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The origins of protein phosphorylation
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Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244
Self-citationCalcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116
Wilks, A. F., Harpur, A. G., Kurban, R. R., Ralph, S. J., Zürcher, G., & Ziemiecki, A. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.4.2057 · Cited by 528
Cited by
Swatek, K. N., & Komander, D. (2016) · Cell Research · doi:10.1038/cr.2016.39 · Cited by 2,081
The growing landscape of lysine acetylation links metabolism and cell signalling
Choudhary, C., Weinert, B. T., Nishida, Y., Verdin, E., & Mann, M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3841 · Cited by 1,324
One‐thousand‐and‐one substrates of protein kinase CK2?
Meggio, F., & Pinna, L. A. (2003) · The FASEB Journal · doi:10.1096/fj.02-0473rev · Cited by 1,310
FDA-approved small-molecule kinase inhibitors
Wu, P., Nielsen, T. E., & Clausen, M. H. (2015) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2015.04.005 · Cited by 1,013
Recent progresses in small-molecule enzymatic fluorescent probes for cancer imaging
Liu, H.-W., Chen, L., Xu, C., Li, Z., Zhang, H., Zhang, X.-B., & Tan, W. (2018) · Chemical Society Reviews · doi:10.1039/c7cs00862g · Cited by 948
The emerging complexity of protein ubiquitination
Komander, D. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370937 · Cited by 821
VDAC, a multi-functional mitochondrial protein regulating cell life and death
Shoshan-Barmatz, V., De Pinto, V., Zweckstetter, M., Raviv, Z., Keinan, N., & Arbel, N. (2010) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2010.03.002 · Cited by 782
Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes
Vlastaridis, P., Kyriakidou, P., Chaliotis, A., Van de Peer, Y., Oliver, S. G., & Amoutzias, G. D. (2017) · GigaScience · doi:10.1093/gigascience/giw015 · Cited by 733
An atlas of substrate specificities for the human serine/threonine kinome
Johnson, J. L., Yaron, T. M., Huntsman, E. M., Kerelsky, A., Song, J., Regev, A., Lin, T.-Y., Liberatore, K., Cizin, D. M., Cohen, B. M., et al. (2023) · Nature · doi:10.1038/s41586-022-05575-3 · Cited by 728
Protein Phosphorylation: A Major Switch Mechanism for Metabolic Regulation
Humphrey, S. J., James, D. E., & Mann, M. (2015) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2015.09.013 · Cited by 558
Cerium Oxide Nanoparticles: A Brief Review of Their Synthesis Methods and Biomedical Applications
Dhall, A., & Self, W. (2018) · Antioxidants · doi:10.3390/antiox7080097 · Cited by 482
Small-molecule kinase inhibitors: an analysis of FDA-approved drugs
Wu, P., Nielsen, T. E., & Clausen, M. H. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2015.07.008 · Cited by 457
The Hexosamine Signaling Pathway: Deciphering the "O-GlcNAc Code"
Love, D. C., & Hanover, J. A. (2005) · Science's STKE · doi:10.1126/stke.3122005re13 · Cited by 461
Mass spectrometry-based proteomics: existing capabilities and future directions
Angel, T. E., Aryal, U. K., Hengel, S. M., Baker, E. S., Kelly, R. T., Robinson, E. W., & Smith, R. D. (2012) · Chemical Society Reviews · doi:10.1039/c2cs15331a · Cited by 441
The Role of Protein Loops and Linkers in Conformational Dynamics and Allostery
Papaleo, E., Saladino, G., Lambrughi, M., Lindorff-Larsen, K., Gervasio, F. L., & Nussinov, R. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00623 · Cited by 431
Cerium oxide nanoparticles: properties, biosynthesis and biomedical application
Singh, K. R., Nayak, V., Sarkar, T., & Singh, R. P. (2020) · RSC Advances · doi:10.1039/d0ra04736h · Cited by 428
The Role of Skeletal Muscle Glycogen Breakdown for Regulation of Insulin Sensitivity by Exercise
Jensen, J., Rustad, P. I., Kolnes, A. J., & Lai, Y.-C. (2011) · Frontiers in Physiology · doi:10.3389/fphys.2011.00112 · Cited by 412
Ca2+/Calmodulin-dependent Protein Kinases
Swulius, M. T., & Waxham, M. N. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8086-2 · Cited by 396
Methods for converting cysteine to dehydroalanine on peptides and proteins
Chalker, J. M., Gunnoo, S. B., Boutureira, O., Gerstberger, S. C., Fernández-González, M., Bernardes, G. J. L., Griffin, L., Hailu, H., Schofield, C. J., & Davis, B. G. (2011) · Chemical Science · doi:10.1039/c1sc00185j · Cited by 367
Phospho.ELM: A database of experimentally verified phosphorylation sites in eukaryotic proteins
Diella, F., Cameron, S., Gemünd, C., Linding, R., Via, A., Kuster, B., Sicheritz-Pontén, T., Blom, N., & Gibson, T. J. (2004) · BMC Bioinformatics · doi:10.1186/1471-2105-5-79 · Cited by 351
Phosphorylation Analysis by Mass Spectrometry
Steen, H., Jebanathirajah, J. A., Rush, J., Morrice, N., & Kirschner, M. W. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500135-mcp200 · Cited by 349
Ten things you should know about protein kinases: IUPHAR R eview 14
Fabbro, D., Cowan‐Jacob, S. W., & Moebitz, H. (2015) · British Journal of Pharmacology · doi:10.1111/bph.13096 · Cited by 347
Chemically Fueled Self‐Assembly in Biology and Chemistry
Das, K., Gabrielli, L., & Prins, L. J. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202100274 · Cited by 336
Prabakaran, S., Lippens, G., Steen, H., & Gunawardena, J. (2012) · WIREs Systems Biology and Medicine · doi:10.1002/wsbm.1185 · Cited by 335
Illuminating the dark phosphoproteome
Needham, E. J., Parker, B. L., Burykin, T., James, D. E., & Humphrey, S. J. (2019) · Science Signaling · doi:10.1126/scisignal.aau8645 · Cited by 334
Tagliabracci, V. S., Engel, J. L., Wiley, S. E., Xiao, J., Gonzalez, D. J., Nidumanda Appaiah, H., Koller, A., Nizet, V., White, K. E., & Dixon, J. E. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402218111 · Cited by 327
Posttranslational mutagenesis: A chemical strategy for exploring protein side-chain diversity
Wright, T. H., Bower, B. J., Chalker, J. M., Bernardes, G. J. L., Wiewiora, R., Ng, W.-L., Raj, R., Faulkner, S., Vallée, M. R. J., Phanumartwiwath, A., et al. (2016) · Science · doi:10.1126/science.aag1465 · Cited by 317
Highly Sensitive and Multiplexed Protein Measurements
Cohen, L., & Walt, D. R. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00257 · Cited by 294
Ubiquitin signalling in DNA replication and repair
Ulrich, H. D., & Walden, H. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2921 · Cited by 275
Signalling scaffolds and local organization of cellular behaviour
Langeberg, L. K., & Scott, J. D. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3966 · Cited by 273
Structural basis of 14-3-3 protein functions
Obsil, T., & Obsilova, V. (2011) · Seminars in Cell & Developmental Biology · doi:10.1016/j.semcdb.2011.09.001 · Cited by 273
Will the Ubiquitin System Furnish as Many Drug Targets as Protein Kinases?
Cohen, P., & Tcherpakov, M. (2010) · Cell · doi:10.1016/j.cell.2010.11.016 · Cited by 271
Self-citationPhosphoprotein Analysis Using Antibodies Broadly Reactive against Phosphorylated Motifs
Zhang, H., Zha, X., Tan, Y., Hornbeck, P. V., Mastrangelo, A. J., Alessi, D. R., Polakiewicz, R. D., & Comb, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206399200 · Cited by 270
Evolution of protein phosphatases in plants and animals
Moorhead, G. B. G., De Wever, V., Templeton, G., & Kerk, D. (2009) · Biochemical Journal · doi:10.1042/bj20081986 · Cited by 254
Protein kinase inhibitors in the treatment of inflammatory and autoimmune diseases
Patterson, H., Nibbs, R., McInnes, I., & Siebert, S. (2014) · Clinical and Experimental Immunology · doi:10.1111/cei.12248 · Cited by 199
Mitochondrial dysfunction in Parkinson's disease
Schapira, A. H. V. (2007) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4402160 · Cited by 175
Complex molecular regulation of tyrosine hydroxylase
Tekin, I., Roskoski, R., Carkaci-Salli, N., & Vrana, K. E. (2014) · Journal of Neural Transmission · doi:10.1007/s00702-014-1238-7 · Cited by 128
Catch me if you can: Mass spectrometry‐based phosphoproteomics and quantification strategies
Eyrich, B., Sickmann, A., & Zahedi, R. P. (2011) · PROTEOMICS · doi:10.1002/pmic.201000489 · Cited by 104
Russell, C. L., Mitra, V., Hansson, K., Blennow, K., Gobom, J., Zetterberg, H., Hiltunen, M., Ward, M., & Pike, I. (2016) · Journal of Alzheimer's Disease · doi:10.3233/jad-160633 · Cited by 52
Kinact: a computational approach for predicting activating missense mutations in protein kinases
Rodrigues, C. H., Ascher, D. B., & Pires, D. E. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky375 · Cited by 31
Kinetic Mechanism and Inhibitor Characterization for c-jun-N-Terminal Kinase 3α1
Ember, B., Kamenecka, T., & LoGrasso, P. (2008) · Biochemistry · doi:10.1021/bi701852z · Cited by 22
Mou, S., Sun, L., & Dovichi, N. J. (2013) · Analytical Chemistry · doi:10.1021/ac402858a · Cited by 22
Photo Cross‐Linking Probes Containing ϵ‐ N ‐Thioacyllysine and ϵ‐ N ‐Acyl‐(δ‐aza)lysine Residues
Bæk, M., Martín‐Gago, P., Laursen, J. S., Madsen, J. L. H., Chakladar, S., & Olsen, C. A. (2020) · Chemistry – A European Journal · doi:10.1002/chem.201905338 · Cited by 16
Architecture and activation of human muscle phosphorylase kinase
Yang, X., Zhu, M., Lu, X., Wang, Y., & Xiao, J. (2024) · Nature Communications · doi:10.1038/s41467-024-47049-2 · Cited by 4
AlphaFold modeling of polyubiquitin complexes and covalently linked proteins
(2025) · doi:10.1016/j.xcrp.2025.102796 · Cited by 3
Coronaviruses spike glycoprotein endodomains: The sequence and structure‐based comprehensive study
Kumar, P., Bhardwaj, A., Mukherjee, B., Joshi, R., & Giri, R. (2023) · Protein Science · doi:10.1002/pro.4804 · Cited by 2
Metadata
- Authors
- Cohen, P.
- Venue
- Nature Cell Biology
- Published
- 2002-05
- Volume
- 4
- Issue
- 5
- Pages
- E127-E130
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2020459598
- Cited by
- 1,139
- References
- 3
- FWCI
- 6.70
- Type
- journal article
- Language
- en
- Open access
- closed
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