ArticleThe Journal of cell biology1980
Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors.
Article in The Journal of cell biology, 1980. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.
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Who cites it
93 citing papers in PubMed, 342 citations in OpenAlex.
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- Aip1 promotes actin filament severing by cofilin and regulates constriction of the cytokinetic contractile ring.The Journal of biological chemistry · 2015Article
- Actin filament severing by cofilin is more important for assembly than constriction of the cytokinetic contractile ring.The Journal of cell biology · 2011Article
- Nitric oxide reduces sickle hemoglobin polymerization: potential role of nitric oxide-induced charge alteration in depolymerization.Archives of biochemistry and biophysics · 2011Article
- Spreading dynamics of biomimetic actin cortices.Biophysical journal · 2011Article
- The proline-rich domain of tau plays a role in interactions with actin.BMC cell biology · 2009Article
- Self-organization of keratin intermediate filaments into cross-linked networks.The Journal of cell biology · 2009Article
- MAP2-mediated in vitro interactions of brain microtubules and their modulation by cAMP.European biophysics journal : EBJ · 2009Article
- Multiple-particle tracking measurements of heterogeneities in solutions of actin filaments and actin bundles.Biophysical journal · 2000Article
- Mechanics of living cells measured by laser tracking microrheology.Biophysical journal · 2000Article
- Diffusing wave spectroscopy microrheology of actin filament networks.Biophysical journal · 1999Article
- Murine adseverin (D5), a novel member of the gelsolin family, and murine adseverin are induced by interleukin-9 in T-helper lymphocytes.Molecular and cellular biology · 1998Article
- Regulation of neurofilament interactions in vitro by natural and synthetic polypeptides sharing Lys-Ser-Pro sequences with the heavy neurofilament subunit NF-H: neurofilament crossbridging by antiparallel sidearm overlapping.Medical & biological engineering & computing · 1998Article
- Mechanical properties of actin filament networks depend on preparation, polymerization conditions, and storage of actin monomers.Biophysical journal · 1998Article
- F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF).Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Structure, subunit topology, and actin-binding activity of the Arp2/3 complex from Acanthamoeba.The Journal of cell biology · 1997Article
- Interaction of a Dictyostelium member of the plastin/fimbrin family with actin filaments and actin-myosin complexes.Molecular biology of the cell · 1997Article
- A new model for the interaction of dystrophin with F-actin.The Journal of cell biology · 1996Article
- Linking microfilaments to intracellular membranes: the actin-binding and vesicle-associated protein comitin exhibits a mannose-specific lectin activity.The EMBO journal · 1996Article
- Identification of a cyclase-associated protein (CAP) homologue in Dictyostelium discoideum and characterization of its interaction with actin.Molecular biology of the cell · 1996Article
33 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have studied the kinetics of the gelation process that occurs upon warming cold extracts of Acanthamoeba using a low-shear falling ball assay. We find that the reaction has at least two steps, requires 0.5 mM ATP and 1.5 mM MgCl2, and is inhibited by micromolar Ca++. The optimum pH is 7.0 and temperature, 25 degrees-30 degrees C. The rate of the reaction is increased by cold preincubation with both MgCl2 and ATP. Nonhydrolyzable analogues of ATP will not substitute for ATP either in this "potentiation reaction" or in the gelation process. Either of two purified or any one of four partially purified Acanthamoeba proteins will cross-link purified actin to form a gel, but none can account for the dependence of the reaction in the crude extract on Mg-ATP or its regulation by Ca++. This suggests that the extract contains, in addition to actin-cross-linking proteins, factors dependent on Mg-ATP and Ca++ that regulate the gelation process.
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