ArticleThe Journal of biological chemistry2019
Intrinsic disorder and amino acid specificity modulate binding of the WW2 domain in kidney and brain protein (KIBRA) to synaptopodin.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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.
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Who cites it
4 citing papers in PubMed, 10 citations in OpenAlex.
- WWC1/2 regulate spinogenesis and cognition in mice by stabilizing AMOT.Cell death & disease · 2023Article
- Identification of AGXT2, SHMT1, and ACO2 as important biomarkers of acute kidney injury by WGCNA.PloS one · 2023Article
- Multivalent Angiomotin-like 1 and Yes-associated protein form a dynamic complex.Protein science : a publication of the Protein Society · 2022Article
- The Effect of Interleukin-4 and Dexamethasone on RNA-Seq-Based Transcriptomic Profiling of Human Podocytes: A Potential Role in Minimal Change Nephrotic Syndrome.Journal of clinical medicine · 2021Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The second WW domain (WW2) of the kidney and brain scaffolding protein, KIBRA, has an isoleucine (Ile-81) rather than a second conserved tryptophan and is primarily unstructured. However, it adopts the canonical triple-stranded antiparallel β-sheet structure of WW domains when bound to a two-PP
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Registered trials
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