The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties.
Open accessAbstract
We observe that one of the high molecular mass microtubule-associated proteins (MAPs) from brain exhibits nucleotide-dependent binding to microtubules. We identify the protein as MAP IC, which was previously described in this laboratory as a minor component of standard microtubule preparations (Bloom, G.S., T. Schoenfeld, and R.B. Vallee, 1984, J. Cell Biol., 98:320-330). We find that MAP 1C is enriched in microtubules prepared in the absence of nucleotide. Kinesin is also found in these preparations, but can be specifically extracted with GTP. A fraction highly enriched in MAP 1C can be prepared by subsequent extraction of the microtubules with ATP. Two activities cofractionate with MAP 1C upon further purification, a microtubule-activated ATPase activity and a microtubule-translocating activity. These activities indicate a role for the protein in cytoplasmic motility. MAP 1C coelectrophoreses with the beta heavy chain of Chlamydomonas flagellar dynein, and has a sedimentation coefficient of 20S. Exposure to ultraviolet light in the presence of vanadate and ATP results in the production of two large fragments of MAP 1C. These characteristics suggest that MAP 1C may be a cytoplasmic analogue of axonemal dynein.
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
Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
VALE, R., REESE, T., & SHEETZ, M. (1985) · Cell · doi:10.1016/s0092-8674(85)80099-4 · Cited by 1,993 · cited 5×
“In other respects the protein differed from MAP 1C. In particular, HMW 4 bundled microtubules, behavior not seen with MAP 1C. Vale et al, (1985a) found a high molecular mass protein in their kinesin preparations, though the protein was not seen in calf brain.”
BackgroundMethodInfluentialCleveland, D. W., Hwo, S.-Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90213-3 · Cited by 915 · cited 1×
“The four smaller ,polypeptides were similar in electrophoretic mobility and composition to the tau MAPs ( Cleveland et al., 1977 ), and the lower two bands migrated very close to alpha- and beta-tubulin.”
BackgroundThe identification of a dynein ATPase in unfertilized sea urchin eggs
Pratt, M. M. (1980) · Developmental Biology · doi:10.1016/0012-1606(80)90438-8 · Cited by 89
Murphy, D. B., Hiebsch, R. R., & Wallis, K. T. (1983) · The Journal of cell biology · doi:10.1083/jcb.96.5.1298 · Cited by 26
Cited by
Translocation of inhaled ultrafine particles to the brain
Oberdörster, G., Sharp, Z., Atudorei, V., Elder, A., Gelein, R., Kreyling, W., & Cox, C. (2004) · Inhalation Toxicology · doi:10.1080/08958370490439597 · Cited by 2,606
The Molecular Motor Toolbox for Intracellular Transport
Vale, R. D. (2003) · Cell · doi:10.1016/s0092-8674(03)00111-9 · Cited by 1,982
Dynamin and Its Role in Membrane Fission
Hinshaw, J. E. (2000) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.16.1.483 · Cited by 699
Axonal transport: cargo-specific mechanisms of motility and regulation
Maday, S., Twelvetrees, A. E., Moughamian, A. J., & Holzbaur, E. L. F. (2014) · Neuron · doi:10.1016/j.neuron.2014.10.019 · Cited by 683
The cytoplasmic dynein transport machinery and its many cargoes
Reck-Peterson, S. L., Redwine, W. B., Vale, R. D., & Carter, A. P. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0004-3 · Cited by 659
Metadata
- Authors
- Paschal, B. M., Shpetner, H. S., & Vallee, R. B.
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1987-09-01
- Volume
- 105
- Issue
- 3
- Pages
- 1273-1282
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W1982275607
- Cited by
- 568
- References
- 4
- FWCI
- 20.43
- 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: MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties. https://app.cochat.ai/papers/10.1083/jcb.105.3.1273
- The paper
- Paschal, B. M., Shpetner, H. S., & Vallee, R. B. (1987). MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties. The Journal of cell biology. https://doi.org/10.1083/jcb.105.3.1273
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.
