Clathrin

Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons

Nicholls, A. O., Sharp, K. A., & Honig, B. H. (1991) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,230

β-Arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptor

Goodman, O. B., Krupnick, J. G., Santini, F., Gurevich, V. V., Penn, R. B., Gagnon, A. W., Keen, J. H., & Benovic, J. (1996) · Nature · doi:10.1038/383447a0 · Cited by 1,383

YOLK PROTEIN UPTAKE IN THE OOCYTE OF THE MOSQUITO AEDES AEGYPTI. L

Roth, T. F., & Porter, K. R. (1964) · The Journal of Cell Biology · doi:10.1083/jcb.20.2.313 · Cited by 1,320

The structure of the G protein heterotrimer Giα1β1γ2

Wall, M. A., Coleman, D. E., Lee, E. N., Iñiguez-Lluhı́, J. A., Posner, B. A., Gilman, A. G., & Sprang, S. R. (1995) · Cell · doi:10.1016/0092-8674(95)90220-1 · Cited by 1,140

The 2.0 Å crystal structure of a heterotrimeric G protein

Lambright, D. G., Sondek, J., Bohm, A., Skiba, N. P., Hamm, H. E., & Sigler, P. B. (1996) · Nature · doi:10.1038/379311a0 · Cited by 1,136

Role of β-Arrestin in Mediating Agonist-Promoted G Protein-Coupled Receptor Internalization

Ferguson, S. S. G., Downey, W. E., Colapietro, A.-M., Barak, L. S., Ménard, L., & Caron, M. G. (1996) · Science · doi:10.1126/science.271.5247.363 · Cited by 974

Interaction of Tyrosine-Based Sorting Signals with Clathrin-Associated Proteins

Ohno, H., Stewart, J., Fournier, M.-C., Bosshart, H., Rhee, I. P., Miyatake, S., Saito, T., Gallusser, A., Kirchhausen, T. L., & Bonifacino, J. S. (1995) · Science · doi:10.1126/science.7569928 · Cited by 971

Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding

Hinshaw, J. E., & Schmid, S. L. (1995) · Nature · doi:10.1038/374190a0 · Cited by 824

CLATHRIN-COATED VESICLE FORMATION AND PROTEIN SORTING: An Integrated Process

Schmid, S. L. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.511 · Cited by 800

Dynamin-like protein encoded by the Drosophila shibire gene associated with vesicular traffic

van der Bliek, A. M., & Meyerowrtz, E. M. (1991) · Nature · doi:10.1038/351411a0 · Cited by 776

Quantitative proteomics reveals reduction of endocytic machinery components in gliomas

Buser, D. P., Ritz, M., Moes, S., Tostado, C., Frank, S., Spiess, M., Mariani, L., Jenö, P., Boulay, J., & Hütter, G. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.07.039 · Cited by 31

Hybrid continuum-particle method for fluctuating lipid bilayer membranes with diffusing protein inclusions

Sigurdsson, J. K., Brown, F. L. H., & Atzberger, P. J. (2013) · Journal of Computational Physics · doi:10.1016/j.jcp.2013.06.016 · Cited by 31

Role of clathrin in the regulated secretory pathway of pancreaticβ-cells

Molinete, M., Dupuis, S., Brodsky, F. M., & Halban, P. A. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.16.3059 · Cited by 31

Comparison of Approximate Methods for Calculating the Friction Coefficient and Intrinsic Viscosity of Nanoparticles and Macromolecules

Mansfield, M. L., Douglas, J. F., Irfan, S., & Kang, E. (2007) · Macromolecules · doi:10.1021/ma061069f · Cited by 31

Brain‐specific functions of the endocytic machinery

Camblor‐Perujo, S., & Kononenko, N. L. (2021) · FEBS Journal · doi:10.1111/febs.15897 · Cited by 33

Cellular and viral peptides bind multiple sites on the N‐terminal domain of clathrin

Muenzner, J., Traub, L. M., Kelly, B. T., & Graham, S. C. (2016) · Traffic · doi:10.1111/tra.12457 · Cited by 29

Clathrin-Mediated Endocytosis

McPherson, P. S., Ritter, B., & Wendland, B. (2009) · Springer eBooks · doi:10.1007/978-0-387-93877-6_9 · Cited by 31

Radiolabeled Liposomes for Nuclear Imaging Probes

Low, H. Y., Yang, C., Xia, B., He, T., Lam, W. W.-C., & Ng, D. C. E. (2023) · Molecules · doi:10.3390/molecules28093798 · Cited by 29

Non-Natural Cell Surface Receptors: Synthetic Peptides Capped with N-Cholesterylglycine Efficiently Deliver Proteins into Mammalian Cells

Martin, S. E., & Peterson, B. R. (2002) · Bioconjugate Chemistry · doi:10.1021/bc025601p · Cited by 29

When less is more – a fast TurboID knock-in approach for high-sensitivity endogenous interactome mapping

Stockhammer, A., Spalt, C., Klemt, A., Benz, L. S., Harel, S., Natalia, V., Wiench, L., Freund, C., Kuropka, B., & Bottanelli, F. (2024) · Journal of Cell Science · doi:10.1242/jcs.261952 · Cited by 26

Chapter 4 Protein Trafficking in Polarized Cells

Duffield, A. S., Caplan, M. J., & Muth, T. R. (2008) · International review of cytology · doi:10.1016/s1937-6448(08)01404-4 · Cited by 29

Conformation of a Clathrin Triskelion in Solution

Ferguson, M., Prasad, K., Sackett, D. L., Boukari, H., Lafer, E. M., & Nossal, R. (2006) · Biochemistry · doi:10.1021/bi052568w · Cited by 29

Clathrin-Mediated Post-Golgi Membrane Trafficking in the Morphogenesis of Hepatitis Delta Virus

Huang, C., Chang, S. C., Yang, H.-C., Chien, C. L., & Chang, M. (2009) · Journal of Virology · doi:10.1128/jvi.01044-09 · Cited by 29

Laa1p, a Conserved AP-1 Accessory Protein Important for AP-1 Localization in Yeast

Fernández, G. E., & Payne, G. S. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-02-0096 · Cited by 29

Structural Requirements for Interactions between Leucine-sorting Signals and Clathrin-associated Adaptor Protein Complex AP3

Rodionov, D., Höning, S., Silye, A., Kongsvik, T. L., FIGURA, K. V., & Bakke, O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207149200 · Cited by 29

Dissection of Swa2p/Auxilin Domain Requirements for Cochaperoning Hsp70 Clathrin-uncoating Activity In Vivo

Xiao, J., Kim, L. S., & Graham, T. R. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-02-0106 · Cited by 29

Nanostructures: between natural environment and medical practice

Trovato, M. C., Andronico, D., Sciacchitano, S., Ruggeri, R. M., Picerno, I., Pietro, A. D., & Visalli, G. (2018) · Reviews on Environmental Health · doi:10.1515/reveh-2017-0036 · Cited by 28

Characterization of herpes simplex virus type 1 L ‐particle assembly and egress in hippocampal neurones by electron cryo‐tomography

Ibiricu, I., Maurer, U. E., & Grünewald, K. (2012) · Cellular Microbiology · doi:10.1111/cmi.12093 · Cited by 28

Key Interactions for Clathrin Coat Stability

Böcking, T., Aguet, F., Rapoport, I., Banzhaf, M., Yu, A., Zeeh, J.-C., & Kirchhausen, T. L. (2014) · Structure · doi:10.1016/j.str.2014.04.002 · Cited by 28

Clathrin Triskelia Show Evidence of Molecular Flexibility

Ferguson, M., Prasad, K., Boukari, H., Sackett, D. L., Krueger, S., Lafer, E. M., & Nossal, R. (2008) · Biophysical Journal · doi:10.1529/biophysj.107.126342 · Cited by 28

Structures and pathways for clathrin self-assembly in the bulk and on membranes

Matthews, R., & Likos, C. N. (2013) · Soft Matter · doi:10.1039/c3sm50737h · Cited by 28

The ubiquitin-dependent endocytosis motif is required for efficient incorporation of growth hormone receptor in clathrin-coated pits, but not clathrin-coated lattices

Sachse, M., van Kerkhof, P., Strous, G. J., & Klumperman, J. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.21.3943 · Cited by 28

Heterogeneity of endocytic proteins: distribution of clathrin adaptor proteins in neurons and glia

Yao, P. J., Zhang, P., Mattson, M. P., & Furukawa, K. (2003) · Neuroscience · doi:10.1016/s0306-4522(03)00431-7 · Cited by 28

Clathrin-Dependent Targeting of Receptors to the Flagellar Pocket of Procyclic-Form Trypanosoma brucei

Hung, C., Qiao, X., Lee, P.-T., & Lee, M. G.-S. (2004) · Eukaryotic Cell · doi:10.1128/ec.3.4.1004-1014.2004 · Cited by 28

Experimental approaches to the interaction of the prion protein with nucleic acids and glycosaminoglycans: Modulators of the pathogenic conversion

Silva, J. L., Vieira, T. C. R. G., Gomes, M. P. B., Rangel, L. P., Scapin, S. M. N., & Cordeiro, Y. (2010) · Methods · doi:10.1016/j.ymeth.2010.12.002 · Cited by 27

Investigation of the pathway dependent endocytosis of gold nanoparticles by surface-enhanced Raman scattering

Yılmaz, D., & Çulha, M. (2021) · Talanta · doi:10.1016/j.talanta.2020.122071 · Cited by 28

The role of F-actin in modulating Clathrin-mediated endocytosis: Lessons from neurons in health and neuropsychiatric disorder

Loebrich, S. (2014) · Communicative & Integrative Biology · doi:10.4161/cib.28740 · Cited by 30

Monomeric but not trimeric clathrin heavy chain regulates p53-mediated transcription

Ohmori, K., Endo, Y., Yoshida, Y., Ohata, H., Taya, Y., & Enari, M. (2007) · Oncogene · doi:10.1038/sj.onc.1210854 · Cited by 27

Rat Neuronal Leucine-Rich Repeat Protein-3: Cloning and Regulation of the Gene Expression

Fukamachi, K., Matsuoka, Y., Kitanaka, C., Kuchino, Y., & Tsuda, H. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5579 · Cited by 27

Visualizing the effect of dynamin inhibition on annular gap vesicle formation and fission

Nickel, B. M., Boller, M. J., Schneider, K., Shakespeare, T. I., GAY, V. L., & Murray, S. (2013) · Journal of Cell Science · doi:10.1242/jcs.116269 · Cited by 27

Intra-Golgi Transport: Roles for Vesicles, Tubules, and Cisternae

Martínez‐Menárguez, J. A. (2013) · ISRN Cell Biology · doi:10.1155/2013/126731 · Cited by 29

Tom1l2 hypomorphic mice exhibit increased incidence of infections and tumors and abnormal immunologic response

Girirajan, S., Hauck, P. M., Williams, S. R., Vlangos, C. N., Szomju, B. B., Solaymani-Kohal, S., Mosier, P. D., White, K. L., McCoy, K. L., & Elsea, S. H. (2008) · Mammalian Genome · doi:10.1007/s00335-008-9100-6 · Cited by 31

Clathrin/AP-2-Dependent Endocytosis: A Novel Playground for the Pharmacological Toolbox?

Rodemer, C., & Haucke, V. (2008) · Handbook of experimental pharmacology · doi:10.1007/978-3-540-72843-6_5 · Cited by 30

Conservation and divergence within the clathrin interactome of Trypanosoma cruzi

Kalb, L. C., Toner, Y. C., Boehm, C., Moreira, C. M. D. N., Soares, M. J., & Field, M. C. (2016) · Scientific Reports · doi:10.1038/srep31212 · Cited by 24

Nanocarriers as Nanomedicines

Grazú, V., Moros, M., & Sánchez‐Espinel, C. (2012) · Frontiers of nanoscience · doi:10.1016/b978-0-12-415769-9.00014-5 · Cited by 27

Hydrogen-Bonding Density of Supramolecular Self-Assembled Fibrillar Networks Probed Using Synchrotron Infrared Spectromicroscopy

Rogers, M. A., Pedersen, T., & Quaroni, L. G. (2009) · Crystal Growth & Design · doi:10.1021/cg900370g · Cited by 26

Recruitment of Cellular Clathrin to Viral Factories and Disruption of Clathrin‐Dependent Trafficking

Ivanovic, T., Boulant, S., Ehrlich, M., Demidenko, A. A., Arnold, M. M., Kirchhausen, T. L., & Nibert, M. L. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01233.x · Cited by 26

Studies of Synaptic Vesicle Endocytosis in the NematodeC. elegans

Harris, T. W., Schuske, K. R., & Jørgensen, E. M. (2001) · Traffic · doi:10.1034/j.1600-0854.2001.002009597.x · Cited by 26

Functional evidence for the identification of an Arabidopsis clathrin light chain polypeptide

Scheele, U., & Holstein, S. E. H. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02439-0 · Cited by 26

Interaction of amphiphysins with AP-1 clathrin adaptors at the membrane

Huser, S., Suri, G., Crottet, P., & Spiess, M. (2012) · Biochemical Journal · doi:10.1042/bj20121373 · Cited by 25

Exosomes: Mediators in microenvironment of colorectal cancer

Yao, J., Chen, Y., & Lin, Z. (2023) · International Journal of Cancer · doi:10.1002/ijc.34471 · Cited by 27

Nuclear Trafficking and Functions of Endocytic Proteins Implicated in Oncogenesis

Borlido, J., Zecchini, V. R., & Mills, I. G. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00922.x · Cited by 25

Functional equivalence of the clathrin heavy chains CHC17 and CHC22 in endocytosis and mitosis

Hood, F. E., & Royle, S. (2009) · Journal of Cell Science · doi:10.1242/jcs.046177 · Cited by 25

AP180-Mediated Trafficking of Vamp7B Limits Homotypic Fusion ofDictyosteliumContractile Vacuoles

Wen, Y., Stavrou, I., Bersuker, K., Brady, R. J., Lozanne, A. D., & O’Halloran, T. J. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-03-0243 · Cited by 25

Chemical-genetic disruption of clathrin function spares adaptor complex 3–dependent endosome vesicle biogenesis

Zlatic, S. A., Grossniklaus, E. J., Ryder, P. V., Salazar, G., Mattheyses, A. L., Peden, A. A., & Faúndez, V. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-12-0860 · Cited by 25

Rotational Brownian Dynamics simulations of clathrin cage formation

Ilie, I. M., den Otter, W. K., & Briels, W. J. (2014) · The Journal of Chemical Physics · doi:10.1063/1.4891306 · Cited by 25

Shotgun Proteomic Analysis of Emiliania huxleyi, a Marine Phytoplankton Species of Major Biogeochemical Importance

Jones, B., Edwards, R. J., Skipp, P. J. S., O’Connor, C. D., & Iglesias-Rodriguez, M. D. (2010) · Marine Biotechnology · doi:10.1007/s10126-010-9320-0 · Cited by 25

Clathrin Interactions with C‐Terminal Regions of the Yeast AP‐1 β and γ Subunits are Important for AP‐1 Association with Clathrin Coats

Yeung, B. G., & Payne, G. S. (2001) · Traffic · doi:10.1034/j.1600-0854.2001.20806.x · Cited by 25

Acid-base effects on intestinal Na+ absorption and vesicular trafficking

Charney, A. N., Egnor, R. W., Alexander-Chacko, J. T., Cassai, N. D., & Sidhu, G. S. (2002) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00079.2002 · Cited by 25

A Systematic Review of the Toxicokinetics of Micro- and Nanoplastics in Mammals Following Digestive Exposure

Popa, R., & Tăbăran, F. (2025) · Applied Sciences · doi:10.3390/app15116135 · Cited by 28

Protein-induced membrane curvature in coarse-grained simulations

Mandal, T., Spagnolie, S. E., Audhya, A., & Cui, Q. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.05.029 · Cited by 24

Contribution of Cysteines to Clathrin Trimerization Domain Stability and Mapping of Light Chain Binding

Ybe, J. A., Ruppel, N. J., Mishra, S., & VanHaaften, E. (2003) · Traffic · doi:10.1046/j.1600-0854.2003.0139.x · Cited by 24

A Single β Adaptin Contributes to AP 1 and AP 2 Complexes and Clathrin Function in D ictyostelium

Sosa, R. T., Weber, M. M., Wen, Y., & O’Halloran, T. J. (2011) · Traffic · doi:10.1111/j.1600-0854.2011.01310.x · Cited by 24

Dynamics of Membrane Clathrin‐Coated Structures During Cytokinesis

Warner, A. K., Keen, J. H., & Wang, Y.-L. (2006) · Traffic : the International Journal of Intracellular Transport · doi:10.1111/j.1600-0854.2005.00377.x · Cited by 29

Hsc70‐induced Changes in Clathrin‐Auxilin Cage Structure Suggest a Role for Clathrin Light Chains in Cage Disassembly

Young, A., Stoilova‐McPhie, S., Rothnie, A. J., Vallis, Y., Harvey‐Smith, P., Ranson, N. A., Kent, H. M., Brodsky, F. M., Pearse, B. M. F., Roseman, A. M., et al. (2013) · Traffic · doi:10.1111/tra.12085 · Cited by 24

A Conformational Change in the α‐subunit of Coatomer Induced by Ligand Binding to γ‐COP Revealed by Single‐pair FRET

Langer, J. D., Roth, C. M., Béthune, J., Stoops, E. H., Brügger, B., Herten, D., & Wieland, F. (2007) · Traffic · doi:10.1111/j.1600-0854.2007.00697.x · Cited by 24

Gene expression effects of lithium and valproic acid in a serotonergic cell line

Balasubramanian, D., Pearson, J. F., & Kennedy, M. A. (2018) · Physiological Genomics · doi:10.1152/physiolgenomics.00069.2018 · Cited by 24

Endocytic pathway for surfactant protein A in human macrophages: binding, clathrin-mediated uptake, and trafficking through the endolysosomal pathway

Crowther, J. E., & Schlesinger, L. S. (2005) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00267.2005 · Cited by 23

Multi‐Site Functionalization of Protein Scaffolds for Bimetallic Nanoparticle Templating

Huggins, K. N. L., Schoen, A. P., Arunagirinathan, M. A., & Heilshorn, S. C. (2014) · Advanced Functional Materials · doi:10.1002/adfm.201402049 · Cited by 22

Golgi tubules: their structure, formation and role in intra-Golgi transport

Martínez‐Alonso, E., Tomás, M., & Martínez‐Menárguez, J. A. (2013) · Histochemistry and Cell Biology · doi:10.1007/s00418-013-1114-9 · Cited by 22

Structures and mechanisms of vesicle coat components and multisubunit tethering complexes

Jackson, L. P., Kümmel, D., Reinisch, K. M., & Owen, D. J. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.05.013 · Cited by 23

Clathrin Heavy Chain Is Important for Viability, Oviposition, Embryogenesis and, Possibly, Systemic RNAi Response in the Predatory Mite Metaseiulus occidentalis

Wu, K., & Hoy, M. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110874 · Cited by 22

Efficient and facile formation of two-component nanoparticles via aromatic moiety directed self-assembly

Wang, W., & Chau, Y. (2011) · Chemical Communications · doi:10.1039/c1cc11048a · Cited by 22

Association of the Hermansky-Pudlak syndrome type-3 protein with clathrin

Helip‐Wooley, A., Westbroek, W., Dorward, H. M., Mommaas, M., Boissy, R. E., Gahl, W. A., & Huizing, M. (2005) · BMC Cell Biology · doi:10.1186/1471-2121-6-33 · Cited by 22

Clathrin is essential for meiotic spindle function in oocytes

Hölzenspies, J., Roelen, B. A. J., Colenbrander, B., Romijn, R. A., Hemrika, W., Stoorvogel, W., & van Haeften, T. (2010) · Reproduction · doi:10.1530/rep-10-0045 · Cited by 22

Leishmania major: clathrin and adaptin complexes of an intra-cellular parasite

Denny, P. W., Morgan, G. W., Field, M. C., & Smith, D. F. (2004) · Experimental Parasitology · doi:10.1016/j.exppara.2004.10.007 · Cited by 22

Involvement of adaptor proteins in clathrin-mediated endocytosis of virus entry

Shi, R., Hou, L., Wei, L., & Liu, J. (2021) · Microbial Pathogenesis · doi:10.1016/j.micpath.2021.105278 · Cited by 23

Clathrin Light Chains: Not to Be Taken so Lightly

Das, J., Tiwari, M., & Subramanyam, D. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.774587 · Cited by 22

Molecular pathology of familial hypercholesterolemia, related dyslipidemias and therapies beyond the statins

Faiz, F., Hooper, A. J., & BOCKXMEER, F. M. V. (2012) · Critical Reviews in Clinical Laboratory Sciences · doi:10.3109/10408363.2011.646942 · Cited by 21

Understanding magnetic nanoparticle osteoblast receptor-mediated endocytosis using experiments and modeling

Tran, N. L., & Webster, T. J. (2013) · Nanotechnology · doi:10.1088/0957-4484/24/18/185102 · Cited by 21

Clathrin expression in Trypanosoma cruzi

Kalb, L. C., Toner, Y. C., Batista, C. M., Eger, I., Fragoso, S. P., & Soares, M. J. (2014) · BMC Cell Biology · doi:10.1186/1471-2121-15-23 · Cited by 21

Crystal structure of human GGA1 GAT domain complexed with the GAT‐binding domain of Rabaptin5

Zhu, G., Zhai, P. C., He, X., Wakeham, N., Rodgers, K. K., Li, G., Tang, J., & Zhang, X. C. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600411 · Cited by 21

The Interaction of the Human GGA1 GAT Domain with Rabaptin-5 Is Mediated by Residues on Its Three-Helix Bundle

Zhai, P. C., He, X., Liu, J., Wakeham, N., Zhu, G., Li, G., Tang, J., & Zhang, X. C. (2003) · Biochemistry · doi:10.1021/bi035392b · Cited by 21

The uptake of extracellular vesicles: Research progress in cancer drug resistance and beyond

Qian, L., Chen, P., Zhang, S., Wang, Z., Guo, Y., Koutouratsas, V., Fleishman, J. S., Huang, C., & Zhang, S. (2025) · Drug Resistance Updates · doi:10.1016/j.drup.2025.101209 · Cited by 21

From Promise to Reality: Bioengineering Strategies to Enhance the Therapeutic Potential of Extracellular Vesicles

Fuzeta, M. D. A., Gonçalves, P. P., Fernandes‐Platzgummer, A., Cabral, J. M. S., Bernardes, N., & da Silva, C. L. (2022) · Bioengineering · doi:10.3390/bioengineering9110675 · Cited by 21

Endocytosis of Environmental and Engineered Micro‐ and Nanosized Particles

Gehr, P., Clift, M. J. D., Brandenberger, C., Lehmann, A. D., Herzog, F., & Rothen‐Rutishauser, B. (2011) · Comprehensive physiology · doi:10.1002/cphy.c100035 · Cited by 20

Recalibration of MARTINI-3 Parameters for Improved Interactions between Peripheral Proteins and Lipid Bilayers

Soni, J., Gupta, S., & Mandal, T. (2024) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c00645 · Cited by 19

Lysosomal protein trafficking in Giardia lamblia: common and distinct features

Maria, C. T. (2011) · Frontiers in Bioscience-Elite · doi:10.2741/511 · Cited by 19

Conformational changes of coat proteins during vesicle formation

Langer, J. D., Stoops, E. H., Béthune, J., & Wieland, F. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.03.020 · Cited by 19

Exosomal miRNA: an alternative mediator of cell-to-cell communication

Li, J., Jiang, X., & Wang, K. (2019) · ExRNA · doi:10.1186/s41544-019-0025-x · Cited by 20

Controllable formation of aromatic nanoparticles in a three-dimensional hydrodynamic flow focusing microfluidic device

Jiang, L., Wang, W., Chau, Y., & Yao, S. (2013) · RSC Advances · doi:10.1039/c3ra42071j · Cited by 19

Regulation of Dynamin by Nucleoside Diphosphate Kinase

Narayanan, R., & Ramaswami, M. (2003) · Journal of Bioenergetics and Biomembranes · doi:10.1023/a:1023441806530 · Cited by 19

The C-terminal sequence of the large hepatitis delta antigen is variable but retains the ability to bind clathrin

Wang, Y., Huang, C., Chao, M., & Lo, S. J. (2009) · Virology Journal · doi:10.1186/1743-422x-6-31 · Cited by 19

The Sla1 adaptor‐clathrin interaction regulates coat formation and progression of endocytosis

Tolsma, T. O., Cuevas, L. M., & Pietro, S. M. D. (2018) · Traffic · doi:10.1111/tra.12563 · Cited by 16

Human Immunodeficiency Virus Type 1 and Related Primate Lentiviruses Engage Clathrin through Gag-Pol or Gag

Popov, S., Strack, B., Sánchez-Merino, V., Popova, E. N., Rosin, H., & Göttlinger, H. G. (2011) · Journal of Virology · doi:10.1128/jvi.02329-10 · Cited by 18

Connexin 31.1 degradation requires the Clathrin‐mediated autophagy in NSCLC cell H1299

Zhu, X., Ruan, Z., Yang, X., Chu, K., Wu, H., Li, Y., & Huang, Y. (2014) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12470 · Cited by 17

Independent Transport and Sorting of Functionally Distinct Protein Families in Tetrahymena thermophila Dense Core Secretory Granules

Rahaman, A., Miao, W., & Turkewitz, A. P. (2009) · Eukaryotic Cell · doi:10.1128/ec.00151-09 · Cited by 18

The Prenylated Rab GTPase Receptor PRA1.F4 Contributes to Protein Exit from the Golgi Apparatus

Lee, M. H., Yoo, Y.-J., Kim, D. H., Hanh, N., Kwon, Y., & Hwang, I. (2017) · PLANT PHYSIOLOGY · doi:10.1104/pp.17.00466 · Cited by 18

Characterization of the localization and function of NECAP 1 in neurons

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