The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association
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Citations
Cites
The Regulation of Rabbit Skeletal Muscle Contraction
Spudich, J. A., & Watt, S. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62016-2 · Cited by 4,493
Yin, H. L., & Stossel, T. P. (1979) · Nature · doi:10.1038/281583a0 · Cited by 779
Mechanism of action of cytochalasin B on actin
MacLean-Fletcher, S. (1980) · Cell · doi:10.1016/0092-8674(80)90619-4 · Cited by 755
Self-citationActin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells
Carlsson, L., Nyström, L.-E., Sundkvist, I., Markey, F., & Lindberg, U. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90166-8 · Cited by 701
A New Calibration Procedure for Gel Filtration Columns
Ackers, G. K. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)95955-7 · Cited by 412
MacLean-Fletcher, S. D., & Pollard, T. D. (1980) · The Journal of cell biology · doi:10.1083/jcb.85.2.414 · Cited by 340
Self-citationCytochalasin inhibits the rate of elongation of actin filament fragments
Brown, S., & Spudich, J. (1979) · The Journal of Cell Biology · doi:10.1083/jcb.83.3.657 · Cited by 295
Brenner, S. L., & Korn, E. D. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86660-7 · Cited by 264
Cytochalasins inhibit nuclei-induced actin polymerization by blocking filament elongation.
Lin, D. C., Tobin, K. D., Grumet, M., & Lin, S. (1980) · The Journal of cell biology · doi:10.1083/jcb.84.2.455 · Cited by 256
Cytochalasin B and the structure of actin gels
Hartwig, J. H., & Stossel, T. P. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90366-8 · Cited by 234
Cited by
Actin and Actin-Binding Proteins
Pollard, T. D. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018226 · Cited by 912
Self-citationFlexibility of Actin Filaments Derived from Thermal Fluctuations
Isambert, H., Venier, P., Maggs, A. C., Fattoum, A., Kassab, R., Pantaloni, D., & Carlier, M.-F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.19.11437 · Cited by 622
How profilin promotes actin filament assembly in the presence of thymosin β4
Pantaloni, D., & Carlier, M.-F. (1993) · Cell · doi:10.1016/0092-8674(93)90544-z · Cited by 543
Higgs, H. N., & Pollard, T. D. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.6.1311 · Cited by 446
Self-citationInteraction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex
Marchand, J.-B., Kaiser, D. A., Pollard, T. D., & Higgs, H. N. (2001) · Nature Cell Biology · doi:10.1038/35050590 · Cited by 331
Self-citation
Metadata
- Authors
- MacLean-Fletcher, S., & Pollard, T. D.
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 1980-09
- Volume
- 96
- Issue
- 1
- Pages
- 18-27
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W1982014176
- Cited by
- 465
- References
- 14
- FWCI
- 8.81
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association. https://app.cochat.ai/papers/10.1016/0006-291x(80)91175-4
- The paper
- MacLean-Fletcher, S., & Pollard, T. D. (1980). Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association. Biochemical and Biophysical Research Communications. https://doi.org/10.1016/0006-291x(80)91175-4
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.