ArticleBiophysical journal2002
Cofilin and DNase I affect the conformation of the small domain of actin.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Role of Tpm Isoforms Produced by theBiomolecules · 2025Article
- Binding of Red Clover Isoflavones to Actin as A Potential Mechanism of Anti-Metastatic Activity Restricting the Migration of Cancer Cells.Molecules (Basel, Switzerland) · 2018Article
- Cofilin-induced cooperative conformational changes of actin subunits revealed using cofilin-actin fusion protein.Scientific reports · 2016Article
- A small molecule inhibitor of tropomyosin dissociates actin binding from tropomyosin-directed regulation of actin dynamics.Scientific reports · 2016Article
- Coordination of the filament stabilizing versus destabilizing activities of cofilin through its secondary binding site on actin.Cytoskeleton (Hoboken, N.J.) · 2014Article
- Biophysics of actin filament severing by cofilin.FEBS letters · 2013Review
- Molecular origins of cofilin-linked changes in actin filament mechanics.Journal of molecular biology · 2013Article
- Conformational dynamics of actin: effectors and implications for biological function.Cytoskeleton (Hoboken, N.J.) · 2010Review
- Cofilin dissociates Arp2/3 complex and branches from actin filaments.Current biology : CB · 2009Article
- Flavonoids affect actin functions in cytoplasm and nucleus.Biophysical journal · 2007Article
- Thymosin beta4 induces a conformational change in actin monomers.Biophysical journal · 2006Article
- ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments.The Journal of cell biology · 2003Article
- A method for rapidly screening functionality of actin mutants and tagged actins.Biological procedures onlineArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cofilin binding induces an allosteric conformational change in subdomain 2 of actin, reducing the distance between probes attached to Gln-41 (subdomain 2) and Cys-374 (subdomain 1) from 34.4 to 31.4 A (pH 6.8) as demonstrated by fluorescence energy transfer spectroscopy. This effect was slightly less pronounced at pH 8.0. In contrast, binding of DNase I increased this distance (35.5 A), a change that was not pH-sensitive. Although DNase I-induced changes in the distance along the small domain of actin were modest, a significantly larger change (38.2 A) was observed when the ternary complex of cofilin-actin-DNase I was formed. Saturation binding of cofilin prevents pyrene fluorescence enhancement normally associated with actin polymerization. Changes in the emission and excitation spectra of pyrene-F actin in the presence of cofilin indicate that subdomain 1 (near Cys-374) assumes a G-like conformation. Thus, the enhancement of pyrene fluorescence does not correspond to the extent of actin polymerization in the presence of cofilin. The structural changes in G and F actin induced by these actin-binding proteins may be important for understanding the mechanism regulating the G-actin pool in cells.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.