ArticleThe Journal of biological chemistry2009
Localization and structure of the ankyrin-binding site on beta2-spectrin.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
39 citing papers in PubMed, 59 citations in OpenAlex.
- Exome sequencing of families from Ghana reveals known and candidate hearing impairment genes.Communications biology · 2022Article
- Giant ankyrin-B mediates transduction of axon guidance and collateral branch pruning factor sema 3A.eLife · 2021Article
- Pathogenic SPTBN1 variants cause an autosomal dominant neurodevelopmental syndrome.Nature genetics · 2021Article
- Heterozygous variants in SPTBN1 cause intellectual disability and autism.American journal of medical genetics. Part A · 2021Article
- βII spectrin (SPTBN1): biological function and clinical potential in cancer and other diseases.International journal of biological sciences · 2021Review
- Mechanical Unfolding of Spectrin Repeats Induces Water-Molecule Ordering.Biophysical journal · 2020Article
- Opposite Modulation of RAC1 by Mutations in TRIO Is Associated with Distinct, Domain-Specific Neurodevelopmental Disorders.American journal of human genetics · 2020Article
- The Spectrinome: The Interactome of a Scaffold Protein Creating Nuclear and Cytoplasmic Connectivity and Function.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- Localized Myosin II Activity Regulates Assembly and Plasticity of the Axon Initial Segment.Neuron · 2018Article
- The genetic dissection ofMolecular vision · 2018Article
- The role of βII spectrin in cardiac health and disease.Life sciences · 2018Review
- Axonal Membranes and Their Domains: Assembly and Function of the Axon Initial Segment and Node of Ranvier.Frontiers in cellular neuroscience · 2017Review
- Article
- Identification of adducin-binding residues on the cytoplasmic domain of erythrocyte membrane protein, band 3.The Biochemical journal · 2016Article
- The Structure of the Plakin Domain of Plectin Reveals an Extended Rod-like Shape.The Journal of biological chemistry · 2016Article
- Axon Initial Segment Cytoskeleton: Architecture, Development, and Role in Neuron Polarity.Neural plasticity · 2016Review
- Dynamic spectrin/ankyrin-G microdomains promote lateral membrane assembly by opposing endocytosis.Science advances · 2015Article
- The Physiological Molecular Shape of Spectrin: A Compact Supercoil Resembling a Chinese Finger Trap.PLoS computational biology · 2015Article
- Ankyrin-G palmitoylation and βII-spectrin binding to phosphoinositide lipids drive lateral membrane assembly.The Journal of cell biology · 2014Article
- Spectrin and phospholipids - the current picture of their fascinating interplay.Cellular & molecular biology letters · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Spectrins are tetrameric actin-cross-linking proteins that form an elastic network, termed the membrane skeleton, on the cytoplasmic surface of cellular membranes. At the plasma membrane, the membrane skeleton provides essential support, preventing loss of membrane material to environmental shear stresses. The skeleton also controls the location, abundance, and activity of membrane proteins that are critical to cell and tissue function. The ability of the skeleton to modulate membrane stability and function requires adaptor proteins that bind the skeleton to membranes. The principal adaptors are the ankyrin proteins, which bind to the beta-subunit of spectrin and to the cytoplasmic domains of numerous integral membrane proteins. Here, we present the crystal structure of the ankyrin-binding domain of human beta2-spectrin at 1.95 A resolution together with mutagenesis data identifying the binding surface for ankyrins on beta2-spectrin.
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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.