ArticleProceedings of the National Academy of Sciences of the United States of America1986
Actin-severing activity copurifies with phosphofructokinase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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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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
6 citing papers in PubMed, 21 citations in OpenAlex.
- Mechanisms of actin-binding proteins in glycolysis-cytoskeleton coupling.Journal of translational medicine · 2026Review
- Direct interaction between GluR2 and GAPDH regulates AMPAR-mediated excitotoxicity.Molecular brain · 2012Article
- Cotransport of glyceraldehyde-3-phosphate dehydrogenase and actin in axons of chicken motoneurons.Cellular and molecular neurobiology · 1999Article
- Stimulation of endogenous ADP-ribosylation by brefeldin A.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
- Fluorescent phallotoxins as probes for filamentous actin.Journal of muscle research and cell motility · 1988Review
- Microinjection of gelsolin into living cells.The Journal of cell biology · 1987Article
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 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microinjection of muscle 6-phosphofructokinase (PFK; EC 2.7.1.11) into tissue culture cells led to a reversible disintegration of microfilament bundles (stress fibers). The mode of disruption as well as of recovery of stress fibers was very similar to that found previously in experiments performed with the actin-severing protein brevin, an extracellular variant of gelsolin. PFK, like brevin, was also capable of disrupting stress fibers in detergent-extracted cells and in ethanol-fixed cells, in a Ca2+-dependent manner. When compared with heart muscle gelsolin, PFK comigrated with the 85- to 90-kDa band. Antibodies against PFK crossreacted with gelsolin from the same species. These results point to a tight association between polypeptides with similar biochemical and immunological parameters present in both preparations. They suggest hitherto unexpected cellular control mechanisms for both microfilament functions and glycolysis.
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Registered trials
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