ArticleBlood2010
Structural basis for spectrin recognition by ankyrin.
Article in Blood, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 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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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.
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Who cites it
51 citing papers in PubMed, 88 citations in OpenAlex.
- A novelFrontiers in pediatrics · 2026Article
- Redox Homeostasis in Red Blood Cells: From Molecular Mechanisms to Antioxidant Strategies.Current issues in molecular biology · 2025Review
- Case Report: Identification and functional characterization of a novel heterozygous splice-donor (c.647+1G>A) site mutation in theFrontiers in genetics · 2025Article
- A sophisticated virulence repertoire and colistin resistance of Citrobacter freundii ST150 from a patient with sepsis admitted to ICU in a tertiary care hospital in Uganda, East Africa: Insight from genomic and molecular docking analyses.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2024Article
- Article
- Spherocytosis-Related L1340P Mutation in Ankyrin Affects Its Interactions with Spectrin.Life (Basel, Switzerland) · 2023Article
- The protein organization of a red blood cell.Cell reports · 2022Article
- Structure, dynamics and assembly of the ankyrin complex on human red blood cell membrane.Nature structural & molecular biology · 2022Article
- Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins.Structure (London, England : 1993) · 2021Article
- Identification of a De Novoc.1000delA ANK1 mutation associated to hereditary spherocytosis in a neonate with Coombs-negative hemolytic jaundice-case reports and review of the literature.BMC medical genomics · 2021Review
- Cargo hold and delivery: Ankyrins, spectrins, and their functional patterning of neurons.Cytoskeleton (Hoboken, N.J.) · 2020Review
- α-Fodrin is required for the organization of functional microtubules during mitosis.Cell cycle (Georgetown, Tex.) · 2019Article
- Neurodevelopmental mutation of giant ankyrin-G disrupts a core mechanism for axon initial segment assembly.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Mechanical unfolding of spectrin reveals a super-exponential dependence of unfolding rate on force.Scientific reports · 2019Article
- The Plasmodium falciparum MESA erythrocyte cytoskeleton-binding (MEC) motif binds to erythrocyte ankyrin.Molecular and biochemical parasitology · 2019Article
- Molecular architecture of the Jumonji C family histone demethylase KDM5B.Scientific reports · 2019Article
- A Novel Homozygous Mutation in SPTBN2 Leads to Spinocerebellar Ataxia in a Consanguineous Family: Report of a New Infantile-Onset Case and Brief Review of the Literature.Cerebellum (London, England) · 2018Review
- Novel hereditary spherocytosis-associated splice site mutation in theHaematologica · 2018Article
- Article
- The role of βII spectrin in cardiac health and disease.Life sciences · 2018Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Maintenance of membrane integrity and organization in the metazoan cell is accomplished through intracellular tethering of membrane proteins to an extensive, flexible protein network. Spectrin, the principal component of this network, is anchored to membrane proteins through the adaptor protein ankyrin. To elucidate the atomic basis for this interaction, we determined a crystal structure of human betaI-spectrin repeats 13 to 15 in complex with the ZU5-ANK domain of human ankyrin R. The structure reveals the role of repeats 14 to 15 in binding, the electrostatic and hydrophobic contributions along the interface, and the necessity for a particular orientation of the spectrin repeats. Using structural and biochemical data as a guide, we characterized the individual proteins and their interactions by binding and thermal stability analyses. In addition to validating the structural model, these data provide insight into the nature of some mutations associated with cell morphology defects, including those found in human diseases such as hereditary spherocytosis and elliptocytosis. Finally, analysis of the ZU5 domain suggests it is a versatile protein-protein interaction module with distinct interaction surfaces. The structure represents not only the first of a spectrin fragment in complex with its binding partner, but also that of an intermolecular complex involving a ZU5 domain.
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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.