ArticleiScience2019
Membrane-Deformation Ability of ANKHD1 Is Involved in the Early Endosome Enlargement.
Article in iScience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 19 citations in OpenAlex.
- Regulation of Notch signaling by multiple Ankyrin repeat containing protein Mask.Cell communication and signaling : CCS · 2025Article
- Selection Increases Mitonuclear DNA Discordance but Reconciles Incompatibility in African Cattle.Molecular biology and evolution · 2025Article
- Nucleic acid-binding KH domain proteins influence a spectrum of biological pathways including as part of membrane-localized complexes.Journal of structural biology: X · 2024Article
- Evaluating the Molecular Properties and Function of ANKHD1, and Its Role in Cancer.International journal of molecular sciences · 2023Review
- Rai14 is a novel interactor of Invariant chain that regulates macropinocytosis.Frontiers in immunology · 2023Article
- Chlamydia trachomatis Alters Mitochondrial Protein Composition and Secretes Effector Proteins That Target Mitochondria.mSphere · 2022Article
- Article
- Heterozygous ANKRD17 loss-of-function variants cause a syndrome with intellectual disability, speech delay, and dysmorphism.American journal of human genetics · 2021Article
- Emerging functions for ANKHD1 in cancer-related signaling pathways and cellular processes.BMB reports · 2020Review
- Protein Amphipathic Helix Insertion: A Mechanism to Induce Membrane Fission.Frontiers in cell and developmental biology · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ankyrin-repeat domains (ARDs) are conserved in large numbers of proteins. ARDs are composed of various numbers of ankyrin repeats (ANKs). ARDs often adopt curved structures reminiscent of the Bin-Amphiphysin-Rvs (BAR) domain, which is the dimeric scaffold for membrane tubulation. BAR domains sometimes have amphipathic helices for membrane tubulation and vesiculation. However, it is unclear whether ARD-containing proteins exhibit similar membrane deformation properties. We found that the ARD of ANK and KH domain-containing protein 1 (ANKHD1) dimerize and deform membranes into tubules and vesicles. Among 25 ANKs of ANKHD1, the first 15 ANKs can form a dimer and the latter 10 ANKs enable membrane tubulation and vesiculation through an adjacent amphipathic helix and a predicted curved structure with a positively charged surface, analogous to BAR domains. Knockdown and localization of ANKHD1 suggested its involvement in the negative regulation of early endosome enlargement owing to its membrane vesiculation.
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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.