ArticlePloS one2022
Redefining the architecture of ferlin proteins: Insights into multi-domain protein structure and function.
Article in PloS one, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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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
16 citing papers in PubMed, 20 citations in OpenAlex.
- Myoferlin at the crossroad of vesicle trafficking and mitochondrial function: implications for pancreatic cancer progression and stromal reprogramming.Biochemical Society transactions · 2026Review
- Laboratory and genetic characteristic associated with gallbladder-related outcomes in sickle cell disease in Brazil: results from the REDS-III multicenter cohort study.Annals of hematology · 2026Article
- Dysferlin and the Regulation of CaCells · 2025Review
- Structural insights into lipid membrane binding by human ferlins.The EMBO journal · 2025Article
- UtilizingJournal of developmental biology · 2025Review
- Review
- Whole Exome Sequencing Identified a Stop-Gained Mutation in DYSF Gene Associated With Dysferlinopathy in an Iranian Family.International journal of genomics · 2025Article
- Nanodysferlins support membrane repair and binding to TRIM72/MG53 but do not localize to t-tubules or stabilize CaMolecular therapy. Methods & clinical development · 2024Article
- The Dysferlinopathies Conundrum: Clinical Spectra, Disease Mechanism and Genetic Approaches for Treatments.Biomolecules · 2024Review
- A conserved electrostatic membrane-binding surface in synaptotagmin-like proteins revealed using molecular phylogenetic analysis and homology modeling.Protein science : a publication of the Protein Society · 2024Article
- A Conserved Electrostatic Membrane-Binding Surface in Synaptotagmin-Like Proteins Revealed Using Molecular Phylogenetic Analysis and Homology Modeling.bioRxiv : the preprint server for biology · 2023Article
- The natural history, clinical outcomes, and genotype-phenotype relationship of otoferlin-related hearing loss: a systematic, quantitative literature review.Human genetics · 2023Review
- TECPR1 conjugates LC3 to damaged endomembranes upon detection of sphingomyelin exposure.The EMBO journal · 2023Article
- The Dysferlin C2A Domain Binds PI(4,5)P2 and Penetrates Membranes.Journal of molecular biology · 2023Article
- Role of calcium-sensor proteins in cell membrane repair.Bioscience reports · 2023Review
- Testis-enriched ferlin, FER1L5, is required for CaScience advances · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ferlins are complex, multi-domain proteins, involved in membrane trafficking, membrane repair, and exocytosis. The large size of ferlin proteins and the lack of consensus regarding domain boundaries have slowed progress in understanding molecular-level details of ferlin protein structure and function. However, in silico protein folding techniques have significantly enhanced our understanding of the complex ferlin family domain structure. We used RoseTTAFold to assemble full-length models for the six human ferlin proteins (dysferlin, myoferlin, otoferlin, Fer1L4, Fer1L5, and Fer1L6). Our full-length ferlin models were used to obtain objective domain boundaries, and these boundaries were supported by AlphaFold2 predictions. Despite the differences in amino acid sequence between the ferlin proteins, the domain ranges and distinct subdomains in the ferlin domains are remarkably consistent. Further, the RoseTTAFold/AlphaFold2 in silico boundary predictions allowed us to describe and characterize a previously unknown C2 domain, ubiquitous in all human ferlins, which we refer to as C2-FerA. At present, the ferlin domain-domain interactions implied by the full-length in silico models are predicted to have a low accuracy; however, the use of RoseTTAFold and AlphaFold2 as a domain finder has proven to be a powerful research tool for understanding ferlin structure.
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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.