The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Modulation of Calmodulin Plasticity in Molecular Recognition on the Basis of X-Ray Structures
Abstract
Calmodulin is the primary calcium-dependent signal transducer and regulator of a wide variety of essential cellular functions. The structure of calcium-calmodulin bound to the peptide corresponding to the calmodulin-binding domain of brain calmodulin-dependent protein kinase IIα was determined to 2 angstrom resolution. A comparison to two other calcium-calmodulin structures reveals how the central helix unwinds in order to position the two domains optimally in the recognition of different target enzymes and clarifies the role of calcium in maintaining recognition-competent domain structures.
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
Three-dimensional structure of myosin subfragment-1: a molecular motor
Rayment, I., Rypniewski, W., Schmidt-Base, K., Smith, R., Tomchick, D., Benning, M., Winkelmann, D., Wesenberg, G., & Holden, H. (1993) · Science · doi:10.1126/science.8316857 · Cited by 2,070
Solution structure of a calmodulin-target peptide complex by multidimensional NMR
Ikura, M., Clore, G. M., Gronenborn, A. M., Zhu, G., Klee, C. B., & Bax, A. (1992) · Science · doi:10.1126/science.1585175 · Cited by 1,269
Three-dimensional structure of calmodulin
Babu, Y. S., Sack, J. S., Greenhough, T. J., Bugg, C. E., Means, A. R., & Cook, W. J. (1985) · Nature · doi:10.1038/315037a0 · Cited by 1,035
Self-citationTarget Enzyme Recognition by Calmodulin: 2.4 Å Structure of a Calmodulin-Peptide Complex
Meador, W. E., Means, A. R., & Quiocho, F. A. (1992) · Science · doi:10.1126/science.1519061 · Cited by 1,033
Self-citationStructure of calmodulin refined at 2.2 Å resolution
Babu, Y. S., Bugg, C. E., & Cook, W. J. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90608-0 · Cited by 1,024
How calmodulin binds its targets: sequence independent recognition of amphiphilic α-helices
O'Neil, K. T., & DeGrado, W. F. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90177-d · Cited by 842
Klee, C. B., & Vanaman, T. C. (1982) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60470-2 · Cited by 778
Calmodulin structure refined at 1.7 Å resolution
Chattopadhyaya, R., Meador, W. E., Means, A. R., & Quiocho, F. A. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90324-d · Cited by 729
Self-citationRibbon models of macromolecules
Carson, M. (1987) · Journal of Molecular Graphics · doi:10.1016/0263-7855(87)80010-3 · Cited by 516
Gellman, S. H. (1991) · Biochemistry · doi:10.1021/bi00241a001 · Cited by 223
Cited by
Clapham, D. E. (2007) · Cell · doi:10.1016/j.cell.2007.11.028 · Cited by 4,175
Intrinsically disordered protein
Dunker, A. K., Lawson, J. D., Brown, C. J., Williams, R. M., Romero, P., Oh, J. S., Oldfield, C. J., Campen, A. M., Ratliff, C. M., Hipps, K. W., et al. (2001) · Journal of Molecular Graphics and Modelling · doi:10.1016/s1093-3263(00)00138-8 · Cited by 2,272
Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK
Zhu, X., Zhao, X., Burkholder, W. F., Gragerov, A., Ogata, C. M., Gottesman, M. E., & Hendrickson, W. A. (1996) · Science · doi:10.1126/science.272.5268.1606 · Cited by 1,258
Kirschner, M., & Gerhart, J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.15.8420 · Cited by 1,129
Intrinsically Disordered Proteins and Intrinsically Disordered Protein Regions
Oldfield, C. J., & Dunker, A. K. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-164947 · Cited by 1,057
Metadata
- Authors
- Meador, W. E., Means, A. R., & Quiocho, F. A.
- Venue
- Science
- Published
- 1993-12-10
- Volume
- 262
- Issue
- 5140
- Pages
- 1718-1721
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2031811477
- Cited by
- 608
- References
- 14
- FWCI
- 12.74
- 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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Modulation of Calmodulin Plasticity in Molecular Recognition on the Basis of X-Ray Structures. https://app.cochat.ai/papers/10.1126/science.8259515
- The paper
- Meador, W. E., Means, A. R., & Quiocho, F. A. (1993). Modulation of Calmodulin Plasticity in Molecular Recognition on the Basis of X-Ray Structures. Science. https://doi.org/10.1126/science.8259515
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.
