The many functions of ESCRTs

Repertoires of Autophagy in the Pathogenesis of Ocular Diseases

Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351

Shedding light on the cell biology of extracellular vesicles

van Niel, G., D'Angelo, G., & Raposo, G. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.125 · Cited by 8,369

Syndecan–syntenin–ALIX regulates the biogenesis of exosomes

Baietti, M. F., Zhang, Z., Mortier, E., Melchior, A., Degeest, G., Geeraerts, A., Ivarsson, Y., Depoortere, F., Coomans, C., Vermeiren, E., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2502 · Cited by 1,899

Ubiquitin-Dependent Sorting into the Multivesicular Body Pathway Requires the Function of a Conserved Endosomal Protein Sorting Complex, ESCRT-I

Katzmann, D. J., Babst, M., & Emr, S. D. (2001) · Cell · doi:10.1016/s0092-8674(01)00434-2 · Cited by 1,473

The Hairpin-type Tail-Anchored SNARE Syntaxin 17 Targets to Autophagosomes for Fusion with Endosomes/Lysosomes

Itakura, E., Kishi‐Itakura, C., & Mizushima, N. (2012) · Cell · doi:10.1016/j.cell.2012.11.001 · Cited by 1,385

Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding

Garrus, J. E., von Schwedler, U. K., Pornillos, O. W., Morham, S. G., Zavitz, K. H., Wang, H. E., Wettstein, D. A., Stray, K. M., Côté, M., Rich, R. L., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00506-2 · Cited by 1,369

The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins

Raiborg, C., & Stenmark, H. (2009) · Nature · doi:10.1038/nature07961 · Cited by 1,359

Nuclear envelope rupture and repair during cancer cell migration

Denais, C. M., Gilbert, R. M., Isermann, P., McGregor, A. L., te Lindert, M., Weigelin, B., Davidson, P. M., Friedl, P., Wolf, K., & Lammerding, J. (2016) · Science · doi:10.1126/science.aad7297 · Cited by 1,318

DNA breaks and chromosome pulverization from errors in mitosis

Crasta, K., Ganem, N. J., Dagher, R., Lantermann, A. B., Ivanova, E. V., Pan, Y., Nezi, L., Protopopov, A., Chowdhury, D., & Pellman, D. (2012) · Nature · doi:10.1038/nature10802 · Cited by 1,227

Multivesicular bodies associate with components of miRNA effector complexes and modulate miRNA activity

Gibbings, D., Ciaudo, C., Erhardt, M., & Voinnet, O. (2009) · Nature Cell Biology · doi:10.1038/ncb1929 · Cited by 1,037

The Endosomal Sorting Complex, ESCRT, has diverse roles in blood progenitor maintenance, lineage choice and immune response

Ray, A., Rai, Y., & Inamdar, M. S. (2024) · Biology Open · doi:10.1242/bio.060412 · Cited by 2

Functions of the UL51 protein during the herpesvirus life cycle

Liu, X., Wang, M., Cheng, A., Yang, Q., Tian, B., Ou, X., Sun, D., He, Y., Wu, Z., Zhao, X., et al. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1457582 · Cited by 2

Peroxisome inter-organelle cooperation in Drosophila

Cheng, A. Y., & Simmonds, A. J. (2024) · Genome · doi:10.1139/gen-2024-0082 · Cited by 2

Endosomal sorting protein SNX4 limits synaptic vesicle docking and release

Poppinga, J., Barret, N. J., Cornelisse, L. N., Verhage, M., & van Weering, J. R. T. (2024) · eLife · doi:10.7554/elife.97910.3 · Cited by 2

HGS Promotes Tumor Growth, Whereas the Coiled-Coil Domain and Its Oligopeptide of HGS Suppress It

Ogura, K., Kawashima, I., & Kasahara, K. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26020772 · Cited by 2

VPS25 Promotes an Immunosuppressive Microenvironment in Head and Neck Squamous Cell Carcinoma

Chen, L., Fang, Y.-H., Wang, K.-M., Zhang, W., & Chen, G. (2025) · Biomolecules · doi:10.3390/biom15030323 · Cited by 2

In Vivo Reprogramming of Tissue‐Derived Extracellular Vesicles for Treating Chronic Tissue Injury Through Metabolic Engineering

Zhao, M., Liu, S., Wang, Y., Lou, P., Lv, K., Wu, T., Li, L., Wu, Q., Zhu, J., Lu, Y., et al. (2025) · Advanced Science · doi:10.1002/advs.202415556 · Cited by 3

Febuxostat alleviate metabolic dysfunction-associated steatohepatitis in rat model via targeting inflammation, cell death, and intestinal barrier dysfunction

Matboli, M., Saad, M., Ahmed, M. F., Hasanin, A. H., Ellithy, G., Abdel-Wahab, M. A.-K., Eltantawy, E. H. B., Hamam, G. G., Hamoud, A., ElShafei, M. M., et al. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118086 · Cited by 2

The ESCRT protein CHMP5 promotes T cell leukemia by enabling BRD4-p300-dependent transcription

Umphred-Wilson, K., Ratnayake, S., Tang, Q., Wang, R., Chaudhary, S. G., Devaiah, B. N., Trichka, J., Wiśniewski, J., Zhou, L., Chen, Q., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59504-9 · Cited by 2

Dysregulation of the endosomal sorting complex III is linked to neurodegeneration in progressive multiple sclerosis

Picón, C., Aleksynas, R., Wojewska, M. J., Virgiliis, F. D., Merkler, D., & Reynolds, R. (2025) · Brain Pathology · doi:10.1111/bpa.70034 · Cited by 2

Mesenchymal Stem Cell-Derived Exosomes: Mechanisms and Applications in Chronic Wound Repair

Amiri, Z., Hashemi, S. A., Oroojalian, F., Molavi, A. M., Rahdar, A., & Pandey, S. (2025) · Nano LIFE · doi:10.1142/s1793984425420048 · Cited by 2

Polystyrene nanoplastics-induced methuosis in brain microvascular endothelial cells: Rescue via ESCRT membrane repair system

Yin, S., Kang, Y., Du, W., Tan, X., Wang, Z., Shao, L., & Liu, J. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.118800 · Cited by 2

Common principles of surface deformation in biology

Roux, A. (2021) · Faraday Discussions · doi:10.1039/d1fd00040c · Cited by 1

Unexpected organellar locations of ESCRT machinery in Giardia intestinalis and complex evolutionary dynamics spanning the transition to parasitism in the lineage FornicataPreprint

Pipaliya, S. V., Santos, R., Salas-Leiva, D. E., Balmer, E. A., Wirdnam, C. D., Roger, A. J., Hehl, A. B., Faso, C., & Dacks, J. B. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.11.430673 · Cited by 2

Identification of in vivo CFTR conformations during biogenesis and upon misfolding by covalent protein painting (CPP)Preprint

Pankow, S., Bamberger, C., Martínez‐Bartolomé, S., Park, S. K., & Yates, J. R. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.02.433670 · Cited by 2

Vps60 initiates formation of alternative membrane-bound ESCRT-III filamentsPreprint

Pfitzner, A.-K., Zivkovic, H., Humbert, F., & Roux, A. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.16.480668 · Cited by 2

ESCRT-dependent STING degradation curtails steady-state and cGAMP-induced signalingPreprint

Gentili, M., Liu, B., Papanastasiou, M., Dele-Oni, D. O., Schwartz, M. A., Carlson, R. J., Al’Khafaji, A. M., Krug, K., Brown, A., Doench, J. G., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.22.509044 · Cited by 2

Two-dimensional HRS condensates drive the assembly of flat clathrin lattices on endosomesPreprint

Hakala, M., Moparthi, S. B., Ganeva, I., Gül, M., Espadas, J., Marcuello, C., Bernat-Silvestre, C., Colom, A., Kudryashev, M., Kukulski, W., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.10.01.616068 · Cited by 2

Proteostasis dysregulation in p.A53T-α-Synuclein iPSC-derived astrocytes exacerbates neurodegeneration in a Parkinson’s disease model with Lewy-like pathologyPreprint

Paschou, C., Apokotou, O., Κόλλιας, Α., Charmpi, K., Dede, S., Samiotaki, M. K., Palese, F., Dimoula, K., Emmanouilidou, E., Taoufik, E., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.06.621638 · Cited by 2

Transcriptional landscape of the archaeal cell cycle is broadly conserved in eukaryotesPreprint

Gomez-Raya-Vilanova, M. V., Teulière, J., Medvedeva, S., Dai, Y., Corel, E., Lopez, P., Lapointe, F., Bhattacharya, D., Haraoui, L., Turc, É., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.20.624502 · Cited by 2

CARM1-mediated methylation controls interactions of ALIX with key partners important for cytokinesisPreprint

Huard, S., Suresh, S., Vayr, J., Ruggiero, S., Dakroub, R., Masson, V., Petrović, A., Dibsy, R., Thomsen, J. H., Younes, Y. H., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.06.663356 · Cited by 2

PefA, an ALG-2-like Ca 2+ sensor, regulates ESCRT and autophagy responses to mycobacterial vacuole damagePreprint

Guallar-Garrido, S., Perret, A., Carreras‐Sureda, A., Michard, C., & Soldati, T. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.01.30.702722 · Cited by 2

Progression in the Relationship between Exosome Production and Atherosclerosis

Yang, Y., Luo, J., Kang, Y., Wu, W., Lu, Y., Fu, J., Zhang, X., Cheng, M., & Cui, X. (2023) · Current Pharmaceutical Biotechnology · doi:10.2174/1389201024666230726114920 · Cited by 1

ESCRT-dependent control of craniofacial morphogenesis with concomitant perturbation of NOTCH signaling

Hermosilla, V. E., Martin, P., Tian, N., Zheng, Y. J., Aho, R., Losa, M., & Selleri, L. (2023) · Developmental Biology · doi:10.1016/j.ydbio.2023.08.002 · Cited by 2

Inflammasome activation in response to aberrations of cellular homeostasis in epithelial cells from human cornea and retina

Korhonen, E. (2024) · Acta Ophthalmologica · doi:10.1111/aos.16646 · Cited by 2

Interaction between ESCRT-III proteins and the yeast SERINC homolog Tms1

Kölling, R. (2024) · Genetics · doi:10.1093/genetics/iyae132 · Cited by 1

HRS Facilitates Newcastle Disease Virus Replication in Tumor Cells by Promoting Viral Budding

Chen, Y., Wang, C., Hu, S., & Liu, X. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms251810060 · Cited by 1

The Role of Autophagy in Heart Disease

Mohiuddin, O., Abraham, S., Zhang, H., & Ruiz‐Velasco, A. (2024) · International Journal of Drug Discovery and Pharmacology · doi:10.53941/ijddp.2024.100021 · Cited by 1

The Greatwall kinase Rim15 promotes microautophagy and microlipophagy under the control of TORC1

Takahashi, Y., San, T. T., Manik, M. I. N., Morshed, S., & Ushimaru, T. (2025) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2025.151468 · Cited by 1

When Extracellular Vesicles Go Viral: A Bird’s Eye View

Margolis, L. B., & Sadovsky, Y. (2025) · Pathogens and Immunity · doi:10.20411/pai.v10i1.787 · Cited by 1

Mechanisms of Asymmetrical Exosome Release from Polarized Epithelial Cells: Implications for the Molecular Basis of Exosomal Heterogeneity

Fukuda, M. (2025) · Springer eBooks · doi:10.1007/978-981-97-7067-0_3 · Cited by 1

Membrane Contact Sites in Proteostasis and ER Stress Response

Vermue, F. C., Sapmaz, A., & Berlin, I. (2025) · Contact · doi:10.1177/25152564251363050 · Cited by 2

The endosomal sorting complex protein FYVE4 affects abscisic acid signaling by regulating the stability of abscisic acid receptors

Chen, J., Liu, C., Yang, Z., Zhuo, D., Li, H., Zhou, J. M., Yang, C., Shen, W., Peng, C., & Gao, C. (2025) · Journal of Experimental Botany · doi:10.1093/jxb/eraf350 · Cited by 1

A Tubules-First Model for the Origin of Eukaryotic Membrane Traffic

Thattai, M. (2026) · Annual Review of Biophysics · doi:10.1146/annurev-biophys-021424-013933 · Cited by 1

A Self‐Homing Liposomal Nanobot for Active Therapy of Glioblastoma

Cheng, Y., Zhu, K., Yang, L., Mao, M., Wu, Y., Xuan, M., & He, Q. Z. (2025) · Angewandte Chemie · doi:10.1002/ange.202512948 · Cited by 1

Analysis of native Ist1 dynamics reveals multiple pools of ESCRT-III on endosomes

Swift, K. A., Pustova, I., Kasberg, W., Bowman, J., Gopinath, K., Voss, E., Nelson, H., & Audhya, A. (2025) · The Journal of Cell Biology · doi:10.1083/jcb.202407013 · Cited by 1

Identification of druggable targets in melanoma by multi-omics Mendelian randomization integrated with transcriptomic and spatial analysis

Xing, J., Yang, M., Chen, M., & Tao, R. (2025) · Frontiers in Genetics · doi:10.3389/fgene.2025.1657356 · Cited by 1

Starving tumor, feeding metastasis: a warning about low-carbohydrate diets in cancer therapy

Kim, B., & Youn, B. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02469-4 · Cited by 1

Deubiquitinase MoAMSH inhibits autophagy by targeting MoAtg6 in Magnaporthe oryzae

Liao, J., Shen, Z.-F., Wang, J.-Y., He, M.-F., Lv, H.-M., Zhao, J., Zhang, Y., Zhu, X., Li, L., Wang, Z., et al. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02487-3 · Cited by 1

Targeting the host factor HGS–viral membrane protein interaction in coronavirus infection

Long, X., Chen, R., Bai, R., Tian, B., Cao, Y., Chen, K., Li, F., Wang, Y., Tang, Y., Yang, Q., et al. (2025) · Journal of Clinical Investigation · doi:10.1172/jci200225 · Cited by 1

Significance of EVs in Prostate Cancer Bone Metastases

Ito, K., Tamura, T., Urabe, F., Sakamoto, S., Kimura, T., Egawa, S., & Ochiya, T. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262412160 · Cited by 1

The multifaceted significance of phosphoinositides in endocytic trafficking

Xie, C., & Shi, A. (2026) · FEBS Letters · doi:10.1002/1873-3468.70268 · Cited by 2

Mislocalization of FTD3-associated mutant CHMP2B to the nucleus of human neurons due to loss of a nuclear export signal

Jun, Y., Hass, E. P., Lee, S., Fazzio, T. G., & Gao, F. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02222-0 · Cited by 1

Molecular crosstalk via exosomes in lung cancer progression

Dhar, R., Kumarasamy, V., Oliver, B. G. G., & Subramaniyan, V. (2026) · Interdisciplinary medicine · doi:10.1002/inmd.70088 · Cited by 1

Elevated TRPP2 promotes malignant behavior of head and neck cancer via enhancing exosome biogenesis

Bai, S., Sun, H., Xu, X., Wei, Y., Zhang, Y., Zhang, C., PENG, Q. C., Zhu, J., & Du, J. (2026) · Extracellular Vesicle · doi:10.1016/j.vesic.2026.100105 · Cited by 1

CHMP7/ESCRT-III Is Localized at the Nuclear Envelope of Cortical Neurons and Required for Expression of Activity-Regulated Genes

Chietera, P., Berger, H., Wahl, N., Ali, M., & Apostolova, G. (2026) · Biology · doi:10.3390/biology15040308 · Cited by 1

Exosomes in Osteoarthritis: Emerging Roles in Pathogenesis, Diagnosis, and Therapeutic Potential

Bagherifard, A., Talebi, S., Hemmatyar, A., Mokhtari, K., Yahyazedeh, H., & Tanzadehpanah, H. (2026) · Current Pharmaceutical Design · doi:10.2174/0113816128412201251125100451 · Cited by 1

Involvement of two ESCRT-Ⅲ accessory proteins, MoDid2 and MoVta1, in development, pathogenicity, and endocytosis in Magnaporthe oryzae

Liao, J., Shen, Z.-F., Wang, J.-Y., He, M., Lv, H.-M., Zhao, J., Zhao, W., Li, L., Wang, Z., Sun, L., et al. (2026) · Microbiological Research · doi:10.1016/j.micres.2026.128479 · Cited by 1

Vesicle carrier-mediated pathways of unconventional secretion

Zhu, M., & Ma, L. (2026) · Trends Open · doi:10.1016/j.treopn.2025.12.001 · Cited by 1

ALIX and ITCH localize to the base of primary cilia and negatively regulate ciliary Polycystin-2 levels

Berggreen, C. R., Laplace, J., Campestre, F., Petersen, A.-L. W., Fixdahl, A. M., Mary, B., Ghazanfar, S., Li, G., Wagner, L. E., Rezi, C. K., et al. (2026) · BMC Molecular and Cell Biology · doi:10.1186/s12860-026-00571-1 · Cited by 1

Unveiling the Potential of Plant-derived Exosomes: A Comprehensive Review

Jaiswal, S., Sethi, M., Rana, R., Tripathi, S., Trivedi, A. K., & Chourasia, M. K. (2026) · AAPS PharmSciTech · doi:10.1208/s12249-026-03407-5 · Cited by 1

Cutting edge: ESCRT-mediated phagophore closure in mammals

Takahashi, Y., Opozda, D. M., & Wang, H. (2026) · Biochemical Journal · doi:10.1042/bcj20250148 · Cited by 1

The dual role of extracellular vesicles in vascular calcification: from molecular mechanisms to clinical translation

Zhang, Y., Wang, Y., Lu, J. L., Li, X., Chen, Z., Wang, X. W., Tang, T., & Tang, R. (2026) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2026.1815938 · Cited by 1

ESCRT-mediated membrane remodeling in cancer immune evasion and resistance to immunotherapy: mechanisms, therapeutic vulnerabilities, and translational implications

Wang, H., Gu, Y., Liu, J., Tan, H., Li, J., Li, J., Shi, W., & Zhang, Y. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.117007 · Cited by 1

Role of ESCRT pathway and autophagy in neurodegenerative diseases

Dongre, S., Soni, N., & Bissa, B. (2026) · International review of neurobiology · doi:10.1016/bs.irn.2026.05.022 · Cited by 1

Systematic analysis of homozygous autosomal copy number losses in exomes improves diagnostic yield and uncovers ultra-rare recessive disorders

Chaurasia, A., Shukla, A., Pande, S., Purushothama, G., Ashokan, A. K., Majethia, P., Kaur, N., Upadhyai, P., Quadri, N., Bhavani, G. S., et al. (2026) · European Journal of Human Genetics · doi:10.1038/s41431-026-02158-y · Cited by 2

Branched actin segregates endocytic cargo to control sorting and fission

Frisby, D., Naslavsky, N., & Caplan, S. (2026) · Journal of Cell Science · doi:10.1242/jcs.265091 · Cited by 1

Insights into programmed cell death from multiple imaging modalities

Li, S. N., Zhang, X., Li, D., Hou, Y., Qian, Y., Xu, J., Gu, Q., Yang, M., & Chu, M. (2026) · Journal of Translational Medicine · doi:10.1186/s12967-026-08568-2 · Cited by 1

Mitochondrial dysfunction and lipid droplet dynamics in MASH: HSD17B13 as a therapeutic target

Noor, S., Tian, Y., & Su, W. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1912237 · Cited by 1

Exosomes—nano-messengers in tumors: capturing techniques, birth codes, and functional deciphering

Li, Y., Gao, Y., Wang, Y.-H., Zhou, K.-F., Zhao, Y., & Zhao, L. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1825151 · Cited by 1

The proteasome promotes cytokinetic abscission by relieving an Aurora B-dependent inhibition of ESCRT-III dynamics

Dibsy, R., Advedissian, T., Custot, C., Baum, B., & Échard, A. (2026) · Current Biology · doi:10.1016/j.cub.2026.07.073 · Cited by 1

Unveiling the role of extracellular vesicles in HIV infection: molecular mechanisms, viral persistence, and therapeutic opportunities

Salzano, F., Capuano, N., Giordano, F., Bellis, E. D., Conti, V., Pagliano, P., & Franci, G. (2026) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuag046 · Cited by 1

Extracellular vesicles in targeted drug delivery: from biological functions to surface engineering

Duca, G., Tinnirello, V., Ganji, N. R., Alessandro, R., & Raimondo, S. (2026) · Molecular Biomedicine · doi:10.1186/s43556-026-00578-2 · Cited by 1

Methyl-HLH-30/TFEB orchestrates holistic intestinal recuperation against bacterial pore-forming toxin intoxication via TTC38 in metazoans

Hsieh, H.-C., Cheng, Y., Wu, C.-C., Luk, C. K. J., Weng, Y.-H., Chiu, T.-H., Chang, S.-W., Chang, T.-W., Gu, Y.-N., Ruan, J., et al. (2026) · Autophagy · doi:10.1080/15548627.2026.2735736 · Cited by 1

Survey of the human proteostasis network: the autophagy-lysosome pathway

Powers, E. T., Elsasser, S., Tan, E. P., Cole, C. M., Xiao, Q., Stoeger, T., Sui, X., Kurtzbard, R. D., Martínez-Botía, P., Richardson, R. A. K., et al. (2026) · Autophagy · doi:10.1080/15548627.2026.2741038 · Cited by 2

ESCRTing membrane collapse

Strzyz, P. J. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0273-5 · Cited by 1

Flattening out: A new ESCRT structure in cell adhesions

Hakala, M., & Roux, A. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202306059 · Cited by 1

BAR-domain proteins and host membrane remodeling in bacterial invasion

Sanchez, L., Valenzuela, C., & Enninga, J. (2023) · Faculty Reviews · doi:10.12703/r/12-15 · Cited by 1

Engineered Exosomes as Nano-Vectors against Neurodegenerative Disorders

Muteeb, G., Zia, Q., & Alshoaibi, A. A. (2023) · Springer eBooks · doi:10.1007/978-981-99-3848-3_12 · Cited by 1

Wheat ESCRT-III protein TaSAL1 regulates male gametophyte transmission and controls tillering and heading date

Song, C., Xie, K., Chen, H., Xu, S., & Mao, H. (2024) · Journal of Experimental Botany · doi:10.1093/jxb/erae012 · Cited by 1

ESCRT-III-dependent and -independent egress of herpesviruses

Arii, J. (2024) · Frontiers in Virology · doi:10.3389/fviro.2024.1378054 · Cited by 1

Sécrétion non conventionnelle

Denus, M., Fargues, W., Filaquier, A., Néel, É., Marin, P., Parmentier, M., & Villeneuve, J. (2024) · médecine/sciences · doi:10.1051/medsci/2024013 · Cited by 1

Biogenesis of EVs in Trypanosomatids

Silva, N. S. D. L., & Schenkman, S. (2024) · Current topics in membranes · doi:10.1016/bs.ctm.2024.06.004 · Cited by 1

EhVps35, a retromer component, is a key factor in secretion, motility, and tissue invasion by Entamoeba histolytica

Díaz-Valdez, J., Javier‐Reyna, R., Galindo, A., Salazar-Villatoro, L. I., Montaño, S., & Orozco, E. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1467440 · Cited by 1

Brassicaceae and Viral Diseases

Ross, I. A. (2024) · Springer eBooks · doi:10.1007/978-3-031-63681-3_14 · Cited by 1

Nuclear ESCRT is involved in intranuclear protein quality control by micronucleophagy

Tasnin, M. N., Takahashi, Y., Takuma, T., & Ushimaru, T. (2024) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2024.151219 · Cited by 1

Comprehensive analysis of ESCRT transcriptome-associated signatures and identification of the regulatory role of LMO7-AS1 in osteosarcoma

Zhao, S., Tian, D., Huang, F., Wang, L., Cheng, J., He, Z., Shen, Q., Liang, S., Gong, D., Liu, J., et al. (2025) · Cancer Cell International · doi:10.1186/s12935-025-03659-4 · Cited by 1

Exosomes shape inflammatory tumor microenvironment

He, C., Yu, W., Zhao, Q., Liu, H., Wang, Y., Xiong, Y., Zeng, Y., Zhao, J., Xu, Z. P., & Zhang, L. L. (2025) · Chinese Chemical Letters · doi:10.1016/j.cclet.2025.111900 · Cited by 1

Canonical versus noncanonical autophagy

Petroni, G., & Galluzzi, L. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820538-9.00008-9 · Cited by 1

Protein Crowding Mediates Membrane Remodeling in Upstream ESCRT-induced Formation of Intraluminal VesiclesPreprint

Liese, S., Wenzel, E. M., Kjos, I., Molina, R. V. R., Schultz, S. W., Brech, A., Stenmark, H., Raiborg, C., & Carlson, A. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/834457 · Cited by 1

ESCRTs cut some slack

Piper, R. C. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0557-1 · Cited by 1

Membrane Trafficking of Integral Cell Junction ProteinsPreprint

Horowitz, A. (2021) · OSF Preprints (OSF Preprints) · doi:10.31219/osf.io/cmdqb · Cited by 1

Rules for the self-assembly of ESCRT-III on endosomesPreprint

Sprenger, S., Migliano, S. M., Oleschko, F., Kobald, M., Hess, M. W., & Teis, D. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.19.431979 · Cited by 1

A lipid primes the final cut in dividing cells

Brill, J. A., & Wilde, A. (2021) · Science · doi:10.1126/science.abm7949 · Cited by 1

NSF/αSNAP2-mediated cis -SNARE complex disassembly precedes membrane fusion generating the cell plate during Arabidopsis cytokinesisPreprint

Park, M., Mayer, U., & Jürgens, G. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.04.29.490041 · Cited by 1

ESCRTing Around the Cell

Hanson, P. I., & Saha, N. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00136-x · Cited by 1

Clathrin and Clathrin-Mediated Membrane Traffic

Bates, G. T., Briant, K., Bultitude, W. P., & Brodsky, F. M. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00155-3 · Cited by 1

Cell-intrinsic and -extrinsic functions of the ESCRT-III component Shrub in cytokinetic abscission of Drosophila Sensory Organ precursorPreprint

Bruelle, C., Pinot, M., Daniel, E., Daudé, M., Mathieu, J., & Borgne, R. L. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.10.27.514017 · Cited by 1

Modifications of Two ESCRT-I Subunits with Distinct Ubiquitin Chains Regulate Plant ImmunityPreprint

Wang, C., Zhang, Y., Zhou, B., Verma, P., Hamera, S., & Zeng, L. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.10.552820 · Cited by 1

Human ESCRT-I and ALIX function as scaffolding helical filaments in vivoPreprint

Spada, S. J., Rose, K. M., Sette, P., O’Connor, S. K., Dussupt, V., Yerramilli, V. S., Nagashima, K., Sjoelund, V. H., Cruz, P., Kabát, J., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.01.592080 · Cited by 1

A PI(3,5)P2/ESCRT-III axis terminates STING signalling by facilitating TSG101-mediated lysosomal microautophagyPreprint

Shoji, T., Shinojima, A., Kusumi, S., Koga, D., Mukai, K., Nakayama, J., Higashiyama, S., Kuchitsu, Y., & Taguchi, T. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.26.595979 · Cited by 1

Autophagy controls differentiation of Drosophila blood cells by regulating Notch levels in response to nutrient availabilityPreprint

Katz, M. J., Rodríguez, F., Evangelisti, F., Pérez-Pandolfo, S., Sommario, N., Borrat, A., Melani, M., & Wappner, P. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.25.600418 · Cited by 1

Exosome regulation by Rubicon in ageing

Zhen, Y., & Stenmark, H. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01482-z · Cited by 1

The G-protein coupled receptor GPR34 maintains the homeostatic state of microglia and restrains the disease-associated microglial response in an Alzheimers disease modelPreprint

Geller, A., Kwon, M. J., Simmons, S., Xu, Q., Martenis, W. E., Doman, J. L., Natarajan, S., Stalnaker, K. J., Zhang, J., Adiconis, X., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.26.690816 · Cited by 1

Pathogen-induced formation of a nascent organelle derived from mitochondriaPreprint

Li, X., Delgado, J. M., Sun, Y., & Pernas, L. F. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.04.23.720395 · Cited by 1

VPS4 and CHMP7 release centromeres from the nuclear envelope for post-mitotic positioning in daughter nucleiPreprint

Kornakov, N., Heiss, T., Kolodzinski, A., Tam, R., Kelley, M. E., Jones, N. H., Pasolli, H. A., & Kapoor, T. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.13.738224 · Cited by 1

Structural Mechanisms of DNAJC13 Dimeric Assembly and InsP6 binding in Recycling Endosome RegulationPreprint

Fu, T., Lee, C., Hundley, F. V., Paulo, J. A., & Harper, J. W. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.07.28.740790 · Cited by 1

Oropouche virus glycoprotein topology and cellular requirements for virus assemblyPreprint

Barbosa, N. S., Concha, J. O., daSilva, L. L. P., Crump, C. M., & Graham, S. C. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.28.122689

Bro1 stimulates Vps4 activity to promote Intralumenal Vesicle Formation during Multivesicular Body biogenesisPreprint

Tseng, C., Dean, S., Davies, B. A., Azmi, I. F., Pashkova, N., Payne, J. A., Staffenhagen, J., West, M., Piper, R. C., Odorizzi, G., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.27.223255

Abscission Checkpoint Bodies Reveal a New Facet of Abscission Checkpoint ControlPreprint

Williams, L. K., Mackay, D. R., Whitney, M. A., Sundquist, W. I., & Ullman, K. S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.07.330290

Cellular Functions and Molecular Mechanisms of the ESCRT Membrane-Scission Machinery

Christ, L., Raiborg, C., Wenzel, E. M., Campsteijn, C., & Stenmark, H. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.08.016 · Cited by 474

ESCRT Is a Great Sealer: Non-Endosomal Function of the ESCRT Machinery in Membrane Repair and Autophagy

Isono, E. (2021) · Plant and Cell Physiology · doi:10.1093/pcp/pcab045 · Cited by 47

ESCRTs in membrane sealing

Radulovic, M., & Stenmark, H. (2018) · Biochemical Society Transactions · doi:10.1042/bst20170435 · Cited by 44

ESCRT‐III and Vps4: a dynamic multipurpose tool for membrane budding and scission

Adell, M. A. Y., Migliano, S. M., & Teis, D. (2016) · FEBS Journal · doi:10.1111/febs.13688 · Cited by 131

Membrane budding and scission by the ESCRT machinery: it's all in the neck

Hurley, J. H., & Hanson, P. I. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2937 · Cited by 793