ArticleProceedings of the National Academy of Sciences of the United States of America1993
Formins: phosphoprotein isoforms encoded by the mouse limb deformity locus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 28 citations in OpenAlex.
- The scaffold-protein IQGAP1 enhances and spatially restricts the actin-nucleating activity of Diaphanous-related formin 1 (DIAPH1).The Journal of biological chemistry · 2020Article
- Mammalian Diaphanous-related formin-1 restricts early phases of influenza A/NWS/33 virus (H1N1) infection in LLC-MK2 cells by affecting cytoskeleton dynamics.Molecular and cellular biochemistry · 2018Article
- Formins: emerging players in the dynamic plant cell cortex.Scientifica · 2012Review
- The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages.Molecular and cellular biology · 2000Article
- The role of a single formin isoform in the limb and renal phenotypes of limb deformity.Molecular medicine (Cambridge, Mass.) · 1997Article
- Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains.The EMBO journal · 1996Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mutations at the mouse limb deformity (ld) locus result in defects of growth and patterning of the limb and kidney during embryonic development. The gene responsible for this phenotype is large and complex, with the capacity to generate a number of alternatively spliced messenger RNA transcripts encoding nuclear protein isoforms called "formins." We have made polyclonal antibodies to specific formin peptides and have confirmed the authenticity of the antibodies' reactivity, using cell lines derived from mice with molecularly defined mutations at the ld locus. In addition, we have used these antibodies to detect and characterize polypeptides encoded by both wild-type and mutant ld alleles. In so doing, we show that a formin isoform (i) is modified by posttranslational phosphorylation at serine and threonine residues and (ii) when present in a crude nuclear extract, is retained by DNA-cellulose.
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Registered trials
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