The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
The ankyrin repeat as molecular architecture for protein recognition
Open accessAbstract
The ankyrin repeat is one of the most frequently observed amino acid motifs in protein databases. This protein–protein interaction module is involved in a diverse set of cellular functions, and consequently, defects in ankyrin repeat proteins have been found in a number of human diseases. Recent biophysical, crystallographic, and NMR studies have been used to measure the stability and define the various topological features of this motif in an effort to understand the structural basis of ankyrin repeat‐mediated protein–protein interactions. Characterization of the folding and assembly pathways suggests that ankyrin repeat domains generally undergo a two‐state folding transition despite their modular structure. Also, the large number of available sequences has allowed the ankyrin repeat to be used as a template for consensus‐based protein design. Such projects have been successful in revealing positions responsible for structure and function in the ankyrin repeat as well as creating a potential universal scaffold for molecular recognition.
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 new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4.
Serrano, M., Hannon, G. J., & Beach, D. (1993) · Nature · doi:10.1038/366704a0 · Cited by 3,650
Notch3 mutations in CADASIL, a hereditary adult-onset condition causing stroke and dementia
Joutel, A., Corpechot, C., Ducros, A., Vahedi, K., Chabriat, H., Mouton, P., Alamowitch, S., Domenga, V., Cécillion, M., Maréchal, E., et al. (1996) · Nature · doi:10.1038/383707a0 · Cited by 2,068
pl5INK4B is a potentia| effector of TGF-β-induced cell cycle arrest
Hannon, G. J., & Beach, D. (1994) · Nature · doi:10.1038/371257a0 · Cited by 1,950
A Switch Between Two-, Three-, and Four-stranded Coiled Coils in GCN4 Leucine Zipper Mutants
Harbury, P. B., Zhang, T., Kim, P. S., & Alber, T. (1993) · Science · doi:10.1126/science.8248779 · Cited by 1,490 · cited 2×
“Early design studies on the coiled-coil to understand the mechanisms of oligomerization, and the contribution of various positions to 1444 Protein Science, vol. 13 stability incorporated knowledge of available sequences (Harbury et al. 1993; Zhou et al. 1994).”
BackgroundRetinoblastoma-protein-dependent cell-cycle inhibition by the tumour suppressor p16
Lukas, J., Parry, D., Aagaard, L., Mann, D. J., Bartkova, J., Strauss, M., Peters, G., & Bartek, J. (1995) · Nature · doi:10.1038/375503a0 · Cited by 899
Tumour-derived p16 alleles encoding proteins defective in cell-cycle inhibition
Koh, J., Enders, G. H., David Dynlacht, B., & Harlow, E. (1995) · Nature · doi:10.1038/375506a0 · Cited by 516
Lim, S., Sala, C., Yoon, J., Park, S., Kuroda, S., Sheng, M., & Kim, E. (2001) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2000.0940 · Cited by 151
Synaptic Scaffolding Proteins in Rat Brain
Böckers, T. M., Mameza, M. G., Kreutz, M. R., Bockmann, J., Weise, C., Buck, F., Richter, D., Gundelfinger, E. D., & Kreienkamp, H.-J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102454200 · Cited by 137
Cited by
Sequence and structural analysis of BTB domain proteins
Stogios, P. J., Downs, G. S., Jauhal, J. J., Nandra, S. K., & Privé, G. G. (2005) · Genome Biology · doi:10.1186/gb-2005-6-10-r82 · Cited by 694
TRPV4: molecular conductor of a diverse orchestra
White, J. P. M., Cibelli, M., Urban, L., Nilius, B., McGeown, J. G., & Nagy, I. (2016) · Physiological Reviews · doi:10.1152/physrev.00016.2015 · Cited by 405
Crystal Structure of the CSL-Notch-Mastermind Ternary Complex Bound to DNA
Wilson, J. J., & Kovall, R. A. (2006) · Cell · doi:10.1016/j.cell.2006.01.035 · Cited by 371
Coleman, M. L., McDonough, M. A., Hewitson, K. S., Coles, C., Mecinovicí, J., Edelmann, M., Cook, K. M., Cockman, M. E., Lancaster, D. E., Kessler, B. M., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704102200 · Cited by 222
Phylogenomic analysis of the GIY-YIG nuclease superfamily
Dunin-Horkawicz, S., Feder, M., & Bujnicki, J. M. (2006) · BMC Genomics · doi:10.1186/1471-2164-7-98 · Cited by 133
Manes, N. P., Estep, R. D., Mottaz, H. M., Moore, R. J., Clauss, T. R. W., Monroe, M. E., Du, X., Adkins, J. N., Wong, S. W., & Smith, R. D. (2008) · Journal of Proteome Research · doi:10.1021/pr070432+ · Cited by 103
RNF24, a new TRPC interacting protein, causes the intracellular retention of TRPC
Lussier, M. P., Lepage, P. K., Bousquet, S. M., & Boulay, G. (2008) · Cell Calcium · doi:10.1016/j.ceca.2007.07.009 · Cited by 47
Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3
Cupo, R. R., Rizo, A. N., Braun, G. A., Tse, E., Chuang, E., Gupta, K., Southworth, D. R., & Shorter, J. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111408 · Cited by 25
Monomer‐scale design of functional protein polymers using consensus repeat sequences
Chang, M. P., Huang, W., & Mai, D. J. (2021) · Journal of Polymer Science · doi:10.1002/pol.20210506 · Cited by 20
Cspg4 high microglia contribute to microgliosis during neurodegeneration
Liu, Y.-J., Ding, Y., Yin, Y.-Q., Xiao, H., Hu, G., & Zhou, J.-W. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2210643120 · Cited by 14
Adcox, H. E., Hunt, J. R., Allen, P. E., Siff, T. E., Rodino, K. G., Ottens, A. K., & Carlyon, J. A. (2024) · Nature Communications · doi:10.1038/s41467-024-52119-6 · Cited by 13
Crystal Structure of Human ASB9-2 and Substrate-Recognition of CKB
Fei, X., Gu, X., Fan, S., Yang, Z., Li, F., Zhang, C., Gong, W., Mao, Y., & Ji, C. (2012) · The Protein Journal · doi:10.1007/s10930-012-9401-1 · Cited by 12
Metadata
- Authors
- Mosavi, L. K., Cammett, T. J., Desrosiers, D. C., & Peng, Z.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2004-06
- Volume
- 13
- Issue
- 6
- Pages
- 1435-1448
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W2065155413
- Cited by
- 907
- References
- 8
- FWCI
- 13.23
- Type
- journal article
- Language
- en
- Open access
- bronze
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.
