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

Negative effects of desiccation on the protein sorting and post-translational modification

Wang, X., & He, Y. (2009) · Plant Signaling & Behavior · doi:10.4161/psb.4.5.8299 · Cited by 1

Clathrin heavy chain is a useful immunohistochemical marker for esophageal squamous intraepithelial neoplasia

Tokita, K., Seimiya, M., Matsushita, K., Tomonaga, T., Onodera, K., Syoji, O. H. K. I., Tanizawa, T., Uesato, M., Shimada, H., Matsubara, H., et al. (2013) · Esophagus · doi:10.1007/s10388-013-0381-9 · Cited by 1

Molecular Mechanisms of Protein Sorting in Polarized Epithelial Cells

Ortega, B., & Welling, P. A. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-382026-6.00057-9 · Cited by 1

Emergence and Characterization of the p23 Molecular Chaperone

Echtenkamp, F., & Freeman, B. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1130-1_9 · Cited by 1

Extracellular vesicles in acute respiratory distress syndrome: Understanding protective and harmful signaling for the development of new therapeutics.

Bavuso, M., Miller, N., Sill, J. M., Dobrian, A. D., & Biancatelli, R. M. L. C. (2024) · PubMed · doi:10.14670/hh-18-659 · Cited by 2

Endocytic Machinery at the Neuronal Synapse

Milošević, I. (2014) · Springer eBooks · doi:10.1007/978-4-431-55166-9_10 · Cited by 1

Molecular Mechanisms of Polarized Protein Trafficking in Epithelial Cells

Ortega, B., & Welling, P. A. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809954-4.00045-1 · Cited by 1

Contrôle endosomal de la signalisation intracellulaire

Zanin, N., & Blouin, C. M. (2018) · Biologie Aujourd hui · doi:10.1051/jbio/2018023 · Cited by 1

Advanced Dynamic Gels

Shrestha, R. G., & Naito, M. (2015) · Wiley eBooks · doi:10.1002/9783527682157.ch13 · Cited by 1

Coupling Drs2p to Phospholipid Translocation, Membrane Asymmetry, and Vesicle Budding

Zhou, X., Natarajan, P., Muthusamy, B.-P., Graham, T. R., & Liu, K. (2011) · Wiley eBooks · doi:10.1002/9781118120118.ch9 · Cited by 1

Dendritic Organelles for Postsynaptic Trafficking

Hanus, C., & Ehlers, M. (2008) · Springer eBooks · doi:10.1007/978-0-387-77232-5_8 · Cited by 1

Drosophila melanogaster gene Merlin interacts with the clathrin adaptor protein gene lap

Копыл, С. А., Dorogova, N. V., Akhmametyeva, E. M., Omelyanchuk, L. V., & Chang, L. (2010) · Russian Journal of Genetics · doi:10.1134/s1022795410030038 · Cited by 1

Synaptic Vesicle Endocytosis

Smitz, L., & Verstreken, P. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-481-0_11 · Cited by 1

Anterograde Trafficking of Toll-Like Receptors Requires the Cargo Sorting Adaptors TMED-2 and 7 and specific N-glycansPreprint

Holm, J. E., Soares, S., Symmons, M., Moncrieffe, M., & Gay, N. (2022) · bioRxiv · doi:10.1101/2022.10.10.511598 · Cited by 1

High‐Resolution Structures of Membrane Proteins: From X‐Ray Crystallography to an Integrated Approach of Membranes

Pebay‐Peyroula, E. (2007) · doi:10.1002/9783527621224.ch1

Intracellular Trafficking of Nanoparticles: Implications for Therapeutic Efficacy of the Encapsulated Drug

Niu, L., & Panyam, J. (2013) · Wiley eBooks · doi:10.1002/9780470571224.pse498

Clathrin light chain b is capable of affecting potently a major protein phosphatase from microtubules (MT‐PP1)

Hiraga, A., MORRICE, N. A., Honda, E., Tamura, S., & Munakata, H. (2006) · FEBS Letters · doi:10.1016/j.febslet.2005.12.105

Bridging Integrator 1 (BIN1)

Turton, J. C., & Morgan, K. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7309-1_6

Understanding Cage Diassembly

Smith, C. J., Young, A., Stoilova‐McPhie, S., Harvey‐Smith, P., Vallis, Y., Kent, H. M., & Pearse, B. M. F. (2007) · Imaging & Microscopy · doi:10.1002/imic.200790153

Membrane Biogenesis

Yèagle, P. L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-800047-2.00011-5

Stimuli-Responsive Self-Healing Viscoelastic Gels

Shrestha, R. G., & Aramaki, K. (2016) · Springer eBooks · doi:10.1007/978-981-10-2463-4_5

Roll out the barrel

Smallridge, R. S. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1544

Simulating Protein-Mediated Membrane Remodeling at Multiple Scales

Simunovic, M., & Voth, G. A. (2018) · Springer eBooks · doi:10.1007/978-3-030-00630-3_14

Molecular Technology for Membrane Functionalization

MURAKOSHI, M., & Muraoka, T. (2019) · doi:10.1002/9783527823987.vol2_c9

Quantitative Proteomics Reveals Global Reduction of Endocytic Machinery Components in GliomasPreprint

Buser, D. P., Ritz, M., Moes, S., Tostado, C., Frank, S., Spiess, M., Mariani, L., Jenö, P., Boulay, J., & Hütter, G. (2019) · SSRN Electronic Journal · doi:10.2139/ssrn.3352502

Sorting of Storage Proteins in the Plant G olgi Apparatus

Hinz, G., & Herman, E. M. (2017) · Annual Plant Reviews online · doi:10.1002/9781119312994.apr0085

Biologically Templated Nanostructure Assemblies

Behrens, S. S. (2015) · Encyclopedia of Inorganic and Bioinorganic Chemistry · doi:10.1002/9781119951438.eibc0316.pub2

Basic Concepts in Drug Targeting

(2016) · CRC Press eBooks · doi:10.1201/9781315370118-2

Clathrin

(2004) · Wiley eBooks · doi:10.1002/0471684228.egp02362

Bioinspired Nanodesigns for Molecular Encapsulation

(2021) · Royal Society of Chemistry eBooks · doi:10.1039/9781788010009-00069

Nanoparticles Targeting and Uptake: Current Advances in Breast Cancer Research

Lugun, O., & Pandey, A. K. (2022) · BENTHAM SCIENCE PUBLISHERS eBooks · doi:10.2174/9781681089522112010011

Excitation-Secretion Coupling of Dense-Core Vesicle Release

Cirkovic, V. (2023) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-10009

Protein Cage-like Vesicles Fabricated via Polymerization-Induced Microphase Separation of Amphiphilic Diblock Copolymers

Yoshida, E. (2025) · Materials · doi:10.3390/ma18030727

Topological architectures enriched by cooperative acetylene coordination

Domoto, Y. (2025) · Journal of Inclusion Phenomena and Macrocyclic Chemistry · doi:10.1007/s10847-025-01297-x

Three-dimensional digital elevation models reconstructed from stereoscopic image of platinum replica in sheared open osteoclasts

Akisaka, T. (2025) · Micron · doi:10.1016/j.micron.2025.103834

Evaluation of Hypovirus Infection on the Vesicular Protein Expression Pattern of Cryphonectria parasitica by TMT-Based Proteomics Analysis

Zeng, Z., Lin, N., Lu, T., Xu, J. Z., Zhang, Z., Wang, F., & Wang, J. (2025) · Biology · doi:10.3390/biology14091123

Innovative Methods to Label, Track, and Quantitate Extracellular Vesicle Uptake

Achuthkumar, A., Wermuth, P. J., & Mahoney, M. G. (2026) · Neuromethods · doi:10.1007/978-1-0716-4905-3_12

Regenerating Earthworm-Derived Extracellular Vesicles Enhance Mouse Fibroblast Growth and Migration

Subramaniam, R. K., Christyraj, J. R. S. S., Mathews, M. G. R., Venkatachalam, S., & Yesudhason, B. V. (2026) · Regenerative Engineering and Translational Medicine · doi:10.1007/s40883-026-00563-9

Rôle de la clathrine dans la formation des lamellipodes

Gautier, J. J. (2011) · theses.fr (ABES) · doi:10.70675/1260cc02z60a9z4b51zaa64zf3641ef4752f

Régulation de l'invasion cellulaire induite par les tyrosine kinases dans le cancer du sein

Chevalier, C. (2014) · theses.fr (ABES) · doi:10.70675/692c8de1za82az4e5ez953bz5e90670eb75d

Study of CAR membrane dynamics in adenovirus infection and CAR endogenous role in healthy and diseased brain

Loustalot, F. (2015) · theses.fr (ABES) · doi:10.70675/549d8b77z73a1z461fza271zec31f12874d2

Nanoparticules polymères ciblant le récepteur CXCR3 : élaboration et évaluation sur modèles de tumeur

Rodrigues, L. (2018) · doi:10.70675/2a475cc6z0bb2z4611zbb30z2a309b5f4523

Search for the target of Retro-2 : a retrograde transport inhibitor and its improvement for therapeutic application

Tepshi, L. (2017) · doi:10.70675/3b2043c6z551fz474bz9373z6e91aa69127a

Caractérisation des vésicules extracellulaires (VEs) d’origine microgliale et mise en évidence de leur effet neurotrophique

Arab, T. (2019) · theses.fr (ABES) · doi:10.70675/fb069a34z1a95z42cfza301z995c5011bbf9

Evaluation of the safety and drug delivery efficacy of carbon dots in in vitro and in vivo models

Fan, J. (2018) · doi:10.70675/1c7fc388ze650z4420z9c0dz7de38470b8e4

Role of extracellular vesicles in type 1 diabetes

Giri, K. R. (2020) · theses.fr (ABES) · doi:10.70675/0b17ca8bz26a4z454bz9cd6zfce0f6d3ddaf

Role of vSNAREs in post-synaptic AMPAR trafficking, glutamatergic transmisson and plasticity

Bakr, M. (2020) · theses.fr (ABES) · doi:10.70675/32528bd6ze209z428fzbe94z1a44fc665a82 · Cited by 1

Secretion of neurotoxic vesicles by muscle cells of ALS patients

Gall, L. L. (2019) · theses.fr (ABES) · doi:10.70675/61e48a01z5133z45e6z8569z1b35b4b8fb4f

Transport intracellulaire des récepteurs AMPA et régulation par leurs protéines associées

Bonnet, C. (2021) · theses.fr (ABES) · doi:10.70675/a51a45f6zee8cz4c6az85a5z8b01dfd87159

DNA origami for spatio-temporal mass spectrometry

Ghosh, D. (2024) · theses.fr (ABES) · doi:10.70675/2eafb946zc4bez445fz8463z503957f8667d

Mechanically engineered extracellular vesicles technology: Regulatory mechanisms and therapeutic applications in orthopedic diseases

Song, C., Xu, Y., Zhang, D., Kang, F., Liao, J., Ding, H., Hu, W., Dong, S., & Li, J. (2026) · Biomedical Technology · doi:10.1016/j.bmt.2026.100163

Single-Point versus Multi-Point Mechanical Loading in Membrane Deformation: Insights from Molecular Dynamics Simulations

Wu, W., Lu, X., Dong, X., Yuan, B., & Yang, K. (2026) · Langmuir · doi:10.1021/acs.langmuir.6c00911

Fluid shear stress has a biphasic effect on clathrin-mediated endocytosis in vascular endothelial cellsPreprint

Yuan, J., Nawara, T. J., Seeley, L. D., Tran, Y. T. B., & Mattheyses, A. L. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.23.734037

Ubiquitin proteasome system and its role in cancer

Mahalik, S., Yadav, S. S., & Devi, S. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-41553-1.00006-2

Protein-lipid interactions

Pandia, S., Mahapatra, P., & Chakraborty, H. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-30042-4.00020-1

From Uptake to Therapeutic Function in Engineered Exosome Delivery Systems

Li, Y., Jin, L., Gao, P., Li, M., Zhao, Z., Jiang, J., An, M., & Li, F. (2026) · Research · doi:10.34133/research.1389

Intraepithelial Lesions of the Cervix

Porcayo, M. A. T., Dimas, J., & Martínez, A. L. (2026) · Springer eBooks · doi:10.1007/978-3-032-13454-7_1

Clathrin: anatomy of a coat protein

Smith, C. J., & Pearse, B. M. F. (1999) · Trends in Cell Biology · doi:10.1016/s0962-8924(99)01631-1 · Cited by 53

Structural insights into the clathrin coat

Young, A. (2007) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2007.07.006 · Cited by 61

Coated pits and coated vesicles — sorting it all out

Kirchhausen, T. L. (1993) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(05)80150-2 · Cited by 112

Assembly Proteins and Adaptors in Clathrin Coated Vesicles

Ungewickell, E. J., Lindner, R. M., & Schröder, S. (1992) · Springer eBooks · doi:10.1007/978-3-642-84295-5_5 · Cited by 1

Molecular Structure, Function, and Dynamics of Clathrin-Mediated Membrane TrafficPreprint

Kirchhausen, T. L., Owen, D., & Harrison, S. C. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016725 · Cited by 501