Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication

RING Domain E3 Ubiquitin Ligases

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Oldfield, C. J., & Dunker, A. K. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-072711-164947 · Cited by 1,057

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Welcker, M., & Clurman, B. E. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2290 · Cited by 1,084

M-phase kinases induce phospho-dependent ubiquitination of somatic Wee1 by SCF β-TrCP

Watanabe, N., Arai, H., Nishihara, Y., Taniguchi, M., Watanabe, N., Hunter, T., & Osada, H. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307700101 · Cited by 472

Degradation of Cdc25A by β-TrCP during S phase and in response to DNA damage

Busino, L., Donzelli, M., Chiesa, M., Guardavaccaro, D., Ganoth, D., Valerio Dorrello, N., Hershko, A., Pagano, M., & Draetta, G. F. (2003) · Nature · doi:10.1038/nature02082 · Cited by 447

Sensing centromere tension: Aurora B and the regulation of kinetochore function

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Tumor suppression by the Fbw7 ubiquitin ligase: mechanisms and opportunities

Davis, R. J., Welcker, M., & Clurman, B. E. (2014) · Cancer Cell · doi:10.1016/j.ccell.2014.09.013 · Cited by 343

SCFβ-TRCP links Chk1 signaling to degradation of the Cdc25A protein phosphatase

Jin, J., Shirogane, T., Xu, L., Nalepa, G., Qin, J., Elledge, S. J., & Harper, J. W. (2003) · Genes & Development · doi:10.1101/gad.1157503 · Cited by 340

Modulation of Glucocorticoid Receptor Function via Phosphorylation

ISMAILI, N., & GARABEDIAN, M. J. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1321.007 · Cited by 318

Motifs, modules and games in bacteria

Wolf, D. M., & Arkin, A. P. (2003) · Current Opinion in Microbiology · doi:10.1016/s1369-5274(03)00033-x · Cited by 303

Shaggy/GSK3 antagonizes Hedgehog signalling by regulating Cubitus interruptus

Jia, J., Amanai, K., Wang, G., Tang, J., Wang, B., & Jiang, J. (2002) · Nature · doi:10.1038/nature733 · Cited by 288

Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity

Borg, M., Mittag, T., Pawson, T., Tyers, M., Forman-Kay, J. D., & Chan, H. S. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702580104 · Cited by 245

Structural assembly of cullin-RING ubiquitin ligase complexes

Zimmerman, E. S., Schulman, B. A., & Zheng, N. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.08.010 · Cited by 227

Suprafacial Orientation of the SCFCdc4 Dimer Accommodates Multiple Geometries for Substrate Ubiquitination

Tang, X., Orlicky, S., Lin, Z., Willems, A., Neculai, D., Ceccarelli, D., Mercurio, F., Shilton, B. H., Sicheri, F., & Tyers, M. (2007) · Cell · doi:10.1016/j.cell.2007.04.042 · Cited by 209

Regulation of Protein Tyrosine Kinase Signaling by Substrate Degradation during Brain Development

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Regulation of Epidermal Growth Factor Receptor Ubiquitination and Trafficking by the USP8·STAM Complex

Berlin, I., Schwartz, H., & Nash, P. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.016287 · Cited by 121

A High-Affinity Arg-X-X-Lys SH3 Binding Motif Confers Specificity for the Interaction between Gads and SLP-76 in T Cell Signaling

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Structural Basis for Specific Binding of the Gads SH3 Domain to an RxxK Motif-Containing SLP-76 Peptide

Liu, Q., Berry, D., Nash, P., Pawson, T., McGlade, C. J., & Li, S. S.-C. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00046-7 · Cited by 119

Homeostatic Control of Hpo/MST Kinase Activity through Autophosphorylation-Dependent Recruitment of the STRIPAK PP2A Phosphatase Complex

Zheng, Y., Liu, B., Wang, L., Lei, H., Pulgar Prieto, K. D., & Pan, D. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.11.076 · Cited by 110

Proteomic screen reveals Fbw7 as a modulator of the NF-κB pathway

Arabi, A., Ullah, K., Branca, R. M. M., Johansson, J., Bandarra, D., Haneklaus, M., Fu, J., Ariës, I., Nilsson, P., Den Boer, M. L., et al. (2012) · Nature Communications · doi:10.1038/ncomms1975 · Cited by 90

Understanding cullin-RING E3 biology through proteomics-based substrate identification

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The Affinity of Ets-1 for DNA is Modulated by Phosphorylation Through Transient Interactions of an Unstructured Region

Lee, G. M., Pufall, M. A., Meeker, C. A., Kang, H.-S., Graves, B. J., & McIntosh, L. P. (2008) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.07.064 · Cited by 58

Enzyme-substrate relationships in the ubiquitin system: approaches for identifying substrates of ubiquitin ligases

O’Connor, H. F., & Huibregtse, J. M. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2529-6 · Cited by 42

Restriction of histone gene transcription to S phase by phosphorylation of a chromatin boundary protein

Kurat, C. F., Lambert, J.-P., van Dyk, D., Tsui, K., van Bakel, H., Kaluarachchi, S., Friesen, H., Kainth, P., Nislow, C., Figeys, D., et al. (2011) · Genes & Development · doi:10.1101/gad.173427.111 · Cited by 41

A cyclin-dependent kinase-mediated phosphorylation switch of disordered protein condensation

Valverde, J. M., Dubra, G., Phillips, M., Haider, A., Elena-Real, C., Fournet, A., Alghoul, E., Chahar, D., Andrés-Sanchez, N., Paloni, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42049-0 · Cited by 33

Intrinsic protein disorder and protein modifications in the processing of biological signals

Phillips, A. H., & Kriwacki, R. W. (2020) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.09.003 · Cited by 21

The PP2A-B56 phosphatase opposes cyclin E autocatalytic degradation via site-specific dephosphorylation

Davis, R. J., Swanger, J., Hughes, B. T., & Clurman, B. E. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00657-16 · Cited by 15

Conformational Characterization of Intrinsically Disordered Proteins and Its Biological Significance

Delaforge, E., Cordeiro, T. N., Bernadó, P., & Sibille, N. (2018) · Modern Magnetic Resonance · doi:10.1007/978-3-319-28388-3_52 · Cited by 7