ArticleJCI insight2016
A flexible, multilayered protein scaffold maintains the slit in between glomerular podocytes.
Article in JCI insight, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 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
56 citing papers in PubMed, 100 citations in OpenAlex.
- Anti-nephrin antibodies in pediatric nephrotic syndrome: a new paradigm.Pediatric nephrology (Berlin, Germany) · 2026Review
- Towards an integrative structural model of the fishnet slit diaphragm: Understanding its physiology through proteomics and structural insight.Pflugers Archiv : European journal of physiology · 2026Review
- Podocin oligomers regulate the ordering of nephrin chains, providing the molecular basis ofProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Long-chain polyphosphates induce glomerular microthrombi and exacerbate LPS-induced acute kidney injury in mouse.Disease models & mechanisms · 2026Article
- Mouse Alport podocytes are susceptible to AAV9 transduction in vivo.Kidney international · 2026Article
- RNA Alternative Splicing and Polyadenylation and Regulation of the Glomerular Filtration Barrier.Journal of the American Society of Nephrology : JASN · 2025Article
- The slit diaphragm in Drosophila exhibits a bilayered, fishnet architecture.Nature communications · 2025Article
- The Life of a Kidney Podocyte.Acta physiologica (Oxford, England) · 2025Review
- Reduced nephrin tyrosine phosphorylation impairs podocyte force transmission and accelerates detachment in disease.iScience · 2025Article
- Revisiting nephrin signaling and its specialized effects on the uniquely adaptable podocyte.The Biochemical journal · 2025Review
- Phenotypic quantification of Nphs1-deficient mice.Journal of nephrology · 2025Article
- Roles of myosin 1e and the actin cytoskeleton in kidney functions and familial kidney disease.Cytoskeleton (Hoboken, N.J.) · 2024Review
- Nephrotic syndrome in a child with neurofibromatosis type 1: A case report and literature review.Nephrology (Carlton, Vic.) · 2024Review
- Neph1 is required for neurite branching and is negatively regulated by the PRRXL1 homeodomain factor in the developing spinal cord dorsal horn.Neural development · 2024Article
- Biophysical characterization and insights into the oligomeric nature of CD2-associated protein.International journal of biochemistry and molecular biology · 2024Article
- Glomerulonephritis: immunopathogenesis and immunotherapy.Nature reviews. Immunology · 2023Review
- Accumulation of α-synuclein mediates podocyte injury in Fabry nephropathy.The Journal of clinical investigation · 2023Article
- Expansion-enhanced super-resolution radial fluctuations enable nanoscale molecular profiling of pathology specimens.Nature nanotechnology · 2023Article
- The classical pathway triggers pathogenic complement activation in membranous nephropathy.Nature communications · 2023Article
- Poroelastic modelling reveals the cooperation between two mechanisms for albuminuria.Journal of the Royal Society, Interface · 2023Article
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Authors and funding
23 authors at 8 institutions in 4 countries.
Funding
Abstract
Vertebrate life critically depends on renal filtration and excretion of low molecular weight waste products. This process is controlled by a specialized cell-cell contact between podocyte foot processes: the slit diaphragm (SD). Using a comprehensive set of targeted KO mice of key SD molecules, we provided genetic, functional, and high-resolution ultrastructural data highlighting a concept of a flexible, dynamic, and multilayered architecture of the SD. Our data indicate that the mammalian SD is composed of NEPHRIN and NEPH1 molecules, while NEPH2 and NEPH3 do not participate in podocyte intercellular junction formation. Unexpectedly, homo- and heteromeric NEPHRIN/NEPH1 complexes are rarely observed. Instead, single NEPH1 molecules appear to form the lower part of the junction close to the glomerular basement membrane with a width of 23 nm, while single NEPHRIN molecules form an adjacent junction more apically with a width of 45 nm. In both cases, the molecules are quasiperiodically spaced 7 nm apart. These structural findings, in combination with the flexibility inherent to the repetitive Ig folds of NEPHRIN and NEPH1, indicate that the SD likely represents a highly dynamic cell-cell contact that forms an adjustable, nonclogging barrier within the renal filtration apparatus.
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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.