ReviewTraffic (Copenhagen, Denmark)2012
Getting in touch with the clathrin terminal domain.
Review in Traffic (Copenhagen, Denmark), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
38 citing papers in PubMed.
- Article
- Targeting clathrin-mediated endocytosis: recent advances in inhibitor development, mechanistic insights, and therapeutic prospects.RSC medicinal chemistry · 2025Review
- Inhibition of the Clathrin Terminal Domain-Amphiphysin Protein-Protein Interaction. Probing the Pitstop 2 Aromatic Moiety.ChemMedChem · 2025Article
- Cell binding, uptake, and infection of influenza A virus using recombinant antibody-based receptors.Journal of virology · 2025Article
- A conserved interaction between the effector Sca4 and host clathrin suggests additional contributions for Sca4 during rickettsial infection.Infection and immunity · 2024Article
- CHC22 clathrin recruitment to the early secretory pathway requires two-site interaction with SNX5 and p115.The EMBO journal · 2024Article
- The Chemical Inhibitors of Endocytosis: From Mechanisms to Potential Clinical Applications.Cells · 2023Review
- An interaction between β'-COP and the ArfGAP, Glo3, maintains post-Golgi cargo recycling.The Journal of cell biology · 2023Article
- Small molecules targeting endocytic uptake and recycling pathways.Frontiers in cell and developmental biology · 2023Review
- Integrating protein copy numbers with interaction networks to quantify stoichiometry in clathrin-mediated endocytosis.Scientific reports · 2022Article
- Cargo sorting zones in the trans-Golgi network visualized by super-resolution confocal live imaging microscopy in plants.Nature communications · 2021Article
- Role of Clathrin and Dynamin in Clathrin Mediated Endocytosis/Synaptic Vesicle Recycling and Implications in Neurological Diseases.Frontiers in cellular neuroscience · 2021Review
- Cargo-mediated recruitment of the endocytic adaptor protein Sla1 inJournal of cell science · 2020Article
- Wbox2: A clathrin terminal domain-derived peptide inhibitor of clathrin-mediated endocytosis.The Journal of cell biology · 2020Article
- Evolving models for assembling and shaping clathrin-coated pits.The Journal of cell biology · 2020Review
- Clathrin's adaptor interaction sites are repurposed to stabilize microtubules during mitosis.The Journal of cell biology · 2020Article
- The Sla1 adaptor-clathrin interaction regulates coat formation and progression of endocytosis.Traffic (Copenhagen, Denmark) · 2018Article
- Article
- Inhibition of endocytosis suppresses the nitric oxide-dependent release of Cl- in retinal amacrine cells.PloS one · 2018Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
The N-terminal domain (TD) of the clathrin heavy chain is folded into a seven-bladed β-propeller that projects inward from the polyhedral outer clathrin coat. As the most membrane-proximal portion of assembled clathrin, the TD is a major protein-protein interaction node. Contact with the TD β-propeller occurs through short peptide sequences typically located within intrinsically disordered segments of coat components that usually are elements of the membrane-apposed, inner 'adaptor' coat layer. A huge variation in TD-binding motifs is known and now four spatially discrete interaction surfaces upon the β-propeller have been delineated. An important operational feature of the TD interaction sites in vivo is functional redundancy. The recent discovery that 'pitstop' chemical inhibitors apparently occupy only one of the four TD interaction surfaces, but potently block clathrin-mediated endocytosis, warrants careful consideration of the underlying molecular basis for this inhibition.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.