The DOI matches its Crossref record; 154 of the 154 references it cites were found in a registry or an index.
Biogenesis and Function of Multivesicular Bodies
Open accessAbstract
The two major cellular sites for membrane protein degradation are the proteasome and the lysosome. Ubiquitin attachment is a sorting signal for both degradation routes. For lysosomal degradation, ubiquitination triggers the sorting of cargo proteins into the lumen of late endosomal multivesicular bodies (MVBs)/endosomes. MVB formation occurs when a portion of the limiting membrane of an endosome invaginates and buds into its own lumen. Intralumenal vesicles are degraded when MVBs fuse to lysosomes. The proper delivery of proteins to the MVB interior relies on specific ubiquitination of cargo, recognition and sorting of ubiquitinated cargo to endosomal subdomains, and the formation and scission of cargo-filled intralumenal vesicles. Over the past five years, a number of proteins that may directly participate in these aspects of MVB function and biogenesis have been identified. However, major questions remain as to exactly what these proteins do at the molecular level and how they may accomplish these tasks.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“For instance, actin-myosin interactions appear critical to the formation of all four types of EVs [66, 85, 100, 115].”
From Biogenesis of extracellular vesicles (EV): exosomes, microvesicles, retrovirus-like vesicles, and apoptotic bodies (2013) · cites this paper as [115]
Citations
Cites
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
Global analysis of protein localization in budding yeast
Huh, W.-K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., & O'Shea, E. K. (2003) · Nature · doi:10.1038/nature02026 · Cited by 4,248 · cited 1×
“Although loss of Sna3 does not cause a sorting defect, other Sna3-like candidates exist among other polytopic membrane proteins that localize to the vacuolar lumen and exhibit no known function (Huh et al. 2003).”
BackgroundPan, B., & Johnstone, R. M. (1983) · Cell · doi:10.1016/0092-8674(83)90040-5 · Cited by 2,042
Théry, C., Boussac, M., Véron, P., Ricciardi‐Castagnoli, P., Raposo, G., Garin, J., & Amigorena, S. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.12.7309 · Cited by 1,564
Heijnen, H. F. G., Schiel, A. E., Fijnheer, R., Geuze, H. J., & Sixma, J. J. (1999) · Blood · doi:10.1182/blood.v94.11.3791 · Cited by 1,488
Katzmann, D. J., Babst, M., & Emr, S. D. (2001) · Cell · doi:10.1016/s0092-8674(01)00434-2 · Cited by 1,473
Self-citationEscola, J.-M., Kleijmeer, M. J., Stoorvogel, W., Griffith, J. M., Yoshie, O., & Geuze, H. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.20121 · Cited by 1,228
Receptor downregulation and multivesicular-body sorting
Katzmann, D. J., Odorizzi, G., & Emr, S. D. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm973 · Cited by 1,201
Self-citationRegulation of Membrane Protein Transport by Ubiquitin and Ubiquitin-Binding Proteins
Hicke, L., & Dunn, R. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.110701.154617 · Cited by 1,131
Localization of phosphatidylinositol 3-phosphate in yeast and mammalian cells
Gillooly, D. J., Morrow, I. C., Lindsay, M., Gould, R., Bryant, N. J., Gaullier, J., Parton, R. G., & Stenmark, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.17.4577 · Cited by 1,031
Research works printed but not linked: 1
- van Deurs B, 1993, Eur. J. Cell Biol., 61, 208
Cited by
Sorted by citations
Items 501–600 of 769
Rost-Roszkowska, M. M., Poprawa, I., Hyra, M., Marek-Swędzioł, M., & Kaczmarek, Ł. (2013) · Journal of Limnology · doi:10.4081/jlimnol.2013.s1.e7 · Cited by 14
Vild, C. J., & Xu, Z. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.532960 · Cited by 15
Conserved and Distinct Elements of Phagocytosis in Human and C. elegans
Lukácsi, S., Farkas, Z., Saskői, É., Bajtay, Z., & Takács‐Vellai, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168934 · Cited by 15
Urine proteomic profiling in patients with nephrolithiasis and cystinuria
Kovacevic, L. G., Caruso, J. A., Lu, H., Kovacevic, N., Lakshmanan, Y., Carruthers, N. J., & Goldfarb, D. S. (2018) · International Urology and Nephrology · doi:10.1007/s11255-018-2044-1 · Cited by 14
Souza-Imberg, A., Carneiro, S. M., Giannotti, K. C., Sant’Anna, S. S., & Yamanouye, N. (2017) · Toxicon · doi:10.1016/j.toxicon.2017.06.013 · Cited by 15
Zhang, G., Huang, X., Yang, J., Zhang, J., Ma, Y., Hu, Y., Lu, S., Li, S., Song, Z., Li, C., et al. (2025) · International Journal of Nanomedicine · doi:10.2147/ijn.s510937 · Cited by 15
Benyair, R., Giridharan, S. S. P., Rivero-Ríos, P., Hasegawa, J., Bristow, E., Eskelinen, E., Shmueli, M. D., Fishbain-Yoskovitz, V., Merbl, Y., Sharkey, L. M., et al. (2023) · Autophagy Reports · doi:10.1080/27694127.2023.2166722 · Cited by 13
Endocytic trafficking of connexins in cancer pathogenesis
Totland, M. Z., Omori, Y., Sørensen, V., Kryeziu, K., Aasen, T., Brech, A., & Leithe, E. (2023) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166812 · Cited by 13
Identification of potential novel proteomic markers of Leishmania spp.-derived exosomes
Filho, A. D. S. L., Lafleur, A., Marcet‐Palacios, M., & Olivier, M. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1354636 · Cited by 13
Jalagadugula, G. S., Mao, G., Goldfinger, L. E., Wurtzel, J. G. T., Carpio‐Cano, F. D., Lambert, M. P., Estevez, B., French, D. L., Poncz, M., & Rao, A. K. (2022) · Blood Advances · doi:10.1182/bloodadvances.2021006945 · Cited by 13
Pulmonary Surfactant Trafficking and Homeostasis
Alcorn, J. L. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-803809-3.00004-x · Cited by 16
Morphology and fine organization of the midgut of Gampsocleis gratiosa (Orthoptera: Tettigoniidae)
Li, K., Zhang, J., Yang, Y.-J., Han, W., & Yin, H. (2018) · PLoS ONE · doi:10.1371/journal.pone.0200405 · Cited by 13
Advances in the diagnosis of exosomal miRNAs in ischemic stroke
Yu, P., & Chen, W. (2019) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s216784 · Cited by 13
Cullin-3 and the endocytic system
Hubner, M., & Peter, M. (2012) · Cellular Logistics · doi:10.4161/cl.20372 · Cited by 13
Cathepsins: Getting in Shape for Lysosomal Proteolysis
Erickson, A. H., Isidoro, C., Mach, L., & Mort, J. S. (2013) · Springer eBooks · doi:10.1007/978-3-7091-0885-7_4 · Cited by 14
Exosomal Long Noncoding RNAs in NSCLC: Dysfunctions and Clinical Potential
Lin, H., Li, J., Wang, M., Zhang, X., & Zhu, T. (2023) · Journal of Cancer · doi:10.7150/jca.84506 · Cited by 15
Boyer, E., Deltenre, L., Dourte, M., Colmant, L., Paître, E., Sleegers, K., Suelves, N., Hanseeuw, B. J., & Kienlen‐Campard, P. (2024) · Alzheimer s Research & Therapy · doi:10.1186/s13195-024-01508-6 · Cited by 16
Hemifusomes and interacting proteolipid nanodroplets mediate multi-vesicular body formation
Tavakoli, A., Hu, S., Ebrahim, S., & Kachar, B. (2025) · Nature Communications · doi:10.1038/s41467-025-59887-9 · Cited by 12
Ubiquitin-like 3 as a new protein-sorting factor for small extracellular vesicles
Takanashi, Y., Kahyo, T., Kamamoto, S., Zhang, H., Chen, B., Ping, Y., Mizuno, K., Kawase, A., Koizumi, K., Satou, M., et al. (2022) · Cell Structure and Function · doi:10.1247/csf.21078 · Cited by 14
Compartmentalization of Proteolysis
Brix, K., Scott, C. J., & Heck, M. M. S. (2013) · Springer eBooks · doi:10.1007/978-3-7091-0885-7_3 · Cited by 12
Vistro, W. A., Tarique, I., Haseeb, A., Yang, P., Huang, Y., Chen, H., Bai, X., Fazlani, S. A., & Chen, Q. (2019) · Micron · doi:10.1016/j.micron.2019.102747 · Cited by 12
Aoyama, N., Yamakawa, T., Sasamura, T., Yoshida, Y., Ohori, M., Okubo, H., Iida, E., Sasaki, N., Ueda, R., & Matsuno, K. (2013) · Genes & Genetic Systems · doi:10.1266/ggs.88.45 · Cited by 12
Transcription factor FOXM1 specifies chromatin DNA to extracellular vesicles
Zhang, Y., Ding, N., Li, Y., Zhao, X., Yang, S., Fu, P., Peng, Y., Cheng, H., Ouyang, M., 王瑞平, et al. (2023) · Autophagy · doi:10.1080/15548627.2023.2284523 · Cited by 15
Hepatitis B virus entry, assembly, and egress
Chuang, Y.-C., & Ou, J. J. (2024) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00014-24 · Cited by 11
Ahmad, I. S., Hussein, A., Kanabar, B. K., Kumar, A., Ramachandran, T., Shankhyan, A., Karthikeyan, A. S., Thatoi, D. N., Aminov, Z., Samarkhazan, H. S., et al. (2025) · Cellular Immunology · doi:10.1016/j.cellimm.2025.104986 · Cited by 12
Gao, X., Mazière, A. M. G. L. D., Iaea, D. B., Arthur, C. P., Klumperman, J., Ciferri, C., & Hannoush, R. N. (2019) · Scientific Reports · doi:10.1038/s41598-019-43285-5 · Cited by 11
Wilson, D. W. (2021) · Viruses · doi:10.3390/v13081622 · Cited by 12
Castroflorio, E., Perez-Berna, A. J., López‐Márquez, A., Badosa, C., Loza‐Álvarez, P., Roldán, M., & Jimenez-Mallebrera, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147651 · Cited by 11
DRAM1 Promotes Lysosomal Delivery of Mycobacterium marinum in Macrophages
Banducci-Karp, A., Xie, J., Engels, S. A. G., Sarantaris, C., van Hage, P., Varela, M., Meijer, A. H., & van der Vaart, M. (2023) · Cells · doi:10.3390/cells12060828 · Cited by 11
Gα s protein binds ubiquitin to regulate epidermal growth factor receptor endosomal sorting
Li, X., Létourneau, D., Holleran, B. J., Leduc, R., Lavigne, P., & Lavoie, C. L. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1708215114 · Cited by 11
All the Same? The Secret Life of Prion Strains within Their Target Cells
Vorberg, I. M. (2019) · Viruses · doi:10.3390/v11040334 · Cited by 11
Pathogen-host interaction mediated by vesicle-based secretion in schistosomes
Bischofsberger, M., Winkelmann, F., Rabes, A., Reisinger, E. C., & Sombetzki, M. (2020) · PROTOPLASMA · doi:10.1007/s00709-020-01515-y · Cited by 11
Hu, F., Liu, J., Liu, H., Li, F., Wan, M., Zhang, M., Jiang, Y., & Rao, M. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.700168 · Cited by 11
Lymphatic and Blood Endothelial Extracellular Vesicles: A Story Yet to Be Written
Trisko, J., Fleck, J., Kau, S., Oesterreicher, J., & Holnthoner, W. (2022) · Life · doi:10.3390/life12050654 · Cited by 11
Marks, M. S. (2007) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2007.00421.x · Cited by 11
Turégano-López, M., Santuy, A., DeFelipe, J., & Merchán-Pérez, Á. (2019) · Cerebral Cortex · doi:10.1093/cercor/bhz211 · Cited by 12
Wang, Y., Hu, M., Spanos, M., Xu, S., Song, J., Li, G., Crețoiu, D., & Xiao, J. (2026) · 中国科学通报:英文版 · doi:10.1016/j.scib.2026.01.067 · Cited by 10
Chander, A. M., Teixeira, M. D. M., Singh, N. K., Williams, M. P., Parker, C. W., Leo, P., Stajich, J., Torok, T., Tighe, S. W., Mason, C. E., et al. (2024) · Scientific Reports · doi:10.1038/s41598-024-61115-1 · Cited by 11
Autophagy in endosomal mutants
Michelet, X., & Legouis, R. (2012) · Worm · doi:10.4161/worm.20848 · Cited by 11
The coordinating role of IQGAP1 in the regulation of local, endosome-specific actin networks
Samson, E. B., Tsao, D., Zimak, J., McLaughlin, R. T., Trenton, N. J., Mace, E. M., Orange, J. S., Schweikhard, V., & Diehl, M. R. (2017) · Biology Open · doi:10.1242/bio.022624 · Cited by 10
Pellicciari, C., Giagnacovo, M., Cisterna, B., Costanzo, M., Croce, A. C., Bottiroli, G. F., & Malatesta, M. (2012) · Histochemistry and Cell Biology · doi:10.1007/s00418-012-1071-8 · Cited by 10
VPS28, an ESCRT-I protein, regulates mitotic spindle organization via Gβγ, EG5 and TPX2
Dionisio-Vicuña, M. N., Gutiérrez-López, T. Y., Adame-Garcia, S. R., Vázquez‐Prado, J., & Reyes‐Cruz, G. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.03.005 · Cited by 11
The Arabidopsis USL1 controls multiple aspects of development by affecting late endosome morphology
Yuan, R., Lan, J., Fang, Y., Yu, H. Q., Zhang, J., Huang, J., & Qin, G. (2018) · New Phytologist · doi:10.1111/nph.15249 · Cited by 10
Socially Distanced Intercellular Communication: Mechanisms for Extracellular Vesicle Cargo Delivery
Popa, S. J., & Stewart, S. E. (2021) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-67171-6_8 · Cited by 10
Delevoye, C., Giordano, F., Marks, M. S., & Raposo, G. (2011) · Melanins and Melanosomes · doi:10.1002/9783527636150.ch9 · Cited by 10
Loss of NPC1 enhances phagocytic uptake and impairs lipid trafficking in microgliaPreprint
Colombo, A. V., Dinkel, L., Müller, S. A., Monasor, L. S., Schifferer, M., Cantuti‐Castelvetri, L., König, J., Vidatic, L., Brémovà-Ertl, T., Hecimovic, S. K., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/789511 · Cited by 10
MicroRNA193a: An Emerging Mediator of Glomerular Diseases
Bharati, J., Kumar, M., Kumar, N. M., Malhotra, A., & Singhal, P. C. (2023) · Biomolecules · doi:10.3390/biom13121743 · Cited by 9
Beltrán, F. A., Torres-Díaz, L., Troncoso-Escudero, P., Villalobos-González, J., Mayorga-Weber, G. A., Lara, M., Covarrubias‐Pinto, A., Valdivia, S., Vicencio, I., Papic, E., et al. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.12.001 · Cited by 9
Hilscher, J., Kapusi, E., Stöger, E., & Ibl, V. (2015) · PROTOPLASMA · doi:10.1007/s00709-015-0798-1 · Cited by 9
Nano-sized CA125 antigen glycocamouflage: Mucin - Extracellular vesicles alliance to watch?
Mitić, N., Kosanović, M., Milutinovic, B. S., Goč, S., Mladenović, D., Grubiša, I., & Janković, M. (2018) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2018.06.017 · Cited by 9
Cell Biology of the Chlamydial Inclusion
Kokes, M., & Valdivia, R. H. (2014) · ASM Press eBooks · doi:10.1128/9781555817329.ch8 · Cited by 9
Chiow, K. H., Tan, Y., Chua, R. Y. R., Huang, D., Ng, M. L., Torta, F. T., Wenk, M. R., & Wong, S. H. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0887-z · Cited by 9
Norgan, A. P., Lee, J. R. E., Oestreich, A. J., Payne, J. A., Krueger, E., & Katzmann, D. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052603 · Cited by 8
Self-citationGonzález, J. B., García-Expósito, L., Puigdomènech, I., de Armas‐Rillo, L., Machado, J. D., Blanco, J., & Valenzuela-Fernández, A. (2011) · Communicative & Integrative Biology · doi:10.4161/cib.16716 · Cited by 12
Fong, Z., & Lee, W.-L. (2022) · Future Medicinal Chemistry · doi:10.4155/fmc-2021-0332 · Cited by 9
Bandyopadhyay, D., Basu, S., Mukherjee, I., Chakrabarti, S., Chakrabarti, P., Mukherjee, K., & Bhattacharyya, S. N. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104999 · Cited by 8
Septin-coated microtubules promote maturation of multivesicular bodies by inhibiting their motility
Robinson, B. P., Bass, N. R., Bhakt, P., & Spiliotis, E. T. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202308049 · Cited by 8
Unlocking the Therapeutic Potential of Oral Cancer Stem Cell-Derived Exosomes
Kumar, P., Lakhera, R., Aggarwal, S., & Gupta, S. (2024) · Biomedicines · doi:10.3390/biomedicines12081809 · Cited by 8
A candidate loss-of-function variant in SGIP1 causes synaptic dysfunction and recessive parkinsonism
Decet, M., Scott, P., Kuenen, S., Meftah, D., Swerts, J., Calatayud, C., Gallego, S. F., Kaempf, N., Nachman, E., Praschberger, R., et al. (2024) · Cell Reports Medicine · doi:10.1016/j.xcrm.2024.101749 · Cited by 8
Su, X., de Oliveira, G. P., Marie, A., Greguš, M., Figueroa‐Navedo, A. M., Ghiran, I. C., & Ivanov, A. R. (2024) · Journal of Extracellular Vesicles · doi:10.1002/jev2.70024 · Cited by 11
Zhang, L., Wong, C. Y., & Shao, H. (2025) · Lab on a Chip · doi:10.1039/d5lc00053j · Cited by 9
Intervention of Bro1 in pH-Responsive Rim20 Localization in Saccharomyces cerevisiae
Boysen, J. H., Subramanian, S. L., & Mitchell, A. P. (2010) · Eukaryotic Cell · doi:10.1128/ec.00027-10 · Cited by 8
da Silva, H. B., Godoy, R. S. M., & Martins, G. F. (2019) · Journal of Medical Entomology · doi:10.1093/jme/tjz045 · Cited by 8
Moreira, R., Mendonça, L. S., & de Almeida, L. P. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212288 · Cited by 7
Removal of cellular protrusions
Inaba, M., Ridwan, S. M., & Antel, M. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.025 · Cited by 8
Romagnoli, G. G., Argenta, P., Katz, I., García, L. C., Alves, M., Regina, C., Cruz, P., & Barbuto, J. A. M. (2013) · Exosomes and Microvesicles · doi:10.5772/52069 · Cited by 8
Fonseca, T. H. S., Gomes, J. M., Alacoque, M., Vannier-Santos, M. A., Gomes, M. A., & Busatti, H. G. N. O. (2018) · Acta Tropica · doi:10.1016/j.actatropica.2018.11.005 · Cited by 8
Basal Budding and Replication of the Murine Leukemia Virus Are Independent of the Gag L Domains
Sabo, Y., Laham-Karam, N., & Bacharach, E. (2008) · Journal of Virology · doi:10.1128/jvi.00741-08 · Cited by 8
Pre-formation loading of extracellular vesicles with exogenous molecules using photoporation
Ramon, J., Pinheiro, C., Vandendriessche, C., Lozano−Andrés, E., Keersmaecker, H. D., Punj, D., Fraire, J. C., Geeurickx, E., Wauben, M. H. M., Vader, P., et al. (2025) · Journal of Nanobiotechnology · doi:10.1186/s12951-025-03640-3 · Cited by 9
Neem secretory cells: developmental cytology and indications of cell autotoxicity
Canaveze, Y., Scudeler, E. L., & Machado, S. R. (2020) · PROTOPLASMA · doi:10.1007/s00709-020-01580-3 · Cited by 7
Weihrauch, D., Keszler, Á., Broeckel, G., Aranda, E., Lindemer, B. J., & Lohr, N. L. (2024) · Photochemical & Photobiological Sciences · doi:10.1007/s43630-023-00522-1 · Cited by 7
Extracellular Vesicle (EV) Survivin for Cancer Diagnostics and Therapeutics: A Review
Wijaya, W., Phyu, S. M., & Jiang, S. (2024) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2908302 · Cited by 10
Kowalska, M., & Rupik, W. (2018) · Journal of Morphology · doi:10.1002/jmor.20806 · Cited by 7
Hadpech, S., Moonmuang, S., Chupradit, K., Yasamut, U., & Tayapiwatana, C. (2021) · Intervirology · doi:10.1159/000519241 · Cited by 8
Debra, a Protein Mediating Lysosomal Degradation, Is Required for Long-Term Memory in Drosophila
Kottler, B., Lampin-Saint-Amaux, A., Comas, D., Préat, T., & Goguel, V. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025902 · Cited by 7
Kwon, S. H., & Lim, Y. (2017) · ACS Macro Letters · doi:10.1021/acsmacrolett.7b00064 · Cited by 7
Regulation mechanism of microRNAs in cardiac cells-derived exosomes in cell crosstalk
Lin, S., Yang, Y., Zhou, Z., Li, W., Wang, X., Liu, Y., Bi, Y., & Mao, J. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1399850 · Cited by 6
Mirzaahmadi, B., Ahmadian, S., Haddadi, P., Nezhad‐Mokhtari, P., Nezamdoust, F. V., Yalameha, B., Chegeni, S. A., Rashidi, S., Mousakhani, A., Sokullu, E., et al. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02286-w · Cited by 10
Přikryl, D., Zhang, Y., Verma, S., & Melikyan, G. B. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1647166 · Cited by 6
Exosomes in cancer diagnosis based on the Latest Evidence: Where are We?
Jin, K., Lan, H., Han, Y., & Qian, J. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113133 · Cited by 6
Recycling of endocytic BDNF through extracellular vesicles in astrocytes
Han, J. H., & Park, H. (2025) · Scientific Reports · doi:10.1038/s41598-025-86200-x · Cited by 6
Urbanek, A., & Rost-Roszkowska, M. M. (2014) · Micron · doi:10.1016/j.micron.2014.11.003 · Cited by 6
High Dynamic Range Structured Illumination Microscope Based on Multiple Exposures
Liang, Y., Chen, X., Sun, Z., Wen, G., Chen, C., Wang, L., Jin, X., Zhang, J., Yang, G., Gao, J., et al. (2021) · Frontiers in Physics · doi:10.3389/fphy.2021.648174 · Cited by 6
Madloo, P., Lema, M., Cartea, M. E., & Soengas, P. (2021) · Microbiology Spectrum · doi:10.1128/spectrum.00180-21 · Cited by 6
ORP1L, ORP1S, and ORP2: Lipid Sensors and Transporters
Aw, Y. C., Brown, A. J., Wu, J., & Yang, H. (2020) · Contact · doi:10.1177/2515256420956818 · Cited by 6
Sojoudi, K., Azizi, H., & Skutella, T. (2023) · Biotechnology and Genetic Engineering Reviews · doi:10.1080/02648725.2023.2193772 · Cited by 6
Primavera‐Tirol, Y. H., Coloso, R. M., Quinitio, G. F., Aguilar, R. O., & Laureta, L. V. (2013) · Fish Physiology and Biochemistry · doi:10.1007/s10695-013-9870-y · Cited by 6
Bandyopadhyay, D., Basu, S., Mukherjee, I., Chakraborty, R., Mukherjee, K., Chattopadhyay, K., Chakrabarti, S., Chakrabarti, P., & Bhattacharyya, S. N. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.11.30.405449 · Cited by 6
Malak, M., Abdel-Moneim, A. M., & Shonouda, M. L. (2025) · Journal of Asia-Pacific Entomology · doi:10.1016/j.aspen.2025.102407 · Cited by 5
Enomoto, S., Hur, Y. H., Solodova, T., Neumann, J., Cerione, R. A., & Antonyak, M. A. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110821 · Cited by 5
Ioannou, S., Kay, A. G., Stone, A. P., Rand, E., Elberfeld, S., Bolton, W., Larson, T. R., Crossland, R. E., Kehoe, O., Mentlak, D. A., et al. (2025) · Stem Cell Research & Therapy · doi:10.1186/s13287-025-04665-z · Cited by 5
Vesicle-driven endomembrane systems in fungi
Pope, R. E., & Prade, R. A. (2025) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00297-24 · Cited by 5
Yin, J., Zhang, C., Zhang, Q., Long, F., Hu, W., Zhou, Y., Mou, F., Zhong, Y., Wu, B., Zhu, M., et al. (2024) · Frontiers in Plant Science · doi:10.3389/fpls.2024.1451897 · Cited by 5
Defects in Exosome Biogenesis Are Associated with Sensorimotor Defects in Zebrafish vps4a Mutants
Shipman, A., Gao, Y., Liu, D., Sun, S., Zang, J., Sun, P., Syed, Z., Bhagavathi, A., Smith, E. T., Erickson, T., et al. (2024) · Journal of Neuroscience · doi:10.1523/jneurosci.0680-24.2024 · Cited by 5
Microparticles are the basic storage units for different proteins in platelet granules
Zhang, C., & Yang, Y. (2012) · Blood · doi:10.1182/blood-2012-04-422907 · Cited by 5
RetractedSOCS2 Binds to and Regulates EphA2 through Multiple Mechanisms
Pilling, C., & Cooper, J. A. (2017) · Scientific Reports · doi:10.1038/s41598-017-11040-3 · Cited by 5
Chang, J., Lo, Z. H. Y., Alenizi, S., & Kovačević, Ž. (2023) · Cancers · doi:10.3390/cancers15102779 · Cited by 5
Xu, J., Nonogaki, M., Madhira, R., Ma, H., Hermanson, O., Kioussi, C., & Gross, M. K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048573 · Cited by 8
Exosome-mediated Antigen Delivery: Unveiling Novel Strategies in Viral Infection ControlPreprint
Safadi, D. E., Krejbich, M., MOKHTARI, A., Lagrave, A., Hirigoyen, U., Lebeau, G., Viranaïcken, W., & Trotot, P. K. (2024) · Preprints.org · doi:10.20944/preprints202401.0044.v1 · Cited by 5
Smart nano exosomes as precision drug carriers: a new frontier in targeted treatment of oral cancer
Mousavi, S. M., Abbasifard, M., Abbasi, R., Tivay, S., Hosseini, H., Taghipoor, M., Kalashgrani, M. Y., Aljabri, M. D., Rahman, M. M., Chiang, W., et al. (2025) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2025.125923 · Cited by 4
Metadata
- Authors
- Piper, R. C., & Katzmann, D. J.
- Affiliations
- University of Iowa (US)
- Mayo Clinic (US)
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2007-11-01
- Volume
- 23
- Issue
- 1
- Pages
- 519-547
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- PMC
- PMC2911632
- OpenAlex
- W2109691647
- Cited by
- 771
- References
- 154
- Citations by year
- 2026: 23 · 2025: 34 · 2024: 55 · 2023: 39 · 2022: 51 · 2021: 49 · 2020: 48 · 2019: 54 · 2018: 46 · 2017: 36 · 2016: 28 · 2015: 37 · 2014: 26 · 2013: 34 · 2012: 38
- FWCI
- 3.06
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Annual Review of Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM58202, R01GM73024, R01GM073024, R01GM058202)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- multivesicular bodies, endosomes, membrane protein degradation, ubiquitination, lysosomal degradation, proteasome, intralumenal vesicles, endosomal sorting, cargo sorting, membrane fission
- MeSH terms
- Animals, Humans, Lysosomes, Protein Conformation, Proteins, Endosomes, Protein Transport, Protein Sorting Signals, Ubiquitin, Lipid Metabolism, Ubiquitination
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