The Mechanisms of Vesicle Budding and Fusion

Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution

Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T. (1998) · Nature · doi:10.1038/26412 · Cited by 2,417

The Rab5 effector EEA1 is a core component of endosome docking

Christoforidis, S., McBride, H. M., Burgoyne, R. D., & Zerial, M. (1999) · Nature · doi:10.1038/17618 · Cited by 854

Inhibition by brefeldin A of a Golgi membrane enzyme that catalyses exchange of guanine nucleotide bound to ARF

Helms, J. B., & Rothman, J. E. (1992) · Nature · doi:10.1038/360352a0 · Cited by 746

ARH Is a Modular Adaptor Protein That Interacts with the LDL Receptor, Clathrin, and AP-2

He, G., Gupta, S., Yi, M., Michaely, P., Hobbs, H. H., & Cohen, J. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m208539200 · Cited by 232

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

SNAREs — engines for membrane fusion

Jahn, R., & Scheller, R. H. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2002 · Cited by 2,635

Molecular anatomy of a trafficking organelle

Takamori, S., Holt, M., Stenius, K., Lemke, E. A., Grønborg, M., Riedel, D., Urlaub, H., Schenck, S., Brügger, B., Ringler, P., et al. (2006) · Cell · doi:10.1016/j.cell.2006.10.030 · Cited by 2,373

Current knowledge on exosome biogenesis and release

Hessvik, N. P., & Llorente, A. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2595-9 · Cited by 2,362

Understanding the mechanism of IL-1β secretion

Lopez-Castejon, G., & Brough, D. (2011) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2011.10.001 · Cited by 1,519

Mitochondrial Fusion and Fission in Mammals

Chan, D. C. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104638 · Cited by 972

Rab5 is necessary for the biogenesis of the endolysosomal system in vivo

Zeigerer, A., Gilleron, J., Bogorad, R. L., Marsico, G., Nonaka, H., Seifert, S., Epstein-Barash, H., Kuchimanchi, S., Peng, C. G., Ruda, V. M., et al. (2012) · Nature · doi:10.1038/nature11133 · Cited by 362

The Vici Syndrome Protein EPG5 Is a Rab7 Effector that Determines the Fusion Specificity of Autophagosomes with Late Endosomes/Lysosomes

Wang, Z., Miao, G., Xue, X., Guo, X., Yuan, C., Wang, Z., Zhang, G., Chen, Y., Feng, D., Hu, J., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.08.021 · Cited by 321

Current Knowledge on Exosome Biogenesis, Cargo-Sorting Mechanism and Therapeutic Implications

Xie, S., Zhang, Q., & Jiang, L. (2022) · Membranes · doi:10.3390/membranes12050498 · Cited by 262

Hepatocyte polarity

Treyer, A., & Müsch, A. (2013) · Comprehensive Physiology · doi:10.1002/cphy.c120009 · Cited by 252

SNAREing immunity: the role of SNAREs in the immune system

Stow, J. L., Manderson, A. P., & Murray, R. Z. (2006) · Nature Reviews Immunology · doi:10.1038/nri1980 · Cited by 235

Insig required for sterol-mediated inhibition of Scap/SREBP binding to COPII proteins in vitro

Sun, L.-P., Li, L., Goldstein, J. L., & Brown, M. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504041200 · Cited by 223

Membrane tension and peripheral protein density mediate membrane shape transitions

Shi, Z., & Baumgart, T. (2015) · Nature Communications · doi:10.1038/ncomms6974 · Cited by 213

Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells

Haas, A. K., Yoshimura, S.-I., Stephens, D. J., Preisinger, C., Fuchs, E., & Barr, F. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.014225 · Cited by 201

Golgi coiled-coil proteins contain multiple binding sites for Rab family G proteins

Sinka, R., Gillingham, A. K., Kondylis, V., & Munro, S. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200808018 · Cited by 190

Genome-wide RNAi screening identifies human proteins with a regulatory function in the early secretory pathway

Simpson, J. C., Joggerst, B., Laketa, V., Verissimo, F., Cetin, C., Erfle, H., Bexiga, M. G., Singan, V. R., Hériché, J.-K., Neumann, B., et al. (2012) · Nature Cell Biology · doi:10.1038/ncb2510 · Cited by 186

Localization and function of Arf family GTPases

Donaldson, J. G., & Honda, A. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330639 · Cited by 170

Pericentrosomal targeting of Rab6 secretory vesicles by Bicaudal-D-related protein 1 (BICDR-1) regulates neuritogenesis

Schlager, M. A., Kapitein, L. C., Grigoriev, I., Burzynski, G. M., Wulf, P. S., Keijzer, N., de Graaff, E., Fukuda, M., Shepherd, I. T., Akhmanova, A., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.51 · Cited by 165

Dynamic Ca 2+ -Dependent Stimulation of Vesicle Fusion by Membrane-Anchored Synaptotagmin 1

Lee, H.-K., Yang, Y., Su, Z., Hyeon, C., Lee, T.-S., Lee, H.-W., Kweon, D.-H., Shin, Y.-K., & Yoon, T.-Y. (2010) · Science · doi:10.1126/science.1187722 · Cited by 123

Revisiting the Role of Clathrin-Mediated Endoytosis in Synaptic Vesicle Recycling

Milosevic, I. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00027 · Cited by 122

SEC24A deficiency lowers plasma cholesterol through reduced PCSK9 secretion

Chen, X.-W., Wang, H., Bajaj, K., Zhang, P., Meng, Z.-X., Ma, D., Bai, Y., Liu, H.-H., Adams, E., Baines, A., et al. (2013) · eLife · doi:10.7554/elife.00444 · Cited by 115

Golgi maturation‐dependent glycoenzyme recycling controls glycosphingolipid biosynthesis and cell growth via GOLPH3

Rizzo, R., Russo, D., Kurokawa, K., Sahu, P., Lombardi, B., Supino, D., Zhukovsky, M. A., Vocat, A., Pothukuchi, P., Kunnathully, V., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020107238 · Cited by 101

Evolutionary reconstruction of the retromer complex and its function in Trypanosoma brucei

Koumandou, V. L., Klute, M. J., Herman, E. K., Nunez-Miguel, R., Dacks, J. B., & Field, M. C. (2011) · Journal of Cell Science · doi:10.1242/jcs.081596 · Cited by 109

Mutant Huntingtin Impairs Vesicle Formation from Recycling Endosomes by Interfering with Rab11 Activity

Li, X., Standley, C., Sapp, E., Valencia, A., Qin, Z.-H., Kegel, K. B., Yoder, J., Comer-Tierney, L. A., Esteves, M., Chase, K., et al. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00420-09 · Cited by 105

Protein complexes containing CYFIP/Sra/PIR121 coordinate Arf1 and Rac1 signalling during clathrin–AP-1-coated carrier biogenesis at the TGN

Anitei, M., Stange, C., Parshina, I., Baust, T., Schenck, A., Raposo, G., Kirchhausen, T., & Hoflack, B. (2010) · Nature Cell Biology · doi:10.1038/ncb2034 · Cited by 102

The WASH complex, an endosomal Arp2/3 activator, interacts with the Hermansky–Pudlak syndrome complex BLOC-1 and its cargo phosphatidylinositol-4-kinase type IIα

Ryder, P. V., Vistein, R., Gokhale, A., Seaman, M. N., Puthenveedu, M. A., & Faundez, V. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-02-0088 · Cited by 87

The Contrasting Role of Extracellular Vesicles in Vascular Inflammation and Tissue Repair

Oggero, S., Austin-Williams, S., & Norling, L. V. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01479 · Cited by 85

Huntingtin differentially regulates the axonal transport of a sub-set of Rab-containing vesicles in vivo

White, J. A., Anderson, E., Zimmerman, K., Zheng, K. H., Rouhani, R., & Gunawardena, S. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv415 · Cited by 67

Bacterial genotoxins: The long journey to the nucleus of mammalian cells

Frisan, T. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2015.08.016 · Cited by 79

Conserved Prefusion Protein Assembly in Regulated Exocytosis

Rickman, C., Jiménez, J. L., Graham, M. E., Archer, D. A., Soloviev, M., Burgoyne, R. D., & Davletov, B. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-07-0620 · Cited by 74

RABIF/MSS4 is a Rab-stabilizing holdase chaperone required for GLUT4 exocytosis

Gulbranson, D. R., Davis, E. M., Demmitt, B. A., Ouyang, Y., Ye, Y., Yu, H., & Shen, J. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1712176114 · Cited by 67

Differential effect of exocytic SNAREs on the production of recombinant proteins in mammalian cells

Peng, R., Abellan, E., & Fussenegger, M. (2011) · Biotechnology and Bioengineering · doi:10.1002/bit.22986 · Cited by 61

AAGAB Controls AP2 Adaptor Assembly in Clathrin-Mediated Endocytosis

Gulbranson, D. R., Crisman, L., Lee, M., Ouyang, Y., Menasche, B. L., Demmitt, B. A., Wan, C., Nomura, T., Ye, Y., Yu, H., et al. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.06.013 · Cited by 57

Proteomic characterization of isolated Arabidopsis clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components

Dahhan, D. A., Reynolds, G. D., Cárdenas, J. J., Eeckhout, D., Johnson, A., Yperman, K., Kaufmann, W. A., Vang, N., Yan, X., Hwang, I., et al. (2022) · The Plant Cell · doi:10.1093/plcell/koac071 · Cited by 54

A role for Rab11 in the homeostasis of the endosome-lysosomal pathway

Zulkefli, K. L., Houghton, F. J., Gosavi, P., & Gleeson, P. A. (2019) · Experimental Cell Research · doi:10.1016/j.yexcr.2019.04.010 · Cited by 52

Recruitment of the Mint3 adaptor is necessary for export of the amyloid precursor protein (APP) from the Golgi complex.

Caster, A. H., & Kahn, R. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.481101 · Cited by 40

Out of the ESCPE room: Emerging roles of endosomal SNX‐BARs in receptor transport and host–pathogen interaction

Simonetti, B., Daly, J. L., & Cullen, P. J. (2023) · Traffic · doi:10.1111/tra.12885 · Cited by 39

Biomimetic Nanoplatform for Dual‐Targeted Clearance of Activated and Senescent Cancer‐Associated Fibroblasts to Improve Radiation Resistance in Breast Cancer

Jian, C., Wu, T., Wang, L., Gao, C., Fu, Z., Zhang, Q., & Shi, C. (2024) · Small · doi:10.1002/smll.202309279 · Cited by 33

Indirect estimation of the area density of Atg8 on the phagophore

Xie, Z., Nair, U., Geng, J., Szefler, M. B., Rothman, E. D., & Klionsky, D. J. (2009) · Autophagy · doi:10.4161/auto.5.2.7201 · Cited by 26

The protein secretory pathway of Candida albicans

Fonzi, W. A. (2009) · Mycoses · doi:10.1111/j.1439-0507.2008.01673.x · Cited by 25

Exploring the MACH Model’s Potential as a Metacognitive Tool to Help Undergraduate Students Monitor Their Explanations of Biological Mechanisms

Trujillo, C. M., Anderson, T. R., & Pelaez, N. J. (2016) · CBE—Life Sciences Education · doi:10.1187/cbe.15-03-0051 · Cited by 19

Regulation of cargo exocytosis by a Reps1-Ralbp1-RalA module

Wang, S., Chen, X., Crisman, L., Dou, X., Winborn, C. S., Wan, C., Puscher, H., Yin, Q., Kennedy, M. J., & Shen, J. (2023) · Science Advances · doi:10.1126/sciadv.ade2540 · Cited by 14

Biogenesis of Melanosomes

Delevoye, C., Giordano, F., Marks, M. S., & Raposo, G. (2011) · Melanins and Melanosomes · doi:10.1002/9783527636150.ch9 · Cited by 10

Golgi‐associated retrograde protein ( GARP ) complex recruits retromer to trans ‐Golgi network for FgKex2 and FgSnc1 recycling, necessary for the development and pathogenicity of Fusarium graminearum

Long, Y., Chen, X., Chen, J., Zhang, H., Lin, Y., Cheng, S., Pu, N., Zhou, X., Sheng, R., Abubakar, Y. S., et al. (2025) · New Phytologist · doi:10.1111/nph.70006 · Cited by 7