ArticleThe Journal of biological chemistry2017
The activities of the C-terminal regions of the formin protein disheveled-associated activator of morphogenesis (DAAM) in actin dynamics.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Regulation of the formin INF2 by actin monomers and calcium/calmodulin.The Journal of cell biology · 2026Article
- Deconvolution Analysis of G and F-Actin Unfolding: Insights into the Thermal Stability and Structural Modifications Induced by PACAP.International journal of molecular sciences · 2025Article
- Exploring the Role of Neuropeptide PACAP in Cytoskeletal Function Using Spectroscopic Methods.International journal of molecular sciences · 2024Article
- Changes of Ex Vivo Cervical Epithelial Cells Due to Electroporation with JMY.International journal of molecular sciences · 2023Article
- Review
- Actin Bundles Dynamics and Architecture.Biomolecules · 2023Review
- The Mechanisms of Thin Filament Assembly and Length Regulation in Muscles.International journal of molecular sciences · 2022Review
- Molecular Dissection of DAAM Function during Axon Growth in Drosophila Embryonic Neurons.Cells · 2022Article
- The C-terminal tail extension of myosin 16 acts as a molten globule, including intrinsically disordered regions, and interacts with the N-terminal ankyrin.The Journal of biological chemistry · 2021Article
- Myosin XVI in the Nervous System.Cells · 2020Review
- The Activities of the Gelsolin Homology Domains of Flightless-I in Actin Dynamics.Frontiers in molecular biosciences · 2020Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Disheveled-associated activator of morphogenesis (DAAM) is a diaphanous-related formin protein essential for the regulation of actin cytoskeleton dynamics in diverse biological processes. The conserved formin homology 1 and 2 (FH1-FH2) domains of DAAM catalyze actin nucleation and processively mediate filament elongation. These activities are indirectly regulated by the N- and C-terminal regions flanking the FH1-FH2 domains. Recently, the C-terminal diaphanous-autoregulatory domain (DAD) and the C terminus (CT) of formins have also been shown to regulate actin assembly by directly interacting with actin. Here, to better understand the biological activities of DAAM, we studied the role of DAD-CT regions of
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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.