The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Ankyrin Repeat: A Unique Motif Mediating Protein−Protein Interactions
Abstract
Ankyrin repeat, one of the most widely existing protein motifs in nature, consists of 30-34 amino acid residues and exclusively functions to mediate protein-protein interactions, some of which are directly involved in the development of human cancer and other diseases. Each ankyrin repeat exhibits a helix-turn-helix conformation, and strings of such tandem repeats are packed in a nearly linear array to form helix-turn-helix bundles with relatively flexible loops. The global structure of an ankyrin repeat protein is mainly stabilized by intra- and inter-repeat hydrophobic and hydrogen bonding interactions. The repetitive and elongated nature of ankyrin repeat proteins provides the molecular bases of the unique characteristics of ankyrin repeat proteins in protein stability, folding and unfolding, and binding specificity. Recent studies have demonstrated that ankyrin repeat proteins do not recognize specific sequences, and interacting residues are discontinuously dispersed into the whole molecules of both the ankyrin repeat protein and its partner. In addition, the availability of thousands of ankyrin repeat sequences has made it feasible to use rational design to modify the specificity and stability of physiologically important ankyrin repeat proteins and even to generate ankyrin repeat proteins with novel functions through combinatorial chemistry approaches.
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Stem-cell ageing modified by the cyclin-dependent kinase inhibitor p16INK4a
Janzen, V., Forkert, R., Fleming, H. E., Saito, Y., Waring, M. T., Dombkowski, D. M., Cheng, T., DePinho, R. A., Sharpless, N. E., & Scadden, D. T. (2006) · Nature · doi:10.1038/nature05159 · Cited by 1,106
Living with or without cyclins and cyclin-dependent kinases
Sherr, C. J., & Roberts, J. M. (2004) · Genes & Development · doi:10.1101/gad.1256504 · Cited by 1,089
p16INK4a induces an age-dependent decline in islet regenerative potential
Krishnamurthy, J., Ramsey, M. R., Ligon, K. L., Torrice, C., Koh, A., Bonner-Weir, S., & Sharpless, N. E. (2006) · Nature · doi:10.1038/nature05092 · Cited by 1,003
Increasing p16INK4a expression decreases forebrain progenitors and neurogenesis during ageing
Molofsky, A. V., Slutsky, S. G., Joseph, N. M., He, S., Pardal, R., Krishnamurthy, J., Sharpless, N. E., & Morrison, S. J. (2006) · Nature · doi:10.1038/nature05091 · Cited by 972
High-affinity binders selected from designed ankyrin repeat protein libraries
Binz, H. K., Amstutz, P., Kohl, A., Stumpp, M. T., Briand, C., Forrer, P., Grütter, M. G., & Plückthun, A. (2004) · Nature Biotechnology · doi:10.1038/nbt962 · Cited by 656
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Evolution and comparative genomics of the most common Trichoderma species
Kubicek, C. P., Steindorff, A. S., Chenthamara, K., Manganiello, G., Henrissat, B., Zhang, J., Cai, F., Kopchinskiy, A. G., Kubicek, E. M., Kuo, A., et al. (2019) · BMC Genomics · doi:10.1186/s12864-019-5680-7 · Cited by 299
Cassago, A., Ferreira, A. P. S., Ferreira, I. M., Fornezari, C., Gomes, E. R. M., Greene, K. S., Pereira, H. M., Garratt, R. C., Dias, S. M. G., & Ambrosio, A. L. B. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1112495109 · Cited by 285
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Xiao, D., Ren, P., Su, H., Yue, M., Xiu, R., Hu, Y., Liu, H., & Qing, G. (2015) · Oncotarget · doi:10.18632/oncotarget.5821 · Cited by 80
Rab40C is a novel Varp-binding protein that promotes proteasomal degradation of Varp in melanocytes
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Metadata
- Authors
- Li, J., Mahajan, A., & Tsai, M.-D.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-11-30
- Volume
- 45
- Issue
- 51
- Pages
- 15168-15178
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1995972219
- Cited by
- 651
- References
- 6
- FWCI
- 7.49
- Type
- journal article
- Language
- en
- Open access
- closed
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