Rotational dynamics of spin-labeled F-actin in the sub-millisecond time range
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Actin contains five cysteine residues, and C374 incorporates more than 70% of spin labels during spin labeling reactions.
“Although actin contains five cysteine residues, a number of studies has shown that the C-terminal C374, which is in close proximity to actin’s hydrophobic pocket (Fig. 2d), is most solvent exposed (Supplementary Fig. 4a, b) and incorporates more than 70% of spin labels during spin labeling reactions37–41.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [40]
Cys374 of actin is solvent exposed and can be labeled with the spin label MTSSL.
“Cys374 of actin is solvent exposed and can be labeled with the spin label MTSSL37–41.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [40]
Binding of Tau and MAP2 to filamentous actin results in actin cross-linking and filament bundling.
“Binding of Tau and MAP2 to filamentous actin results in actin cross-linking and filament bundling5, 6, 14, 22, 40–43.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [40]
Cited by
Sorted by citations
Cabrales Fontela, Y., Kadavath, H., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications · doi:10.1038/s41467-017-02230-8 · Cited by 148 · see citing works
- Authors
- Thomas, D. D., Seidel, J. C., & Gergely, J.
- Affiliations
- Boston Biomedical Research Institute (US)
- ORCID
- Thomas, David D.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1979-08
- Volume
- 132
- Issue
- 3
- Pages
- 257-273
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W1979513345
- Cited by
- 137
- References
- 0
- Citations by year
- 2025: 1 · 2023: 1 · 2020: 2 · 2019: 2 · 2018: 2 · 2017: 1 · 2015: 1 · 2013: 2 · 2012: 1
- FWCI
- 7.55
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Electron Spin Resonance Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Keywords
- F-actin, myosin subfragment 1, actomyosin, actin-tropomyosin complex
- MeSH terms
- Actins, Electron Spin Resonance Spectroscopy, Myosins, Protein Conformation, Rotation, Spin Labels, Time Factors, Tropomyosin, Myosin Subfragments
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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