ArticleBiophysical journal1995
A single myosin head can be cross-linked to the N termini of two adjacent actin monomers.
Article in Biophysical journal, 1995. 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.
- Highly selective inhibition of myosin motors provides the basis of potential therapeutic application.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Unique charge distribution in surface loops confers high velocity on the fast motor protein Chara myosin.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Binding assay and preliminary X-ray crystallographic analysis of ACTIBIND, a protein with anticarcinogenic and antiangiogenic activities.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007Article
- Interaction of myosin with F-actin: time-dependent changes at the interface are not slow.Biophysical journal · 2000Article
- Histidine-tagged wild-type yeast actin: its properties and use in an approach for obtaining yeast actin mutants.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Small segmental rearrangements in the myosin head can explain force generation in muscle.Biophysical journal · 1996Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myosin subfragment-1 (S1) can be cross-linked to two actin monomers by 1-ethyl-3-[3-(dimethylamino)-propyl]-carbodiimide only when F-actin is in excess over S1. Electron micrographs of the covalent actin2-S1 complex showed that S1 was cross-linked to two adjacent monomers of the same actin filament. Cross-linking experiments with pre-proteolyzed S1 derivatives in combination with a proteolytic dissection of the intact covalent actin2-S1 adduct (m = 265 kDa), revealed that two N-terminal segments of actin (residues 1-28) were covalently attached to a single S1 molecule. One was cross-linked to either the 20-kDa or the 50-kDa heavy chain fragments of S1, and the other only to the 50-kDa region. The doubly cross-linked product was formed under physiological ionic strength with S1 or with reconstituted myosin filaments, regardless of the presence of ADP or the regulatory proteins, tropomyosin and troponin. Finally, we found that this cross-linking could also take place within myofibrils in the rigor state. These results demonstrate that under nonsaturating conditions, the actin-S1 interface encompasses a much larger region than that recently proposed for the nonphysiological, fully saturated actin filaments.
Indexed as
Identifiers
7787098PMC1281859W1443095410What 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.