The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
In vitro reconstitution of calf brain microtubules: effects of solution variables
Abstract
The effects of solution variables on the in vitro reconstitution of calf brain tubulin, purified by the method of Weisenberg et al. (Weisenberg, R. C., Borisy, G. G., and Taylor, E. W. (1968), Biochemistry 7, 4466-4479; Weisenberg, R. C., and Timasheff, S. N. (1970), Biochemistry 9, 4110-4116), as modified by Lee et al. (Lee, J. C., Frigon, R. P., and Timasheff, S. N. (1973), J. Biol. Chem. 248, 7253-7262), were investigated at pH 7.0. Reconstitution of microtubules was successful in a variety of buffer systems, the free energy of the propagation step of microtubule formation being little dependent on the buffer. Microtubule formation is promoted by magnesium ions and guanosine triphosphate, but inhibited by calcium ions. The dependence of the apparent association constant for microtubule formation on ligand concentration was analyzed by the linked function theory of Wyman (Wyman, J. (1964), Adv. Protein Chem. 19, 224-286), leading to the conclusion that the formation of a tubulin-tubulin contact involves the binding of one additional magnesium ion per tubulin dimer. Microtubule formation is also accompanied by the apparent binding of one additional proton and the release of water molecules, as suggested by the thermodynamic parameters determined. The reaction is entropy driven with an apparent heat capacity change, deltaCp, of -1500 +/- 500 cal/deg-mol. The enhancement of tubulin reassembly by glycerol is most likely due to nonspecific protein-solvent general thermodynamic interactions.
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
A protein factor essential for microtubule assembly
Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089
Microtubule Assembly in the Absence of Added Nucleotides
Shelanski, M. L., Gaskin, F., & Cantor, C. R. (1973) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.70.3.765 · Cited by 2,053
Microtubule Formation in vitro in Solutions Containing Low Calcium Concentrations
Weisenberg, R. C. (1972) · Science · doi:10.1126/science.177.4054.1104 · Cited by 1,210
Colchicine-binding protein of mammalian brain and its relation to microtubules
Weisenberg, R. C., Broisy, G. G., & Taylor, E. W. (1968) · Biochemistry · doi:10.1021/bi00852a043 · Cited by 1,158
Turbidimetric studies of the in vitro assembly and disassembly of porcine neurotubules
Gaskin, F., Cantor, C. R., & Shelanski, M. L. (1974) · Journal of Molecular Biology · doi:10.1016/0022-2836(74)90048-5 · Cited by 816
A theory of linear and helical aggregations of macromolecules
Oosawa, F., & Kasai, M. (1962) · Journal of Molecular Biology · doi:10.1016/s0022-2836(62)80112-0 · Cited by 766
Murphy, D. B., & Borisy, G. G. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.7.2696 · Cited by 534
Glasstone, S. (1947) · Medical Entomology and Zoology · Cited by 329
Characterization of microtubule assembly in porcine brain extracts by viscometry
Olmsted, J. B., & Borisy, G. G. (1973) · Biochemistry · doi:10.1021/bi00745a037 · Cited by 317
Nucleated Assembly of Microtubules in Porcine Brain Extracts
Borisy, G. G., & Olmsted, J. B. (1972) · Science · doi:10.1126/science.177.4055.1196 · Cited by 316
Ionic and nucleotide requirements for microtubule polymerization in vitro
Olmsted, J. B., & Borisy, G. G. (1975) · Biochemistry · doi:10.1021/bi00684a032 · Cited by 293
Reconstitution of microtubules from purified calf brain tubulin
Lee, J. C., & Timasheff, S. N. (1975) · Biochemistry · doi:10.1021/bi00694a025 · Cited by 235
Self-citationThe Chemical Characterization of Calf Brain Microtubule Protein Subunits
Lee, J. C., Frigon, R. P., & Timasheff, S. N. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43386-3 · Cited by 226
Self-citationKirschner, M. W., Williams, R. C., Weingarten, M., & Gerhart, J. C. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.4.1159 · Cited by 203
Magnesium-induced self-association of calf brain tubulin. I. Stoichiometry
Frigon, R. P., & Timasheff, S. N. (1975) · Biochemistry · doi:10.1021/bi00692a001 · Cited by 173
Self-citationProperties of the depolymerization products of microtubules from mammalian brain
Weingarten, M. D., Suter, M. M., Littman, D. R., & Kirschner, M. W. (1974) · Biochemistry · doi:10.1021/bi00724a012 · Cited by 169
Tubulin: Nucleotide binding and enzymic activity
Jacobs, M., Smith, H., & Taylor, E. W. (1974) · Journal of Molecular Biology · doi:10.1016/0022-2836(74)90475-6 · Cited by 156
THE MECHANISM OF ACTION OF COLCHICINE
Wilson, L., & Meza, I. (1973) · The Journal of Cell Biology · doi:10.1083/jcb.58.3.709 · Cited by 155
Microtubule assembly: Some possible regulatory mechanisms
Olmsted, J. B., Marcum, J. M., Johnson, K. A., Allen, C. A., & Borisy, G. G. (1974) · Journal of Supramolecular Structure · doi:10.1002/jss.400020230 · Cited by 147
Interpretation of the light scattering from long rods
Berne, B. J. (1974) · Journal of Molecular Biology · doi:10.1016/0022-2836(74)90049-7 · Cited by 141
Assembly of microtubules from preformed, ring‐shaped protofilaments and 6‐s tubulin
Erickson, H. (1974) · Journal of Supramolecular Structure · doi:10.1002/jss.400020228 · Cited by 138
Quantitative electron microscopy of microtubule assembly in vitro
Kirschner, M. W., Honig, L. S., & Williams, R. C. (1975) · Journal of Molecular Biology · doi:10.1016/s0022-2836(75)80144-6 · Cited by 125
The mechanism of microtubule assembly in vitro
Kirschner, M. W., & Williams, R. C. (1974) · Journal of Supramolecular Structure · doi:10.1002/jss.400020229 · Cited by 114
Pressure-Induced Depolymerization of Brain Microtubules in Vitro
Salmon, E. D. (1975) · Science · doi:10.1126/science.1171523 · Cited by 81
THE DISSOCIATION OF CALCIUM AND MAGNESIUM PHOSPHATES
Greenwald, I., Redish, J., & Kibrick, A. C. (1940) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)73159-1 · Cited by 70
The in vitro polymerization of tubulin from beef brain
Lee, Y. C., Samson, F. E., Houston, L. L., et al. (1974) · Journal of Neurobiology · doi:10.1002/neu.480050404 · Cited by 68
Duplex microtubule is a new form of tubulin assembly induced by polycations
Jacobs, M., Bennett, P. M., & Dickens, M. J. (1975) · Nature · doi:10.1038/257707a0 · Cited by 61
REGULATION OF THE IN VIVO MITOTIC APPARATUS BY GLYCOLS AND METABOLIC INHIBITORS*
Rebhun, L. I., Jemiolo, D. K., Ivy, N., Mellon, M., & Nath, J. (1975) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1975.tb19214.x · Cited by 36
Cited by
Stability of Protein Pharmaceuticals
Manning, M. C., Patel, K., & Borchardt, R. T. (1989) · Pharmaceutical Research · doi:10.1023/a:1015929109894 · Cited by 1,078
Privalov, P. L. (1990) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239009090612 · Cited by 1,071
Timasheff, S. N. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.122225399 · Cited by 718
Self-citationTimasheff, S. N. (1998) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60656-7 · Cited by 620
Self-citationLacey, E. (1988) · International Journal for Parasitology · doi:10.1016/0020-7519(88)90175-0 · Cited by 560
Metadata
- Authors
- Lee, J. C., & Timasheff, S. N.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1977-04-19
- Volume
- 16
- Issue
- 8
- Pages
- 1754-1764
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1968324550
- Cited by
- 332
- References
- 28
- FWCI
- 9.53
- Type
- journal article
- Language
- en
- Open access
- closed
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
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.