ArticleBiophysical journal2002
Role of the DNase-I-binding loop in dynamic properties of actin filament.
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 17 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
17 citing papers in PubMed, 49 citations in OpenAlex.
- The divergent intron-containing actin in sponge morphogenetic processes.NAR genomics and bioinformatics · 2025Article
- Myopathy-Sensitive G-Actin Segment 227-235 Is Involved in Salt-Induced Stabilization of Contacts within the Actin Filament.International journal of molecular sciences · 2021Article
- Bacterial Actin-Specific Endoproteases Grimelysin and Protealysin as Virulence Factors Contributing to the Invasive Activities ofInternational journal of molecular sciences · 2020Review
- Tropomyosin isoforms regulate cofilin 1 activity by modulating actin filament conformation.Archives of biochemistry and biophysics · 2020Article
- K336I mutant actin alters the structure of neighbouring protomers in filaments and reduces affinity for actin-binding proteins.Scientific reports · 2019Article
- ANGUSTIFOLIA Regulates Actin Filament Alignment for Nuclear Positioning in Leaves.Plant physiology · 2019Article
- Cryo-EM reveals different coronin binding modes for ADP- and ADP-BeFx actin filaments.Nature structural & molecular biology · 2014Article
- Draft Genome Sequence of Serratia grimesii Strain A2.Genome announcements · 2014Article
- Structural differences explain diverse functions of Plasmodium actins.PLoS pathogens · 2014Article
- Role of calpains in the injury-induced dysfunction and degeneration of the mammalian axon.Neurobiology of disease · 2013Review
- Structural states and dynamics of the D-loop in actin.Biophysical journal · 2012Article
- Structural polymorphism in F-actin.Nature structural & molecular biology · 2010Article
- Mutation of actin Tyr-53 alters the conformations of the DNase I-binding loop and the nucleotide-binding cleft.The Journal of biological chemistry · 2010Article
- Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Phosphorylation of actin Tyr-53 inhibits filament nucleation and elongation and destabilizes filaments.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- The crystal structure of a cross-linked actin dimer suggests a detailed molecular interface in F-actin.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Role of actin DNase-I-binding loop in myosin subfragment 1-induced polymerization of G-actin: implications for the mechanism of polymerization.Biophysical journal · 2005Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Effects of proteolytic modifications of the DNase-I-binding loop (residues 39-51) in subdomain 2 of actin on F-actin dynamics were investigated by measuring the rates of the polymer subunit exchange with the monomer pool at steady state and of ATP hydrolysis associated with it, and by determination of relative rate constants for monomer addition to and dissociation from the polymer ends. Cleavage of actin between Gly-42 and Val-43 by protease ECP32 resulted in enhancement of the turnover rate of polymer subunits by an order of magnitude or more, in contrast to less than a threefold increase produced by subtilisin cleavage between Met-47 and Gly-48. Probing the structure of the modified actins by limited digestion with trypsin revealed a correlation between the increased F-actin dynamics and a change in the conformation of subdomain 2, indicating a more open state of the filament subunits relative to intact F-actin. The cleavage with trypsin and steady-state ATPase were cooperatively inhibited by phalloidin, with half-maximal effects at phalloidin to actin molar ratio of 1:8 and full inhibition at a 1:1 ratio. The results support F-actin models in which only the N-terminal segment of loop 39-51 is involved in monomer-monomer contacts, and suggest a possibility of regulation of actin dynamics in the cell through allosteric effects on this segment of the actin polypeptide chain.
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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.