ArticleBlood2010
Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex.
Article in Blood, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 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.
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.
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Who cites it
44 citing papers in PubMed, 77 citations in OpenAlex.
- Red cell shape regulation by band 3-ankyrin-spectrin linkage: implications for clinical severity of bovine hereditary spherocytosis.Blood red cells & iron · 2025Article
- Identification of βIIΣ1-Spectrin as a Binding Partner of the GH-regulated Human Obesity Scaffold Protein SH2B1.Endocrinology · 2025Article
- Hereditary Spherocytosis: Can Next-Generation Sequencing of the Five Most Frequently Affected Genes Replace Time-Consuming Functional Investigations?International journal of molecular sciences · 2023Article
- Spectrins: molecular organizers and targets of neurological disorders.Nature reviews. Neuroscience · 2023Review
- A cryo-ET survey of microtubules and intracellular compartments in mammalian axons.The Journal of cell biology · 2022Article
- Clinical and molecular genetic analysis of a Chinese family with hereditary elliptocytosis caused by a novel mutation in the EPB41 gene.Journal of clinical laboratory analysis · 2021Article
- A Fresh Look at the Structure, Regulation, and Functions of Fodrin.Molecular and cellular biology · 2020Review
- Cotranslational folding cooperativity of contiguous domains of α-spectrin.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cargo hold and delivery: Ankyrins, spectrins, and their functional patterning of neurons.Cytoskeleton (Hoboken, N.J.) · 2020Review
- The Spectrinome: The Interactome of a Scaffold Protein Creating Nuclear and Cytoplasmic Connectivity and Function.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- Aberrant splicing contributes to severe α-spectrin-linked congenital hemolytic anemia.The Journal of clinical investigation · 2019Article
- Mechanical unfolding reveals stable 3-helix intermediates in talin and α-catenin.PLoS computational biology · 2018Article
- The role of βII spectrin in cardiac health and disease.Life sciences · 2018Review
- Affinity of IDPs to their targets is modulated by ion-specific changes in kinetics and residual structure.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Axonal Membranes and Their Domains: Assembly and Function of the Axon Initial Segment and Node of Ranvier.Frontiers in cellular neuroscience · 2017Review
- Genotype-phenotype correlations in hereditary elliptocytosis and hereditary pyropoikilocytosis.Blood cells, molecules & diseases · 2016Article
- The Structure of the Plakin Domain of Plectin Reveals an Extended Rod-like Shape.The Journal of biological chemistry · 2016Article
- A novel strain energy relationship for red blood cell membrane skeleton based on spectrin stiffness and its application to micropipette deformation.Biomechanics and modeling in mechanobiology · 2016Article
- Axon Initial Segment Cytoskeleton: Architecture, Development, and Role in Neuron Polarity.Neural plasticity · 2016Review
- Structural Basis of Neuronal Nitric-oxide Synthase Interaction with Dystrophin Repeats 16 and 17.The Journal of biological chemistry · 2015Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
As the principal component of the membrane skeleton, spectrin confers integrity and flexibility to red cell membranes. Although this network involves many interactions, the most common hemolytic anemia mutations that disrupt erythrocyte morphology affect the spectrin tetramerization domains. Although much is known clinically about the resulting conditions (hereditary elliptocytosis and pyropoikilocytosis), the detailed structural basis for spectrin tetramerization and its disruption by hereditary anemia mutations remains elusive. Thus, to provide further insights into spectrin assembly and tetramer site mutations, a crystal structure of the spectrin tetramerization domain complex has been determined. Architecturally, this complex shows striking resemblance to multirepeat spectrin fragments, with the interacting tetramer site region forming a central, composite repeat. This structure identifies conformational changes in alpha-spectrin that occur upon binding to beta-spectrin, and it reports the first structure of the beta-spectrin tetramerization domain. Analysis of the interaction surfaces indicates an extensive interface dominated by hydrophobic contacts and supplemented by electrostatic complementarity. Analysis of evolutionarily conserved residues suggests additional surfaces that may form important interactions. Finally, mapping of hereditary anemia-related mutations onto the structure demonstrate that most, but not all, local hereditary anemia mutations map to the interacting domains. The potential molecular effects of these mutations are described.
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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.