Folding and trimerization of clathrin subunits at the triskelion hub
Cell, ISSN: 0092-8674, Vol: 68, Issue: 5, Page: 899-910
1992
- 140Citations
- 43Captures
- 1Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations140
- Citation Indexes140
- 140
- CrossRef107
- Captures43
- Readers43
- 43
- Mentions1
- References1
- Wikipedia1
Article Description
The triskelion shape of the clathrin molecule enables it to form the polyhedral protein network that covers clathrin-coated pits and vesicles. Domains within the clathrin heavy chain that are responsible for maintaining triskelion shape and function were identified and localized. Sequences that mediate trimerization are distal to the carboxyl terminus and are adjacent to a domain that mediates both light chain binding and clathrin assembly. Structural modeling predicts that within this domain, the region of heavy chain-light chain interaction is a bundle of three or four α helices. These studies establish a low resolution model of clathrin subunit folding in the central portion (hub) of the triskelion, thus providing a basis for future mutagenesis experiments.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0092867492900339; http://dx.doi.org/10.1016/0092-8674(92)90033-9; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0026503136&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/1547490; https://linkinghub.elsevier.com/retrieve/pii/0092867492900339; http://dx.doi.org/10.1016/0092-8674%2892%2990033-9; https://dx.doi.org/10.1016/0092-8674%2892%2990033-9
Elsevier BV
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