ArticleProceedings of the National Academy of Sciences of the United States of America1994
Interchain binding at the tail end of the Drosophila spectrin molecule.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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Who cites it
7 citing papers in PubMed, 40 citations in OpenAlex.
- [Clinical and gene mutation characteristics of patients with hereditary ellipsocytosis: nine cases report and literature review].Zhonghua xue ye xue za zhi = Zhonghua xueyexue zazhi · 2023Review
- Intertwined αβ spectrin meeting helical actin protofilament in the erythrocyte membrane skeleton: wrap-around vs. point-attachment.Annals of biomedical engineering · 2011Article
- Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex.Blood · 2010Article
- Characterization and expression of a heart-selective alternatively spliced variant of alpha II-spectrin, cardi+, during development in the rat.Journal of molecular and cellular cardiology · 2010Article
- Article
- A hybrid model for erythrocyte membrane: a single unit of protein network coupled with lipid bilayer.Biophysical journal · 2007Article
- Molecular mechanism of the calcium-induced conformational change in the spectrin EF-hands.The EMBO journal · 1995Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Spectrin's function as an actin-crosslinking protein and membrane skeleton component involves the tail end of the molecule, where multiple interactions between two spectrin chains and between these chains and other proteins give rise to complexes that form membrane skeleton network junctions. To determine whether the sequences that contribute to interchain binding can be distinguished from sequences that are involved in other spectrin tail end functions, we mapped the regions in each Drosophila spectrin chain that are required for interchain binding in vitro. Segments 20 and 21 of the alpha chain and 2 and 3 of the beta chain are required for binding. Binding appears to be very dependent on the lateral register of segments in the two apposed chains. Domains of the nonrepetitive segments, 22 of alpha chain and 1 of beta chain, are also involved in associating the two chains. Required sequences within these nonrepetitive segments are interspersed within domains that are known to be involved in associations with other structural proteins, such as actin, and regulatory components, such as protein 4.1 and calcium.
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