1016/S0955-0674(00)00236-2 · DOI
- Danino, 2004, Rapid constriction of lipid bilayers by the mechanochemical enzyme dynamin, J. Struct. Biol., 147, 259, 10.1016/j.jsb.2004.04.005 · DOI
- Eccleston, 2002, Oligomerization and kinetic mechanism of the dynamin GTPase, Eur. Biophys. J., 31, 275, 10.1007/s00249-002-0226-2 · DOI
- Ehrlich, 2004, Endocytosis by random initiation and stabilization of clathrin-coated pits, Cell, 118, 591, 10.1016/j.cell.2004.08.017 · DOI · Paper page
- Ezratty, 2005, Microtubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase, Nat. Cell Biol., 7, 581, 10.1038/ncb1262 · DOI
- Gout, 1993, The GTPase dynamin binds to and is activated by a subset of SH3 domains, Cell, 75, 25, 10.1016/S0092-8674(05)80081-9 · DOI
- Hanover, 1984, Kinetics of transit of transferrin and epidermal growth factor through clathrin-coated membranes, Cell, 39, 283, 10.1016/0092-8674(84)90006-0 · DOI
- Henley, 1998, Dynamin-mediated internalization of caveolae, J. Cell Biol., 141, 85, 10.1083/jcb.141.1.85 · DOI · Paper page
- Hill, 2001, The role of dynamin and its binding partners in coated pit invagination and scission, J. Cell Biol., 152, 309, 10.1083/jcb.152.2.309 · DOI
- Horisberger, 1992, Interferon-induced human protein MxA is a GTPase which binds transiently to cellular proteins, J. Virol., 66, 4705, 10.1128/jvi.66.8.4705-4709.1992 · DOI
- Jiang, 2003, Epidermal growth factor receptor internalization through clathrin-coated pits requires Cbl RING finger and proline-rich domains but not receptor polyubiquitylation, Traffic, 4, 529, 10.1034/j.1600-0854.2003.t01-1-00109.x · DOI
- Kelly, 1999, New twists for dynamin, Nat. Cell Biol., 1, E8, 10.1038/8957 · DOI
- Kirchhausen, 1999, Cell biology. Boa constrictor or rattlesnake?, Nature, 398, 470, 10.1038/18989 · DOI
- Kochs, 2002, Self-assembly of human MxA GTPase into highly ordered dynamin-like oligomers, J. Biol. Chem., 277, 14172, 10.1074/jbc.M200244200 · DOI
- Koenig, 1989, Disappearance and reformation of synaptic vesicle membrane upon transmitter release observed under reversible blockage of membrane retrieval, J. Neurosci., 9, 3844, 10.1523/JNEUROSCI.09-11-03844.1989 · DOI
- Kosaka, 1983, Reversible blockage of membrane retrieval and endocytosis in the garland cell of the temperature-sensitive mutant of Drosophila melanogaster, shibirets1, J. Cell Biol., 97, 499, 10.1083/jcb.97.2.499 · DOI
- Lancaster, 1994, Characterization of rhoGAP. A GTPase-activating protein for rho-related small GTPases, J. Biol. Chem., 269, 1137, 10.1016/S0021-9258(17)42232-0 · DOI
- Maehama, 2000, A sensitive assay for phosphoinositide phosphatases, Anal. Biochem., 279, 248, 10.1006/abio.2000.4497 · DOI
- Marks, 2001, GTPase activity of dynamin and resulting conformation change are essential for endocytosis, Nature, 410, 231, 10.1038/35065645 · DOI
- Massol, 2004, Cholera toxin toxicity does not require functional Arf6- and dynamin-dependent endocytic pathways, Mol. Biol. Cell, 15, 3631, 10.1091/mbc.e04-04-0283 · DOI
- Massol, 2005, Possible role of deep tubular invaginations of the plasma membrane in MHC-I trafficking, Exp. Cell Res., 306, 142, 10.1016/j.yexcr.2005.01.021 · DOI
- McNiven, 1998, Dynamin: a molecular motor with pinchase action, Cell, 94, 151, 10.1016/S0092-8674(00)81414-2 · DOI
- Merrifield, 2002, Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits, Nat. Cell Biol., 4, 691, 10.1038/ncb837 · DOI · Paper page
- Miwako, 2003, Clathrin- and dynamin-dependent coated vesicle formation from isolated plasma membranes, Traffic, 4, 376, 10.1111/j.1365-313X.2008.03782.x · DOI
- Nabi, 2003, Caveolae/raft-dependent endocytosis, J. Cell Biol., 161, 673, 10.1083/jcb.200302028 · DOI
- Narayanan, 2005, An internal GAP domain negatively regulates presynaptic dynamin in vivo: a two-step model for dynamin function, J. Cell Biol., 169, 117, 10.1083/jcb.200502042 · DOI
- Nichols, 2003, Caveosomes and endocytosis of lipid rafts, J. Cell Sci., 116, 4707, 10.1242/jcs.00840 · DOI
- Oh, 1998, Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium, J. Cell Biol., 141, 101, 10.1083/jcb.141.1.101 · DOI
- Orth, 2003, Dynamin at the actin-membrane interface, Curr. Opin. Cell Biol., 15, 31, 10.1016/S0955-0674(02)00010-8 · DOI
- Praefcke, 2004, The dynamin superfamily: universal membrane tubulation and fission molecules?, Nat. Rev. Mol. Cell Biol., 5, 133, 10.1038/nrm1313 · DOI
- Rappoport, 2003, Real-time analysis of clathrin-mediated endocytosis during cell migration, J. Cell Sci., 116, 847, 10.1242/jcs.00289 · DOI
- Rasmussen, 1998, Mixed-lineage kinase 2–SH3 domain binds dynamin and greatly enhances activation of GTPase by phospholipid, Biochem. J., 335, 119, 10.1042/bj3350119 · DOI
- Richter, 1995, Interferon-induced MxA protein. GTP binding and GTP hydrolysis properties, J. Biol. Chem., 270, 13512, 10.1074/jbc.270.22.13512 · DOI
- Schlunck, 2004, Modulation of Rac localization and function by dynamin, Mol. Biol. Cell, 15, 256, 10.1091/mbc.e03-01-0019 · DOI
- Sever, 2002, Dynamin and endocytosis, Curr. Opin. Cell Biol., 14, 463, 10.1016/S0955-0674(02)00347-2 · DOI
- Sever, 2000, Dynamin:GTP controls the formation of constricted coated pits, the rate limiting step in clathrin-mediated endocytosis, J. Cell Biol., 150, 1137, 10.1083/jcb.150.5.1137 · DOI
- Sever, 2000, Garrotes, springs, ratches and whips: putting dynamin models to test, Traffic, 1, 385, 10.1034/j.1600-0854.2000.010503.x · DOI
- Simpson, 1999, SH3-domain-containing proteins function at distinct steps in clathrin-coated vesicle formation, Nat. Cell Biol., 1, 119, 10.1038/10091 · DOI
- Song, 2003, A molecular motor or a regulator? Dynamin's in a class of its own, Biochemistry, 42, 1369, 10.1021/bi027062h · DOI
- Song, 2004, Dynamin GTPase domain mutants that differentially affect GTP binding, GTP hydrolysis, and clathrin-mediated endocytosis, J. Biol. Chem., 279, 40431, 10.1074/jbc.M407007200 · DOI
- Stowell, 1999, Nucleotide-dependent conformational changes in dynamin: evidence for a mechanochemical molecular spring, Nat. Cell Biol., 1, 27, 10.1038/8997 · DOI
- Sweitzer, 1998, Dynamin undergoes a GTP-dependent conformational change causing vesiculation, Cell, 93, 1021, 10.1016/S0092-8674(00)81207-6 · DOI
- Torgersen, 2001, Internalization of cholera toxin by different endocytic mechanisms, J. Cell Sci., 114, 3737, 10.1242/jcs.114.20.3737 · DOI
- Yang, 1999, Endocytosis: is dynamin a ‘blue collar’ or ‘white collar’ worker?, Curr. Biol., 9, R511, 10.1016/S0960-9822(99)80323-6 · DOI
- Zhang, 2001, Three-dimensional reconstruction of dynamin in the constricted state, Nat. Cell Biol., 3, 922, 10.1038/ncb1001-922 · DOI
Cited by
Sorted by citations
The effect of particle design on cellular internalization pathways
Gratton, S. E. A., Ropp, P. A., Pohlhaus, P. D., Luft, J. C., Madden, V. J., Napier, M. E., & DeSimone, J. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801763105 · Cited by 2,918
Gilleron, J., Querbes, W., Zeigerer, A., Borodovsky, A., Marsico, G., Schubert, U., Manygoats, K., Seifert, S., Andree, C., Stöter, M., et al. (2013) · Nature Biotechnology · doi:10.1038/nbt.2612 · Cited by 1,681
Islam, M. N., Das, S. R., Emin, M. T., Wei, M., Sun, L., Westphalen, K., Rowlands, D. J., Quadri, S. K., Bhattacharya, S., & Bhattacharya, J. (2012) · Nature Medicine · doi:10.1038/nm.2736 · Cited by 1,585
Mitochondrial dynamics in health and disease: mechanisms and potential targets
Chen, W., Zhao, H., & Li, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01547-9 · Cited by 1,306
Cassidy-Stone, A., Chipuk, J. E., Ingerman, E., Song, C., Yoo, C., Kuwana, T., Kurth, M. J., Shaw, J. T., Hinshaw, J. E., Green, D. R., et al. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.11.019 · Cited by 1,200
A High Precision Survey of the Molecular Dynamics of Mammalian Clathrin-Mediated Endocytosis
Taylor, M. J., Perrais, D., & Merrifield, C. J. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000604 · Cited by 754
Mitochondrial Dysfunction and Oxidative Stress in Alzheimer’s Disease
Misrani, A., Tabassum, S., & Yang, L. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.617588 · Cited by 654
Ultrafast endocytosis at mouse hippocampal synapses
Watanabe, S., Rost, B. R., Camacho-Pérez, M., Davis, M. W., Söhl-Kielczynski, B., Rosenmund, C., & Jorgensen, E. M. (2013) · Nature · doi:10.1038/nature12809 · Cited by 607
Wu, J. W., Herman, M., Liu, L., Simoes, S., Acker, C. M., Figueroa, H., Steinberg, J. I., Margittai, M., Kayed, R., Zurzolo, C., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.394528 · Cited by 537
Endophilin marks and controls a clathrin-independent endocytic pathway
Boucrot, E., Ferreira, A. P. A., Almeida-Souza, L., Debard, S., Vallis, Y., Howard, G., Bertot, L., Sauvonnet, N., & McMahon, H. T. (2015) · Nature · doi:10.1038/nature14067 · Cited by 542
Self-citationSARS-CoV-2 infects cells after viral entry via clathrin-mediated endocytosis
Bayati, A., Kumar, R., Francis, V., & McPherson, P. S. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100306 · Cited by 499
Cheng, G., Li, W., Ha, L., Han, X., Hao, S., Wan, Y., Wang, Z., Dong, F., Zou, X., Mao, Y., et al. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b03584 · Cited by 371
Clathrin regenerates synaptic vesicles from endosomes
Watanabe, S., Trimbuch, T., Camacho-Pérez, M., Rost, B. R., Brokowski, B., Söhl-Kielczynski, B., Felies, A., Davis, M. W., Rosenmund, C., & Jorgensen, E. M. (2014) · Nature · doi:10.1038/nature13846 · Cited by 333
Mitochondrial fragmentation limits NK cell-based tumor immunosurveillance
Zheng, X., Qian, Y., Fu, B., Jiao, D., Jiang, Y., Chen, P., Shen, Y., Zhang, H., Sun, R., Tian, Z., et al. (2019) · Nature Immunology · doi:10.1038/s41590-019-0511-1 · Cited by 316
Protective astrogenesis from the SVZ niche after injury is controlled by Notch modulator Thbs4
Benner, E. J., Luciano, D., Jo, R., Abdi, K., Paez-Gonzalez, P., Sheng, H., Warner, D. S., Liu, C., Eroglu, C., & Kuo, C. T. (2013) · Nature · doi:10.1038/nature12069 · Cited by 282
Neural stem cells traffic functional mitochondria via extracellular vesicles
Peruzzotti-Jametti, L., Bernstock, J. D., Willis, C. M., Manferrari, G., Rogall, R., Fernandez-Vizarra, E., Williamson, J. C., Braga, A., van den Bosch, A., Leonardi, T., et al. (2021) · PLOS Biology · doi:10.1371/journal.pbio.3001166 · Cited by 263
Anionic nanoplastic contaminants promote Parkinson’s disease–associated α-synuclein aggregation
Liu, Z., Sokratian, A., Duda, A. M., Xu, E., Stanhope, C., Fu, A., Strader, S., Li, H., Yuan, Y., Bobay, B. G., et al. (2023) · Science Advances · doi:10.1126/sciadv.adi8716 · Cited by 262
Schmick, M., Vartak, N., Papke, B., Kovacevic, M., Truxius, D. C., Rossmannek, L., & Bastiaens, P. I. H. (2014) · Cell · doi:10.1016/j.cell.2014.02.051 · Cited by 243
Spreading of Neurodegenerative Pathology via Neuron-to-Neuron Transmission of -Amyloid
Nath, S., Agholme, L., Kurudenkandy, F. R., Granseth, B., Marcusson, J., & Hallbeck, M. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0615-12.2012 · Cited by 244
Wilson, P. M., Fryer, R. H., Fang, Y., & Hatten, M. E. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0032-10.2010 · Cited by 169
Muir, J., Arancibia-Carcamo, I. L., MacAskill, A. F., Smith, K. R., Griffin, L. D., & Kittler, J. T. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000589107 · Cited by 158
Exosomes in cancer: Use them or target them?
Bastos, N., Ruivo, C. F., da Silva, S., & Melo, S. A. (2018) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2017.08.009 · Cited by 140
Candida albicans internalization by host cells is mediated by a clathrin-dependent mechanism
Moreno-Ruiz, E., Galán-Díez, M., Zhu, W., Fernández-Ruiz, E., d'Enfert, C., Filler, S. G., Cossart, P., & Veiga, E. (2009) · Cellular Microbiology · doi:10.1111/j.1462-5822.2009.01319.x · Cited by 133
Frosi, Y., Anastasi, S., Ballarò, C., Varsano, G., Castellani, L., Maspero, E., Polo, S., Alemà, S., & Segatto, O. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201002032 · Cited by 125
Bourgeois, C., Majer, O., Frohner, I. E., Lesiak-Markowicz, I., Hildering, K.-S., Glaser, W., Stockinger, S., Decker, T., Akira, S., Müller, M., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1002599 · Cited by 116
Reddy, P. H., Manczak, M., & Yin, X. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170051 · Cited by 116
Histone deacetylase 8 is required for centrosome cohesion and influenza A virus entry
Yamauchi, Y., Boukari, H., Banerjee, I., Sbalzarini, I. F., Horvath, P., & Helenius, A. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002316 · Cited by 84
Scotti, E., Calamai, M., Goulbourne, C. N., Zhang, L., Hong, C., Lin, R. R., Choi, J., Pilch, P. F., Fong, L. G., Zou, P., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01716-12 · Cited by 81
Human autoantibodies to amphiphysin induce defective presynaptic vesicle dynamics and composition
Werner, C., Pauli, M., Doose, S., Weishaupt, A., Haselmann, H., Grünewald, B., Sauer, M., Heckmann, M., Toyka, K. V., Asan, E., et al. (2016) · Brain · doi:10.1093/brain/awv324 · Cited by 75
Liu, S., Hossinger, A., Heumüller, S.-E., Hornberger, A., Buravlova, O., Konstantoulea, K., Müller, S. A., Paulsen, L., Rousseau, F., Schymkowitz, J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25855-2 · Cited by 72
Regulation of AMPA Receptor Trafficking by Protein Ubiquitination
Widagdo, J., Guntupalli, S., Jang, S. E., & Anggono, V. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00347 · Cited by 68
Niederst, E. D., Reyna, S. M., & Goldstein, L. S. B. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-06-1049 · Cited by 51
Dilna, A., Deepak, K. V., Damodaran, N., Kielkopf, C. S., Kagedal, K., Ollinger, K., & Nath, S. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166246 · Cited by 51
The Race against Protease Activation Defines the Role of ESCRTs in HIV Budding
Bendjennat, M., & Saffarian, S. (2016) · PLOS Pathogens · doi:10.1371/journal.ppat.1005657 · Cited by 45
Retinal pigment epithelial cells mitigate the effects of complement attack by endocytosis of C5b-9
Georgiannakis, A., Burgoyne, T., Lueck, K., Futter, C., Greenwood, J., & Moss, S. E. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1500937 · Cited by 41
Kang, T., Park, C., & Lee, B.-J. (2016) · Archives of Pharmacal Research · doi:10.1007/s12272-016-0847-0 · Cited by 35
Huang, T., Lehmann, M. J., Said, A., Ma, G., & Osterrieder, N. (2014) · Journal of Virology · doi:10.1128/jvi.02079-14 · Cited by 24
Entry of equid herpesvirus 1 into CD172a+ monocytic cells.
Laval, K., Favoreel, H. W., Van Cleemput, J., Poelaert, K. C. K., Brown, I. K., Verhasselt, B., & Nauwynck, H. J. (2016) · Journal of General Virology · doi:10.1099/jgv.0.000375 · Cited by 12
Kumbol, V., Ivanov, A., McGurran, H., Schüler, J., Zhai, Y., Ludwik, K., Hinkelmann, L., Brehm, M., Krüger, C., Küchler, J., et al. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02199-8 · Cited by 8
He, C.-W., & Díaz, E. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1568908 · Cited by 3
Metadata
- Authors
- Macia, E., Ehrlich, M., Massol, R., Boucrot, E., Brunner, C., & Kirchhausen, T.
- Venue
- Developmental Cell
- Publisher
- Elsevier BV
- Published
- 2006-06
- Volume
- 10
- Issue
- 6
- Pages
- 839-850
- ISSN
- 1534-5807
- Cited by
- 1,958
- References
- 0
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2603 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Funders
- National Institutes of Health (GM03548, GM075252, GM62566-05)
- European Molecular Biology Organization
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