The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins.
Open accessAbstract
Two high molecular weight heat shock proteins, HSP90 (Mr, 90,000) and HSP100 (Mr, 100,000), were separately purified from extracts of cultured cells of a mouse lymphoma cell line, L5178Y. Both of the HSPs exist in homodimeric form under physiological conditions. Their physicochemical properties are quite similar to each other. Each of the purified HSPs was shown to coprecipitate with rabbit skeletal muscle actin under actin-polymerizing conditions. Both HSP90 and HSP100 increased the low-shear viscosity of filamentous actin solutions in a dose-dependent manner, which suggests that these HSPs cross-link actin filaments. Although some molecular properties and the effects described above on actin solution of HSP90 and HSP100 resemble those of alpha-actinin, the HSPs were distinguished from alpha-actinin by various means, including visualization of molecular shapes by electron microscopy with the aid of the low-angle rotary shadowing technique. Immunofluorescence staining by specific antisera against HSP90 revealed that HSP90 was localized in ruffling membranes in addition to the cytoplasmic space.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,221
Cleveland, D. W., Fischer, S. G., Kirschner, M. W., & Laemmli, U. K. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75212-0 · Cited by 5,556
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
High resolution two-dimensional electrophoresis of basic as well as acidic proteins
O'Farrell, P. Z., Goodman, H. M., & O'Farrell, P. H. (1977) · Cell · doi:10.1016/0092-8674(77)90176-3 · Cited by 3,513
The induction of gene activity in drosophila by heat shock
Ashburner, M., & Bonner, J. J. (1979) · Cell · doi:10.1016/0092-8674(79)90150-8 · Cited by 1,287
Fluorescent phallotoxin, a tool for the visualization of cellular actin.
Wulf, E., Deboben, A., Bautz, F. A., Faulstich, H., & Wieland, T. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4498 · Cited by 786
Actin Antibody: The Specific Visualization of Actin Filaments in Non-Muscle Cells
Lazarides, E., & Weber, K. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.6.2268 · Cited by 723
Catelli, M. G., Binart, N., Jung-Testas, I., Renoir, J. M., Baulieu, E. E., Feramisco, J. R., & Welch, W. J. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb04055.x · Cited by 516
Welch, W. J., & Feramisco, J. R. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43075-4 · Cited by 506
Cited by
Steroid Receptor Interactions with Heat Shock Protein and Immunophilin Chaperones*
Pratt, W. B., & Toft, D. O. (1997) · Endocrine Reviews · doi:10.1210/edrv.18.3.0303 · Cited by 1,791
Whitesell, L., Mimnaugh, E. G., De Costa, B., Myers, C. E., & Neckers, L. M. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8324 · Cited by 1,444
The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
Hoter, A., El-Sabban, M. E., & Naim, H. Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092560 · Cited by 693
Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., & Lindquist, S. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3919 · Cited by 641
Prodromou, C., Panaretou, B., Chohan, S., Siligardi, G., O'Brien, R., Ladbury, J. E., Roe, S. M., Piper, P. W., & Pearl, L. H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.16.4383 · Cited by 492
Metadata
- Authors
- Koyasu, S., Nishida, E., Kadowaki, T., Matsuzaki, F., Iida, K., Harada, F., Kasuga, M., Sakai, H., & Yahara, I.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1986-11
- Volume
- 83
- Issue
- 21
- Pages
- 8054-8058
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2043881813
- Cited by
- 329
- References
- 34
- FWCI
- 7.46
- Type
- journal article
- Language
- en
- Open access
- green
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.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins. https://app.cochat.ai/papers/10.1073/pnas.83.21.8054
- The paper
- Koyasu, S., Nishida, E., Kadowaki, T., Matsuzaki, F., Iida, K., Harada, F., Kasuga, M., Sakai, H., & Yahara, I. (1986). Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.83.21.8054
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.