The juxtamembrane linker of synaptotagmin 1 regulates Ca2+ binding via liquid-liquid phase separation

Highly accurate protein structure prediction with AlphaFold

Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works

Molecular dynamics with coupling to an external bath

Berendsen, H. J. C., Postma, J. P. M., van Gunsteren, W. F., DiNola, A., & Haak, J. R. (1984) · The Journal of Chemical Physics · doi:10.1063/1.448118 · Cited by 30,626 · see citing works

‘GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers’

Abraham, M. J., Murtola, T., Schulz, R., Páll, S., Smith, J. C., Hess, B., & Lindahl, E. (2015) · SoftwareX · doi:10.1016/j.softx.2015.06.001 · Cited by 27,190 · see citing works

Polymorphic transitions in single crystals: A new molecular dynamics method

Parrinello, M., & Rahman, A. (1981) · Journal of Applied Physics · doi:10.1063/1.328693 · Cited by 19,668 · see citing works

Canonical sampling through velocity rescaling

Bussi, G., Donadio, D., & Parrinello, M. (2007) · The Journal of Chemical Physics · doi:10.1063/1.2408420 · Cited by 18,034 · see citing works

AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models

Varadi, M., Anyango, S., Deshpande, M., Nair, S., Natassia, C., Yordanova, G., Yuan, D., Stroe, O., Wood, G., Laydon, A., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1061 · Cited by 7,850 · see citing works

CHARMM36m: An Improved Force Field for Folded and Intrinsically Disordered Proteins

Huang, J., Rauscher, S., Nawrocki, G., Ran, T., Feig, M., de Groot, B. L., Grubmüller, H., & MacKerell, A. (2016) · Nature Methods · doi:10.1038/nmeth.4067 · Cited by 6,708 · see citing works

Biomolecular condensates: organizers of cellular biochemistry

Banani, S. F., Lee, H. O., Hyman, A., & Rosen, M. (2017) · Nature reviews. Molecular cell biology · doi:10.1038/nrm.2017.7 · Cited by 5,574 · see citing works

PLUMED 2: New feathers for an old bird

Tribello, G. A., Bonomi, M., Branduardi, D., Camilloni, C., & Bussi, G. (2013) · Computer Physics Communications · doi:10.1016/j.cpc.2013.09.018 · Cited by 3,427 · see citing works

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation

Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927 · see citing works

Engineering and characterization of a superfolder green fluorescent protein

Pédelacq, J. D., Cabantous, S., Tran, T. H., Terwilliger, T. C., & Waldo, G. S. (2005) · Nature Biotechnology · doi:10.1038/nbt1172 · Cited by 2,295 · see citing works

Germline Transmission and Tissue-Specific Expression of Transgenes Delivered by Lentiviral Vectors

Lois, C., Hong, E. J., Pease, S., Brown, E. J., & Baltimore, D. (2002) · Science · doi:10.1126/science.1067081 · Cited by 1,974 · see citing works

Martini 3: A general purpose force field for coarse-grained molecular dynamics

Souza, P. C. T., Alessandri, R., Barnoud, J., Thallmair, S., Faustino, I., Grünewald, F., Patmanidis, I., Abdizadeh, H., Bruininks, B. M. H., Wassenaar, T. A., et al. (2021) · Nature Methods · doi:10.1038/s41592-021-01098-3 · Cited by 1,551 · see citing works

Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues

Das, R. K., & Pappu, R. V. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1304749110 · Cited by 1,008 · see citing works

Synaptotagmin: a Calcium Sensor on the Synaptic Vesicle Surface

Brose, N., Petrenko, A. G., Südhof, T. C., & Jahn, R. (1992) · Science · doi:10.1126/science.1589771 · Cited by 979 · see citing works

Molecular machines governing exocytosis of synaptic vesicles

Jahn, R., & Fasshauer, D. (2012) · Nature · doi:10.1038/nature11320 · Cited by 973 · see citing works

α‐Synuclein aggregation nucleates through liquid‐liquid phase separation

Ray, S., Singh, N., Kumar, R., Patel, K., Pandey, S., Datta, D., Mahato, J., Panigrahi, R., Navalkar, A., Mehra, S., et al. (2020) · Nature Chemistry · doi:10.1038/s41557-020-0465-9 · Cited by 863 · see citing works

Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C

Perin, M. S., Fried, V. A., Mignery, G. A., Jahn, R., & Südhof, T. C. (1990) · Nature · doi:10.1038/345260a0 · Cited by 813 · see citing works

Evaluating phase separation in live cells: diagnosis, caveats, and functional consequencesPreprint

McSwiggen, D. T., Mir, M., Darzacq, X., & Tjian, R. (2019) · Genes & Development · doi:10.1101/gad.331520.119 · Cited by 593 · see citing works

Identification of a synaptic vesicle-specific membrane protein with a wide distribution in neuronal and neurosecretory tissue.

Matthew, W. D., Tsavaler, L., & Reichardt, L. F. (1981) · The Journal of Cell Biology · doi:10.1083/jcb.91.1.257 · Cited by 562 · see citing works

How does synaptotagmin trigger neurotransmitter release?

Chapman, E. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.062005.101135 · Cited by 545 · see citing works

A liquid phase of synapsin and lipid vesicles

Milovanović, D., Wu, Y., Bian, X., & Camilli, P. V. D. (2018) · Science · doi:10.1126/science.aat5671 · Cited by 494 · see citing works

A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding.

Davletov, B. A., & Südhof, T. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74326-9 · Cited by 480 · cited 1× · see citing works

Molecular Mechanisms for Synchronous, Asynchronous, and Spontaneous Neurotransmitter Release

Kaeser, P. S., & Regehr, W. G. (2014) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021113-170338 · Cited by 447 · see citing works

Relation between single-molecule properties and phase behavior of intrinsically disordered proteins

Dignon, G. L., Zheng, W., Best, R. B., Kim, Y. C., & Mittal, J. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1804177115 · Cited by 413 · see citing works

PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane

Bai, J.-H., Tucker, W., & Chapman, E. (2004) · Nature Structural &Molecular Biology · doi:10.1038/nsmb709 · Cited by 390 · see citing works

Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine.

Fernández, I., Araç, D., Ubach, J., Gerber, S. H., Shin, O., Gao, Y., Anderson, R. G. W., Südhof, T., & Rizo, J. (2001) · Neuron · doi:10.1016/s0896-6273(01)00548-7 · Cited by 387 · see citing works

Domain structure of synaptotagmin (p65)

Perin, M., Brose, N., Jahn, R., & Südhof, T. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52480-7 · Cited by 329 · see citing works

Defective recycling of synaptic vesicles in synaptotagmin mutants of Caenorhabditis elegans

Jørgensen, E. M., Hartwieg, E. A., Schuske, K. R., Nonet, M. L., Jin, Y., & Horvitz, H. R. (1995) · Nature · doi:10.1038/378196a0 · Cited by 305 · see citing works

Regulation of Transmembrane Signaling by Phase Separation

Case, L. B., Ditlev, J. A., & Rosen, M. K. (2019) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-052118-115534 · Cited by 304 · see citing works

Ca2+ binding to synaptotagmin: how many Ca2+ ions bind to the tip of a C2‐domain?

Ubach, J., Zhang, X., Shao, X., Südhof, T., & Rizo, J. (1998) · EMBO Journal · doi:10.1093/emboj/17.14.3921 · Cited by 298 · see citing works

Synaptotagmin-Mediated Bending of the Target Membrane Is a Critical Step in Ca2+-Regulated Fusion

Hui, E., Johnson, C. P., Yao, J., Dunning, F. M., & Chapman, E. R. (2009) · Cell · doi:10.1016/j.cell.2009.05.049 · Cited by 291 · see citing works

Sequence Data Analysis for Long Disordered Regions Prediction in the Calcineurin Family.

Romero, Obradovic, & Dunker, K. (1997) · PubMed · Cited by 278 · see citing works

Calcium dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants.

Littleton, J. T., Stern, M., Perin, M. S., & Bellen, H. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.23.10888 · Cited by 274 · see citing works

Kinetics of synaptotagmin responses to Ca2+ and assembly with the core SNARE complex onto membranes.

Davis, A. F., Bai, J.-H., Fasshauer, D., Wolowick, M. J., Lewis, J. L., & Chapman, E. (1999) · Neuron · doi:10.1016/s0896-6273(00)80850-8 · Cited by 271 · see citing works

Direct Interaction of a Ca2+-binding Loop of Synaptotagmin with Lipid Bilayers*

Chapman, E., & Davis, A. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.22.13995 · Cited by 252 · see citing works

Synaptotagmin arrests the SNARE complex before triggering fast, efficient membrane fusion in response to Ca2+

Chicka, M. C., Hui, E., Liu, H., & Chapman, E. R. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1463 · Cited by 198 · see citing works

Membrane bending by protein phase separation

Yuan, F., Alimohamadi, H., Bakka, B., Trementozzi, A. N., Day, K. J., Fawzi, N. L., Rangamani, P., & Stachowiak, J. C. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2017435118 · Cited by 198 · see citing works

A Novel Function for the Second C2 Domain of Synaptotagmin

Chapman, E. R., An, S. J., Edwardson, J., & Jahn, R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.10.5844 · Cited by 191 · see citing works

Ca2+–synaptotagmin directly regulates t-SNARE function during reconstituted membrane fusion

Bhalla, A., Chicka, M. C., Tucker, W. C., & Chapman, E. R. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1076 · Cited by 184 · see citing works

Morphologically Docked Synaptic Vesicles Are Reduced insynaptotagminMutants ofDrosophila

Reist, N. E., Buchanan, J., Li, J., DiAntonio, A., Buxton, E. M., & Schwarz, T. L. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-19-07662.1998 · Cited by 176 · see citing works

Improving Martini 3 for Disordered and Multidomain Proteins

Thomasen, F. E., Pesce, F., Roesgaard, M. A., Tesei, G., & Lindorff‐Larsen, K. (2022) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.1c01042 · Cited by 151 · see citing works

Kinetic efficiency of endocytosis at mammalian CNS synapses requires synaptotagmin I

Nicholson-Tomishima, K., & Ryan, T. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406968101 · Cited by 149 · see citing works

The key role of solvent in condensation: Mapping water in liquid-liquid phase-separated FUS

Ahlers, J., Adams, E. M., Bader, V., Pezzotti, S., Winklhofer, K. F., Tatzelt, J., & Havenith, M. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.01.019 · Cited by 139 · see citing works

The C2B domain of synaptotagmin I is a Ca2+-binding module.

Ubach, J., Lao, Y., Fernández, I., Araç, D., Südhof, T., & Rizo, J. (2001) · Biochemistry · doi:10.1021/bi010340c · Cited by 127 · see citing works

Martinize2 and Vermouth provide a unified framework for molecular topology generation

Kroon, P. C., Grünewald, F., Barnoud, J., van Tilburg, M., Brasnett, C., Souza, P. C., Wassenaar, T. A., & Marrink, S. J. (2025) · eLife · doi:10.7554/elife.90627 · Cited by 124 · see citing works

Phosphatidylinositol 4,5-Bisphosphate Increases Ca2+ Affinity of Synaptotagmin-1 by 40-fold*

van den Bogaart, G., Meyenberg, K., Diederichsen, U., & Jahn, R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.343418 · Cited by 123 · see citing works

Synaptotagmin 1 clamps synaptic vesicle fusion in mammalian neurons independent of complexin

Courtney, N. A., Bao, H., Briguglio, J. S., & Chapman, E. R. (2019) · Nature Communications · doi:10.1038/s41467-019-12015-w · Cited by 116 · see citing works

Synaptotagmin-1 binds to PIP2-containing membrane but not to SNAREs at physiological ionic strength

Park, Y., Seo, J., Fraind, A. M., Pérez-Lara, Á., Yavuz, H., Han, K., Jung, S.-R., Kattan, I., Walla, P., Choi, M., et al. (2015) · Nature Structural &Molecular Biology · doi:10.1038/nsmb.3097 · Cited by 105 · see citing works

Cooperative function of synaptophysin and synapsin in the generation of synaptic vesicle-like clusters in non-neuronal cells

Park, D., Wu, Y., Lee, S., Kim, G., Jeong, S., Milovanović, D., Camilli, P. V. D., & Chang, S. (2021) · Nature Communications · doi:10.1038/s41467-020-20462-z · Cited by 104 · see citing works

Regulation of Synaptotagmin I Phosphorylation by Multiple Protein Kinases

Hilfiker, S., Pieribone, V. A., Nordstedt, C., Greengard, P., & Czernik, A. J. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0730921.x · Cited by 100 · see citing works

Reconstituted synaptotagmin I mediates vesicle docking, priming, and fusion

Wang, Z., Liu, H., Gu, Y., & Chapman, E. R. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201104079 · Cited by 98 · see citing works

Calcium sensitive ring-like oligomers formed by synaptotagmin

Wang, J., Bello, O., Auclair, S., Coleman, J., Pincet, F., Krishnakumar, S. S., Sindelar, C., & Rothman, J. (2014) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1415849111 · Cited by 83 · see citing works

Visualization of synaptotagmin I oligomers assembled onto lipid monolayers

Wu, Y., He, Y.-H., Bai, J.-H., Ji, S., Tucker, W., Chapman, E., & Sui, S.-F. (2003) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0435872100 · Cited by 82 · see citing works

Membrane-embedded Synaptotagmin Penetrates cis ortrans Target Membranes and Clusters via a Novel Mechanism*

Bai, J.-H., Earles, C. A., Lewis, J. L., & Chapman, E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m906729199 · Cited by 77 · see citing works

Mechanism and function of synaptotagmin-mediated membrane apposition

Hui, E., Gaffaney, J. D., Wang, Z., Johnson, C. P., Evans, C. S., & Chapman, E. R. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2075 · Cited by 76 · see citing works

Synapsin condensation controls synaptic vesicle sequestering and dynamics

Hoffmann, C., Rentsch, J., Tsunoyama, T. A., Chhabra, A., Pérez, G. A., Chowdhury, R., Trnka, F., Коробейников, А., Shaib, A., Ganzella, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42372-6 · Cited by 74 · see citing works

Uncoupling the roles of synaptotagmin I as a dual Ca2+ sensor during endo- and exocytosis of synaptic vesicles

Yao, J., Kwon, S. E., Gaffaney, J. D., Dunning, F., & Chapman, E. (2011) · Nature Neuroscience · doi:10.1038/nn.3013 · Cited by 71 · see citing works

Fatty Acylation of Synaptotagmin in PC12 Cells and Synaptosomes

Chapman, E. R., Blasi, J., An, S., Brose, N., Johnston, P. A., Südhof, T. C., & Jahn, R. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1174 · Cited by 71 · see citing works

Ultrastructural Imaging of Activity-Dependent Synaptic Membrane-Trafficking Events in Cultured Brain Slices

Imig, C., López-Murcia, F. J., Maus, L., García-Plaza, I. H., Mortensen, L. S., Schwark, M., Schwarze, V., Angibaud, J., Nägerl, U. V., Taschenberger, H., et al. (2020) · Neuron · doi:10.1016/j.neuron.2020.09.004 · Cited by 66 · see citing works

Computational Screening of Phase-Separating Proteins

Shen, B., Chen, Z., Yu, C., Chen, T., Shi, M., & Li, T. (2021) · Genomics Proteomics & Bioinformatics · doi:10.1016/j.gpb.2020.11.003 · Cited by 64 · see citing works

Different states of synaptotagmin regulate evoked versus spontaneous release

Bai, H., Xue, R., Bao, H., Zhang, L., Yethiraj, A., Cui, Q., & Chapman, E. R. (2016) · Nature Communications · doi:10.1038/ncomms10971 · Cited by 58 · see citing works

Ring-like oligomers of Synaptotagmins and related C2 domain proteins

Zanetti, M. N., Bello, O. D., Wang, J., Coleman, J., Cai, Y., Sindelar, C. V., Rothman, J. E., & Krishnakumar, S. S. (2016) · eLife · doi:10.7554/elife.17262 · Cited by 57 · see citing works

Linker mutations reveal the complexity of synaptotagmin 1 action during synaptic transmission

Liu, H., Bai, H., Xue, R., Takahashi, H., Edwardson, J. M., & Chapman, E. R. (2014) · Nature Neuroscience · doi:10.1038/nn.3681 · Cited by 50 · see citing works

Coacervation of poly-electrolytes in the presence of lipid bilayers: mutual alteration of structure and morphology

Mondal, S., & Cui, Q. (2022) · Chemical Science · doi:10.1039/d2sc02013k · Cited by 40 · see citing works

Distinct Effects of Guanidine Thiocyanate on the Structure of Superfolder GFP

Stepanenko, O. V., Stepanenko, O. V., Kuznetsova, I. М., Shcherbakova, D. M., Verkhusha, V. V., & Константинович, Т. К. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048809 · Cited by 36 · see citing works

A synaptotagmin suppressor screen indicates SNARE binding controls the timing and Ca2+ cooperativity of vesicle fusion

Guan, Z., Bykhovskaia, M., Jorquera, R. A., Sutton, R. B., Akbergenova, Y., & Littleton, J. T. (2017) · eLife · doi:10.7554/elife.28409 · Cited by 35 · see citing works

Synaptotagmin 1 oligomerization via the juxtamembrane linker regulates spontaneous and evoked neurotransmitter release

Courtney, K. C., Vevea, J., Li, Y., Wu, Z., Zhang, Z., & Chapman, E. R. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2113859118 · Cited by 31 · see citing works

Synaptic vesicle proteins are selectively delivered to axons in mammalian neurons

Watson, E. T., Pauers, M. M., Seibert, M. J., Vevea, J., & Chapman, E. R. (2023) · eLife · doi:10.7554/elife.82568 · Cited by 30 · see citing works

Sequence Blockiness Controls the Structure of Polyampholyte Necklaces

Rumyantsev, A. M., Johner, A., & Pablo, J. (2021) · ACS Macro Letters · doi:10.1021/acsmacrolett.1c00318 · Cited by 30 · see citing works

Phosphatidylinositol 4,5 Bisphosphate Controls the cis and trans Interactions of Synaptotagmin 1

Nyenhuis, S. B., Thapa, A., & Cafiso, D. S. (2019) · Biophysical Journal · doi:10.1016/j.bpj.2019.06.016 · Cited by 29 · see citing works

Functional analysis of the interface between the tandem C2 domains of synaptotagmin-1

Evans, C. S., He, Z., Bai, H., Lou, X., Jeggle, P., Sutton, R. B., Edwardson, J. M., & Chapman, E. R. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-07-0503 · Cited by 26 · see citing works

An Engineered Metal Sensor Tunes the Kinetics of Synaptic Transmission

Evans, C. S., Ruhl, D. A., & Chapman, E. R. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.1694-15.2015 · Cited by 21 · see citing works

Compartmentalization of soluble endocytic proteins in synaptic vesicle clusters by phase separation

Yoshida, T., Takenaka, K.-I., Sakamoto, H., Kojima, Y., Sakano, T., Shibayama, K., Nakamura, K., Hanawa‐Suetsugu, K., Mori, Y., Hirabayashi, Y., et al. (2023) · iScience · doi:10.1016/j.isci.2023.106826 · Cited by 21 · see citing works

The mechanism of folding robustness revealed by the crystal structure of extra‐superfolder GFP

Choi, J. Y., Jang, T.-H., & Park, H. H. (2016) · FEBS Letters · doi:10.1002/1873-3468.12534 · Cited by 16 · see citing works

Intersectin and endophilin condensates prime synaptic vesicles for release site replenishment

Ogunmowo, T. H., Hoffmann, C., Patel, C., Pepper, R., wang, H., Gowrisankaran, S., Idel, J., Ho, A. S., Raychaudhuri, S., Maher, B. J., et al. (2025) · Nature Neuroscience · doi:10.1038/s41593-025-02002-4 · Cited by 13 · see citing works

Synaptotagmin I’s Intrinsically Disordered Region Interacts with Synaptic Vesicle Lipids and Exerts Allosteric Control over C2A

Fealey, M. E., Mahling, R. W., Rice, A. M., Dunleavy, K. M., Kobany, S., Lohese, K. J., Horn, B. T., & Hinderliter, A. K. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00085 · Cited by 10 · see citing works

Diallyl Trisulfide From Garlic Regulates RAB18 Phase Separation to Inhibit Lipophagy and Induce Cuproptosis in Hepatic Stellate Cells for Antifibrotic Effects

Tian, H., Sun, S., Qiu, X., Wang, J.-R., Gao, Y., Chen, J., Han, X., Bao, Z., Guo, X., Sun, Y., et al. (2025) · Advancement of science · doi:10.1002/advs.202415325 · Cited by 39 · see citing works

Aggregation and phase separation of α-synuclein in Parkinson's disease

Han, W., Wei, M., Xu, F., & Niu, Z. (2024) · Chemical Communications · doi:10.1039/d4cc01591f · Cited by 22 · see citing works

Synaptotagmin-1 undergoes phase separation to regulate its calcium-sensitive oligomerization

Zhu, M., Xu, H., Jin, Y., Kong, X., Xu, B., Liu, Y., & Yu, H. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202311191 · Cited by 18 · see citing works

Membrane Association of Intrinsically Disordered Proteins

MacAinsh, M., Muhammedkutty, F. N. K., Prasad, R., & Zhou, H. (2025) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-070124-092816 · Cited by 13 · see citing works

Phase Separation–Mediated Compartmentalization Underlies Synapse Formation and Plasticity

Wu, X., Shen, Z., & Zhang, M. (2025) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-112723-040159 · Cited by 14 · see citing works

Insights into de-mixing and morphology modulation in coacervate-membrane interactions from integrating experiments and simulations

Mondal, S., Mangiarotti, A., Dimova, R., & Cui, Q. (2025) · Communications Chemistry · doi:10.1038/s42004-025-01810-w · Cited by 7 · see citing works

Phase separation in the multi-compartment organization of synapses

Zhu, S., Shen, Z., Wu, X., & Zhang, M. (2025) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2025.102975 · Cited by 7 · see citing works

The liprin-α/RIM complex regulates the dynamic assembly of presynaptic active zones via liquid–liquid phase separation

Jin, G., Campos, J., Liu, Y., de la Cruz, B. M., Zhang, S., Liang, M., Li, K., Xie, X., Yu, C., Sterky, F. H., et al. (2025) · PLoS Biology · doi:10.1371/journal.pbio.3002817 · Cited by 6 · see citing works

SNAP25 undergoes phase separation to facilitate the assembly of the synaptic vesicle fusion machinery

Zhu, M., Jin, Y., Liu, J., Kong, X., Liu, Y., & Yu, H. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.116983 · Cited by 5 · see citing works

Epsin1 enforces a condensation-dependent checkpoint for ubiquitylated cargo during clathrin-mediated endocytosis

Sarkar, S., Liu, H., Yuan, F., Malady, B. T., Wang, L., Lafer, E. M., Perez, J., Huibregtse, J. M., & Stachowiak, J. C. (2025) · Nature Communications · doi:10.1038/s41467-025-63238-z · Cited by 3 · see citing works

Metal-induced nanoscale clusterization initiates protein liquid-liquid phase separation

Xiang, S., Hou, Z., Wang, Y., Yang, Y., Hu, H., Yin, C., Huang, G., Cao, K., & Liu, Y. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116067 · Cited by 3 · see citing works

Injectable Silk Fibroin-Based Hydrogels with Ultrafast In Situ Gelation via an Unfolding-Aggregating Strategy for Osteoarthritis Treatment

Wu, Y., Qiu, L., Ou, X., Tao, J., Zheng, M. J., Huang, Y., & Bai, S. (2025) · Biomacromolecules · doi:10.1021/acs.biomac.5c01002 · Cited by 3 · see citing works

HcCnAα regulates NF-κB signaling in Hyriopsis cumingii by interacting with HcIKK and facilitating IκB phosphorylation

Li, Y., Yang, Q., He, G., Long, K., Tang, X., Su, Y., & Wu, Z. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.138787 · Cited by 3 · see citing works

Genome-wide identification of plant C2 domain-containing protein family and the role of OsNTMC2T2.2 under chilling stress in rice

Zhao, L., Wang, J., Zhou, Y., Shi, J., Liu, G., Xie, G., & Wang, L. (2025) · Environmental and Experimental Botany · doi:10.1016/j.envexpbot.2025.106202 · Cited by 2 · see citing works

HRD1 negatively regulates autolysosome formation by inhibiting liquid-liquid phase separation of SNAP29

Qu, W., Chen, D., Zhao, H., Sheng, Q., Wang, J., Shen, Y., & Shen, Y. (2026) · Cell Reports · doi:10.1016/j.celrep.2025.116914 · Cited by 2 · see citing works

Origin of the ionic-strength dependent reentrant behavior in the liquid-liquid phase separation of uncharged intrinsically disordered proteins

Mondal, S., & Shakhnovich, E. I. (2026) · Communications Chemistry · doi:10.1038/s42004-026-02011-9 · Cited by 2 · see citing works

Synaptotagmin-1 in phase: Condensate biology reveals new insights into the synaptic calcium sensor

Tromm, J. V., & Milovanović, D. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202408073 · Cited by 2 · see citing works

Investigating the Context‐Dependent Phase Separation of Human HOX Transcription Factors

Karmakar, S., Manglam, J., Kant, K., & De, S. (2025) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.70009 · Cited by 1 · see citing works

Liquid–liquid phase separation of designer EF-hand peptides for selective and enhanced recovery of rare earth elements

Shen, X., Zhao, J., Wang, H., Yan, R., Wang, W., Yan, T., & Cao, M. (2026) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2026.142293 · Cited by 1 · see citing works

Multi-Force-Field Molecular Dynamics Reveals How Cation Hydration Kinetics Dictate Polypeptide Assembly Pathways and Timescales

Bao, L., Zhu, B., Feng, C., Wang, Z., & Liu, Y. (2026) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.6c00849 · Cited by 1 · see citing works

Alternative splicing of synaptotagmin 7 regulates oligomerization and short-term synaptic plasticity

Mehta, N., Larson, D. T., Wozney, M., Mishra, S., Subramani, S., Kaur, S., Jain, A., & Chapman, E. R. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2601714123 · Cited by 1 · see citing works

Redox-dependent synaptic clustering of gephyrin

Gehling, M.-T., Bruckisch, E. H. W., Eggersmann, F. R., Benting, K., Jacobs, L. H. C., Behrmann, E., Riemer, J., Kloppenburg, P., Liebsch, F., & Schwarz, G. (2026) · Nature Communications · doi:10.1038/s41467-026-77147-2 · Cited by 1 · see citing works

The Origin of the Ionic-strength Dependent Reentrant Behavior in Liquid-Liquid Phase Separation of Uncharged IDPsPreprint

Mondal, S., & Shakhnovich, E. I. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.20.644249 · Cited by 1 · see citing works

Integrating experiments and simulations to unravel coacervate-membrane Interactions: Insights into de-mixing and morphology modulationPreprint

Mondal, S., Mangiarotti, A., Dimova, R., & Cui, Q. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.16.654554 · Cited by 1 · see citing works

Phase separation drives SNARE complexes formationPreprint

Chen, F., Ke, Q., Feng, S., Chen, H., Haung, Q., Ma, F., Cai, Y., Chen, J., Li, S., Wei, W., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.04.641570

Unleashed condensation by recurrent mutations of an epigenetic regulator promotes cancerPreprint

Song, Y., Hao, Y., Latacz, M., Cykowiak, M., Kirylczuk, J., Quan, X., Palomba, F., Ni, S., Liu, L., Hu, J., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.02.18.706652

Biomolecular Condensates in Metabolic Regulation: Phase-Separated Organization of Glycolytic Enzymes

Kihali, E. (2026) · American Journal of Biomedical and Life Sciences · doi:10.11648/j.ajbls.20261402.11

Mechanistic Insights into Adaptive Binding of Vitamins and Hormones at Hotspot-Enriched Interfaces of the Synaptotagmin 1 C2AB DomainPreprint

Hazra, S., Tiwary, B. K., Chaudhuri, A. G., & Chakrabarti, N. B. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.10.18.760018

Synaptotagmin-1 undergoes phase separation to regulate its calcium-sensitive oligomerization

Zhu, M., Xu, H., Jin, Y., Kong, X., Xu, B., Liu, Y., & Yu, H. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202311191 · Cited by 18 · see citing works

The Juxtamembrane Linker of Full-length Synaptotagmin 1 Controls Oligomerization and Calcium-dependent Membrane Binding

Lu, B., Kiessling, V., Tamm, L. K., & Cafiso, D. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.569327 · Cited by 26 · see citing works

Linker mutations reveal the complexity of synaptotagmin 1 action during synaptic transmission

Liu, H., Bai, H., Xue, R., Takahashi, H., Edwardson, J. M., & Chapman, E. R. (2014) · Nature Neuroscience · doi:10.1038/nn.3681 · Cited by 50 · see citing works

Synaptotagmin 1 oligomerization via the juxtamembrane linker regulates spontaneous and evoked neurotransmitter release

Courtney, K. C., Vevea, J., Li, Y., Wu, Z., Zhang, Z., & Chapman, E. R. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2113859118 · Cited by 31 · see citing works

PtdInsP2 and PtdSer cooperate to trap synaptotagmin-1 to the plasma membrane in the presence of calcium

Pérez-Lara, Á., Thapa, A., Nyenhuis, S. B., Nyenhuis, D. A., Halder, P., Tietzel, M., Tittmann, K., Cafiso, D., & Jahn, R. (2016) · eLife · doi:10.7554/elife.15886 · Cited by 89 · see citing works