Mechanisms of specificity in protein phosphorylation

The PyMOL Molecular Graphics System

DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147 · see citing works

The protein kinase complement of the human genome

Manning, G., Whyte, D. B., Martinez, R., Hunter, T., & Sudarsanam, S. (2002) · Science · doi:10.1126/science.1075762 · Cited by 8,145 · see citing works

The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic Domains

Hanks, S. K., Quinn, A. M., & Hunter, T. R. (1988) · Science · doi:10.1126/science.3291115 · Cited by 5,040 · see citing works

Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks

Olsen, J. V., Blagoev, B., Gnad, F., Maček, B., Kumar, C., Mortensen, P., & Mann, M. (2006) · Cell · doi:10.1016/j.cell.2006.09.026 · Cited by 3,484 · see citing works

Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification.

Hanks, S. K., & Hunter, T. R. (1995) · PubMed · Cited by 2,518 · see citing works

The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification 1

Hanks, S. K., & Hunter, T. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.8.7768349 · Cited by 2,361 · see citing works

Transforming gene product of Rous sarcoma virus phosphorylates tyrosine

Hunter, T. R., & Sefton, B. M. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.3.1311 · Cited by 2,333 · see citing works

Signaling Through Scaffold, Anchoring, and Adaptor Proteins

Pawson, T., & Scott, J. D. (1997) · Science · doi:10.1126/science.278.5346.2075 · Cited by 2,256 · see citing works

Protein Tyrosine Phosphatases in the Human Genome

Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., & Mustelin, T. (2004) · Cell · doi:10.1016/j.cell.2004.05.018 · Cited by 1,886 · see citing works

Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

Knighton, D. R., Zheng, J., Eyck, L. F. T., Ashford, V. A., Xuong, N., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862342 · Cited by 1,764 · see citing works

Kinetic proofreading: a new mechanism for reducing errors in biosynthetic processes requiring high specificity

Hopfield, J. J. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.10.4135 · Cited by 1,594 · see citing works

Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex

Jeffrey, P. D., Russo, A. A., Polyák, K., Gibbs, E., Hurwitz, J., Massagué, J., & Pavletich, N. P. (1995) · Nature · doi:10.1038/376313a0 · Cited by 1,441 · see citing works

Transcription Factor ATF2 Regulation by the JNK Signal Transduction Pathway

Gupta, S., Campbell, D., Dérijard, B., & Davis, R. J. (1995) · Science · doi:10.1126/science.7824938 · Cited by 1,440 · see citing works

Three-dimensional structure of the tyrosine kinase c-Src

Xu, W., Harrison, S. C., & Eck, M. J. (1997) · Nature · doi:10.1038/385595a0 · Cited by 1,428 · see citing works

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 1,315 · see citing works

Protein Tyrosine Kinase Structure and Function

Hubbard, S. R., & Till, J. H. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.373 · Cited by 1,176 · see citing works

The regulation of protein function by multisite phosphorylation – a 25 year update

Cohen, P. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01712-6 · Cited by 1,138 · see citing works

AKAP signalling complexes: focal points in space and time

Wong, W., & Scott, J. D. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1527 · Cited by 1,073 · see citing works

Bmi-1 collaborates with c-Myc in tumorigenesis by inhibiting c-Myc-induced apoptosis via INK4a/ARFPreprint

Jacobs, J. J. L., Scheijen, B., Voncken, J. W., Kieboom, K., Berns, A. J. M., & van Lohuizen, M. (1999) · Genes & Development · doi:10.1101/gad.13.20.2678 · Cited by 1,060 · see citing works

[3] Protein kinase phosphorylation site sequences and consensus specificity motifs: Tabulations

Pearson, R. B., & Kemp, B. E. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)00127-i · Cited by 1,045 · see citing works

Evolution of protein kinase signaling from yeast to man

Manning, G., Plowman, G. D., Hunter, T. R., & Sudarsanam, S. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02179-5 · Cited by 986 · see citing works

Crystal structure of cyclin-dependent kinase 2

Bondt, H. L. D., Rosenblatt, J., Jancarik, J., Jones, H. D., Morgan, D. O., & Kim, S. (1993) · Nature · doi:10.1038/363595a0 · Cited by 980 · see citing works

Global analysis of protein phosphorylation in yeast

Ptacek, J., Devgan, G., Michaud, G. A., Zhu, H., Zhu, X., Fasolo, J., Guo, H., Jona, G., Breitkreutz, A., Sopko, R., et al. (2005) · Nature · doi:10.1038/nature04187 · Cited by 970 · see citing works

Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog

Hubbard, S. R. (1997) · The EMBO Journal · doi:10.1093/emboj/16.18.5572 · Cited by 954 · see citing works

Catalytic specificity of protein-tyrosine kinases is critical for selective signalling

Songyang, Z., Carraway, K. L., Eck, M. J., Harrison, S. C., Feldman, R. A., Mohammadi, M., Schlessinger, J., Hubbard, S. R., Smith, D. P., Eng, C., et al. (1995) · Nature · doi:10.1038/373536a0 · Cited by 919 · see citing works

Protein phosphatase 1 – targeted in many directions

Cohen, P. T. W. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.2.241 · Cited by 916 · see citing works

Targets of the cyclin-dependent kinase Cdk1

Ubersax, J. A., Woodbury, E. L., Quang, P. N., Paraz, M., Blethrow, J. D., Shah, K., Shokat, K. M., & Morgan, D. O. (2003) · Nature · doi:10.1038/nature02062 · Cited by 892 · see citing works

Crystal Structures of c-Src Reveal Features of Its Autoinhibitory Mechanism

Xu, W., Doshi, A. H., Lei, M., Eck, M. J., & Harrison, S. C. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80356-1 · Cited by 871 · see citing works

Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase.

Kemp, B. E., Graves, D. J., Benjamini, E., & Krebs, E. G. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40137-2 · Cited by 835 · see citing works

A conserved docking motif in MAP kinases common to substrates, activators and regulators

Tanoue, T., Adachi, M., Moriguchi, T., & Nishida, E. (2000) · Nature Cell Biology · doi:10.1038/35000065 · Cited by 816 · see citing works

Signaling Pathways for PC12 Cell Differentiation: Making the Right Connections

Vaudry, D., Stork, P. A., Lazarovici, P., & Eiden, L. E. (2002) · Science · doi:10.1126/science.1071552 · Cited by 795 · see citing works

Analysis of yeast protein kinases using protein chips

Zhu, H., Klemic, J. F., Chang, S., Bertone, P., Casamayor, A., Klemic, K. G., Smith, D. F., Gerstein, M., Reed, M. A., & Snyder, M. P. (2000) · Nature Genetics · doi:10.1038/81576 · Cited by 791 · see citing works

The Molecular Basis for Phosphodependent Substrate Targeting and Regulation of Plks by the Polo-Box Domain

Elia, A. E. H., Rellos, P., Haire, L. F., Chao, J. W., Ivins, F. J., Hoepker, K., Mohammad, D. H., Cantley, L. C., Smerdon, S. J., & Yaffe, M. B. (2003) · Cell · doi:10.1016/s0092-8674(03)00725-6 · Cited by 767 · see citing works

Structural and Evolutionary Relationships among Protein Tyrosine Phosphatase Domains

Andersen, J. N., Mortensen, O. H., Peters, G. H. J., Drake, P. G., Iversen, L. F., Olsen, O. H., Jansen, P. G., Andersen, H. S., Tonks, N. K., & Møller, N. P. H. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.21.7117-7136.2001 · Cited by 707 · see citing works

A Common Phosphate Binding Site Explains the Unique Substrate Specificity of GSK3 and Its Inactivation by Phosphorylation

Frame, S., Cohen, P., & Biondi, R. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00253-2 · Cited by 703 · see citing works

Proteomic Screen Finds pSer/pThr-Binding Domain Localizing Plk1 to Mitotic Substrates

Elia, A. E. H., Cantley, L. C., & Yaffe, M. B. (2003) · Science · doi:10.1126/science.1079079 · Cited by 688 · see citing works

Crystal Structure of Glycogen Synthase Kinase 3β

Dajani, R., Fraser, E., Roe, S. M., Young, N., Good, V. M., Dale, T. C., & Pearl, L. H. (2001) · Cell · doi:10.1016/s0092-8674(01)00374-9 · Cited by 678 · see citing works

Use of an oriented peptide library to determine the optimal substrates of protein kinases

Songyang, Z., Blechner, S., Hoagland, N., Hoekstra, M. F., Piwnica-Worms, H. M., & Cantley, L. C. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00221-9 · Cited by 654 · see citing works

A Mammalian Scaffold Complex That Selectively Mediates MAP Kinase Activation

Whitmarsh, A. J., Cavanagh, J., Tournier, C., Yasuda, J., & Davis, R. J. (1998) · Science · doi:10.1126/science.281.5383.1671 · Cited by 652 · see citing works

JNK2 contains a specificity-determining region responsible for efficient c-Jun binding and phosphorylation.

Kallunki, T., Su, B., Tsigelny, I., Sluss, H. K., Dérijard, B., Moore, G., Davis, R., & Karin, M. (1994) · Genes & Development · doi:10.1101/gad.8.24.2996 · Cited by 642 · see citing works

Kinetic and Catalytic Mechanisms of Protein Kinases

Adams, J. A. (2001) · Chemical Reviews · doi:10.1021/cr000230w · Cited by 630 · see citing works

Association of Protein Kinase A and Protein Phosphatase 2B with a Common Anchoring Protein

Coghlan, V. M., Perrino, B. A., Howard, M. L., Langeberg, L. K., Hicks, J. B., Gallatin, W. M., & Scott, J. D. (1995) · Science · doi:10.1126/science.7528941 · Cited by 617 · see citing works

Active cyclin B1–Cdk1 first appears on centrosomes in prophase

Jackman, M. R., Lindon, C., Nigg, E. A., & Pines, J. (2003) · Nature Cell Biology · doi:10.1038/ncb918 · Cited by 614 · see citing works

Atomic structure of the MAP kinase ERK2 at 2.3 A resolution

Zhang, F., Strand, A., Robbins, D., Cobb, M. H., & Goldsmith, E. J. (1994) · Nature · doi:10.1038/367704a0 · Cited by 592 · see citing works

Structural Basis for Phosphotyrosine Peptide Recognition by Protein Tyrosine Phosphatase 1B

Jia, Z., Barford, D., Flint, A. J., & Tonks, N. K. (1995) · Science · doi:10.1126/science.7540771 · Cited by 583 · see citing works

Coordination of Three Signaling Enzymes by AKAP79, a Mammalian Scaffold Protein

Klauck, T. M., Faux, M. C., Labudda, K., Langeberg, L. K., Jaken, S., & Scott, J. D. (1996) · Science · doi:10.1126/science.271.5255.1589 · Cited by 550 · see citing works

A Structural Basis for Substrate Specificities of Protein Ser/Thr Kinases: Primary Sequence Preference of Casein Kinases I and II, NIMA, Phosphorylase Kinase, Calmodulin-Dependent Kinase II, CDK5, and Erk1

Songyang, Z., Lu, K. P., Kwon, Y. T., Tsai, L., Filhol, O., Cochet, C., Brickey, D. A., Soderling, T. R., Bartleson, C., Graves, D. J., et al. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.11.6486 · Cited by 550 · see citing works

The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases

Brown, N. R., Noble, M. E. M., Endicott, J., & Johnson, L. N. (1999) · Nature Cell Biology · doi:10.1038/15674 · Cited by 546 · see citing works

A motif-based profile scanning approach for genome-wide prediction of signaling pathways

Yaffe, M. B., Leparc, G. G., Lai, J., Obata, T., Volinia, S., & Cantley, L. C. (2001) · Nature Biotechnology · doi:10.1038/86737 · Cited by 517 · see citing works

mAKAP assembles a protein kinase A/PDE4 phosphodiesterase cAMP signaling module

Dodge‐Kafka, K. L., Khouangsathiene, S., Kapiloff, M. S., Mouton, R., Hill, E. V., Houslay, M. D., Langeberg, L. K., & Scott, J. D. (2001) · The EMBO Journal · doi:10.1093/emboj/20.8.1921 · Cited by 507 · see citing works

Identification of intracellular receptor proteins for activated protein kinase C.

Mochly‐Rosen, D., Khaner, H., & Lopez, J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.9.3997 · Cited by 500 · see citing works

ATF‐2 contains a phosphorylation‐dependent transcriptional activation domain.

Livingstone, C., Patel, G., & Jones, N. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07167.x · Cited by 494 · see citing works

How do protein kinases recognize their substrates?

Pinna, L. A., & Ruzzene, M. (1996) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(96)00083-3 · Cited by 471 · see citing works

The JIP Group of Mitogen-Activated Protein Kinase Scaffold Proteins

Yasuda, J., Whitmarsh, A. J., Cavanagh, J., Sharma, M., & Davis, R. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.10.7245 · Cited by 458 · see citing works

Domains, Motifs, and Scaffolds: The Role of Modular Interactions in the Evolution and Wiring of Cell Signaling Circuits

Bhattacharyya, R. P., Reményi, A., Yeh, B. J., & Lim, W. A. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142710 · Cited by 449 · see citing works

Docking domains and substrate-specificity determination for MAP kinases

Sharrocks, A. D., Yang, S.-H., & Galanis, A. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01627-3 · Cited by 442 · see citing works

Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase

Jacobs, D., Glossip, D., Xing, H., Muslin, A. J., & Kornfeld, K. (1999) · Genes & Development · doi:10.1101/gad.13.2.163 · Cited by 439 · see citing works

Structure of GSK3beta reveals a primed phosphorylation mechanism.

ter Haar, E., Coll, J. T., Austen, D. A., Hsiao, H.-M., Swenson, L. L., & Jain, J. (2001) · Nature Structural Biology · doi:10.1038/89624 · Cited by 394 · see citing works

Phosphotransferase and substrate binding mechanism of the cAMP‐dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5‐24).

Bossemeyer, D., Engh, R. A., Kinzel, V., Ponstingl, H., & Huber, R. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05725.x · Cited by 389 · see citing works

Peptide and Protein Library Screening Defines Optimal Substrate Motifs for AKT/PKB

Obata, T., Yaffe, M. B., Leparc, G., Piro, E. T., Maegawa, H., Kashiwagi, A., Kikkawa, R., & Cantley, L. C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005497200 · Cited by 388 · see citing works

2.2 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor

Zheng, J., Trafny, E. A., Knighton, D. R., Xuong, N., Taylor, S. S., Eyck, L. F. T., & Sowadski, J. M. (1993) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444993000423 · Cited by 374 · see citing works

Identification of a Cyclin-cdk2 Recognition Motif Present in Substrates and p21-Like Cyclin-Dependent Kinase Inhibitors

Adams, P. D., Sellers, W. R., Sharma, S. K., Wu, A. D., Nalin, C. M., & Kaelin, W. G. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.12.6623 · Cited by 373 · see citing works

Substrate recruitment to cyclin-dependent kinase 2 by a multipurpose docking site on cyclin A

Schulman, B. A., Lindstrom, D. L., & Harlow, E. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10453 · Cited by 372 · see citing works

Formation of protein kinase recognition sites by covalent modification of the substrate. Molecular mechanism for the synergistic action of casein kinase II and glycogen synthase kinase 3.

Fiol, C. J., Mahrenholz, A. M., Wang, Y., Roeske, R. W., & Roach, P. J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47901-x · Cited by 367 · see citing works

Emerging roles of nuclear protein phosphatases

Moorhead, G. B. G., Trinkle‐Mulcahy, L., & Ulke‐Lemée, A. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2126 · Cited by 365 · see citing works

Determinants of specificity in TGF-β signal transductionPreprint

Chen, Y., Hata, A., Lo, R. S., Wotton, D., Shi, Y., Pavletich, N. P., & Massagué, J. (1998) · Genes & Development · doi:10.1101/gad.12.14.2144 · Cited by 361 · see citing works

A rapid method for determining protein kinase phosphorylation specificity

Hutti, J. E., Jarrell, E. T., Chang, J. D., Abbott, D. W., Störz, P., Toker, A., Cantley, L. C., & Turk, B. E. (2004) · Nature Methods · doi:10.1038/nmeth708 · Cited by 356 · see citing works

Rewiring MAP Kinase Pathways Using Alternative Scaffold Assembly Mechanisms

Park, S.-H., Zarrinpar, A., & Lim, W. A. (2003) · Science · doi:10.1126/science.1076979 · Cited by 355 · see citing works

Cyclin specificity in the phosphorylation of cyclin-dependent kinase substrates

Loog, M., & Morgan, D. O. (2005) · Nature · doi:10.1038/nature03329 · Cited by 354 · see citing works

Mechanistic Studies of the Dual Phosphorylation of Mitogen-activated Protein Kinase

Ferrell, J. E., & Bhatt, R. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.19008 · Cited by 344 · see citing works

Phosphate groups as substrate determinants for casein kinase I action.

Flotow, H., Graves, P. R., Wang, A. Q., Fiol, C. J., Roeske, R. W., & Roach, P. J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77295-5 · Cited by 337 · see citing works

Localization of Protein Kinase C Isozymes in Cardiac Myocytes

Disatnik, M., Buraggi, G., & Mochly‐Rosen, D. (1994) · Experimental Cell Research · doi:10.1006/excr.1994.1041 · Cited by 335 · see citing works

Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions

BIONDI, R. M., & NEBREDA, A. R. (2003) · Biochemical Journal · doi:10.1042/bj20021641 · Cited by 334 · see citing works

A phosphoserine‐regulated docking site in the protein kinase RSK2 that recruits and activates PDK1

Frödin, M., Jensen, C. J., Mérienne, K., & Gammeltoft, S. (2000) · The EMBO Journal · doi:10.1093/emboj/19.12.2924 · Cited by 317 · see citing works

A constitutively active and nuclear form of the MAP kinase ERK2 is sufficient for neurite outgrowth and cell transformation

Robinson, M. J., Stippec, S. A., Goldsmith, E. J., White, M. A., & Cobb, M. H. (1998) · Current Biology · doi:10.1016/s0960-9822(07)00485-x · Cited by 311 · see citing works

The mouse kinome: Discovery and comparative genomics of all mouse protein kinases

Caenepeel, S. R., Charydczak, G., Sudarsanam, S., Hunter, T. R., & Manning, G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0306880101 · Cited by 308 · see citing works

Crystal Structures of MAP Kinase p38 Complexed to the Docking Sites on Its Nuclear Substrate MEF2A and Activator MKK3b

Chang, C.-I., Xu, B.-E., Akella, R., Cobb, M. H., & Goldsmith, E. J. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00525-7 · Cited by 302 · see citing works

Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C‐terminal residues of PKA

Biondi, R. M., Cheung, P., Casamayor, A., Deák, M., Currie, R. A., & Alessi, D. R. (2000) · The EMBO Journal · doi:10.1093/emboj/19.5.979 · Cited by 301 · see citing works

Docking Motif Interactions in MAP Kinases Revealed by Hydrogen Exchange Mass Spectrometry

Lee, T., Hoofnagle, A. N., Kabuyama, Y., Stroud, J., Min, X., Goldsmith, E. J., Chen, L., Resing, K. A., & Ahn, N. G. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00161-3 · Cited by 282 · see citing works

The Ste5 Scaffold Allosterically Modulates Signaling Output of the Yeast Mating Pathway

Bhattacharyya, R. P., Reményi, A., Good, M. C., Bashor, C. J., Falick, A. M., & Lim, W. A. (2006) · Science · doi:10.1126/science.1120941 · Cited by 276 · see citing works

Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125

Heo, Y., Kim, S., Seo, C. I., Kim, Y. K., Sung, B., Lee, H. S., Lee, J. I., Park, S., Kim, J. H., Hwang, K. Y., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600212 · Cited by 275 · cited 1× · see citing works

Translocation of cyclin B1 to the nucleus at prophase requires a phosphorylation-dependent nuclear import signal

Hagting, A., Jackman, M. R., Simpson, K., et al. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80308-x · Cited by 275 · see citing works

The biological functions of A-kinase anchor proteins1 1Edited by P. E. Wright

Feliciello, A., Gottesman, M. E., & Avvedimento, E. V. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4585 · Cited by 274 · see citing works

The L3 loop: a structural motif determining specific interactions between SMAD proteins and TGF‐β receptors

Lo, R. S., Chen, Y., Shi, Y., Pavletich, N. P., & Massagué, J. (1998) · The EMBO Journal · doi:10.1093/emboj/17.4.996 · Cited by 266 · see citing works

Human cyclins B1 and B2 are localized to strikingly different structures: B1 to microtubules, B2 primarily to the Golgi apparatus.

Jackman, M. R., Firth, M., & Pines, J. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07153.x · Cited by 263 · see citing works

The Elk-1 ETS-Domain Transcription Factor Contains a Mitogen-Activated Protein Kinase Targeting Motif

Yang, S., Yates, P. R., Whitmarsh, A. J., Davis, R. J., & Sharrocks, A. D. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.2.710 · Cited by 255 · see citing works

Dynamics of signaling by PKA

Taylor, S. S., Kim, C., Vigil, D., Haste, N. M., Yang, J., Wu, J., & Anand, G. S. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.08.024 · Cited by 249 · see citing works

Targeting of p38 Mitogen-Activated Protein Kinases to MEF2 Transcription Factors

Yang, S.-H., Galanis, A., & Sharrocks, A. D. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4028 · Cited by 244 · see citing works

Principles of MAP Kinase Signaling Specificity inSaccharomyces cerevisiae

Schwartz, M. A., & Madhani, H. D. (2004) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.073003.112634 · Cited by 239 · see citing works

ERK2 Mitogen-activated Protein Kinase Binding, Phosphorylation, and Regulation of the PDE4D cAMP-specific Phosphodiesterases

MacKenzie, S. J., Baillie, G. S., McPhee, I., Bolger, G. B., & Houslay, M. D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.22.16609 · Cited by 237 · see citing works

Crystal Structure and Mutational Analysis of the Human CDK2 Kinase Complex with Cell Cycle–Regulatory Protein CksHs1

Bourne, Y., Watson, M. H., Hickey, M. J., Holmes, W., Rocque, W. J., Reed, S. I., & Tainer, J. A. (1996) · Cell · doi:10.1016/s0092-8674(00)81065-x · Cited by 236 · see citing works

More on target with protein phosphorylation: conferring specificity by location.

Faux, M. C., & Scott, J. D. (1996) · PubMed · Cited by 229 · see citing works

Substrate Competition as a Source of Ultrasensitivity in the Inactivation of Wee1

Kim, S. Y., & Ferrell, J. E. (2007) · Cell · doi:10.1016/j.cell.2007.01.039 · Cited by 220 · see citing works

High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site

Biondi, R. M., Komander, D., Thomas, C. C., Lizcano, J. M., Deak, M., Alessi, D. R., & van Aalten, D. M. F. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf437 · Cited by 203 · see citing works

The crystal structure of a phosphorylase kinase peptide substrate complex: kinase substrate recognition

Lowe, E. D., Noble, M. E. M., Skamnaki, V. T., Oikonomakos, N. G., Owen, D. J., & Johnson, L. N. (1997) · The EMBO Journal · doi:10.1093/emboj/16.22.6646 · Cited by 200 · see citing works

Substrate specificity of the cyclic AMP-dependent protein kinase.

Kemp, B. E., Bylund, D., Huang, T., & Krebs, E. G. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.9.3448 · Cited by 198 · see citing works

Docking interactions in protein kinase and phosphatase networks

Reményi, A., Good, M. C., & Lim, W. A. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.10.008 · Cited by 188 · see citing works

Spatial gradients of cellular phospho‐proteins

Brown, G. C., & Kholodenko, B. Ν. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01058-3 · Cited by 186 · see citing works

Synthetic peptide substrates for a tyrosine protein kinase.

Hunter, T. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34602-7 · Cited by 183 · see citing works

Specificity of MAP Kinase Signaling in Yeast Differentiation Involves Transient versus Sustained MAPK Activation

Sabbagh, W., Flatauer, L. J., Bardwell, A. J., & Bardwell, L. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00322-7 · Cited by 182 · see citing works

Signaling in the Yeast Pheromone Response Pathway: Specific and High-Affinity Interaction of the Mitogen-Activated Protein (MAP) Kinases Kss1 and Fus3 with the Upstream MAP Kinase Kinase Ste7

Bardwell, L., Cook, J. G., Chang, E. C., Cairns, B. R., & Thorner, J. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.7.3637 · Cited by 161 · see citing works

Cross-talk and decision making in MAP kinase pathways

McClean, M. N., Mody, A., Broach, J. R., & Ramanathan, S. (2007) · Nature Genetics · doi:10.1038/ng1957 · Cited by 159 · see citing works

Ordered multisite protein phosphorylation. Analysis of glycogen synthase kinase 3 action using model peptide substrates.

Fiol, C. J., Wang, A. Q., Roeske, R. W., & Roach, P. J. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)39291-9 · Cited by 158 · see citing works

The Role of Docking Interactions in Mediating Signaling Input, Output, and Discrimination in the Yeast MAPK Network

Reményi, A., Good, M. C., Bhattacharyya, R. P., & Lim, W. A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.10.030 · Cited by 154 · see citing works

The structure of the cell cycle protein Cdc14 reveals a proline‐directed protein phosphatase

Gray, C. H., Good, V. M., Tonks, N. K., et al. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg348 · Cited by 151 · see citing works

Pheromone-Dependent Destruction of the Tec1 Transcription Factor Is Required for MAP Kinase Signaling Specificity in Yeast

Bao, M. Z., Schwartz, M. A., Cantin, G. T., Yates, J. R., & Madhani, H. D. (2004) · Cell · doi:10.1016/j.cell.2004.11.052 · Cited by 148 · see citing works

Fus3-Regulated Tec1 Degradation through SCFCdc4 Determines MAPK Signaling Specificity during Mating in Yeast

Chou, S., Huang, L., & Liu, H. (2004) · Cell · doi:10.1016/j.cell.2004.11.053 · Cited by 147 · see citing works

Interaction of the S-phase cyclin Clb5 with an 'RXL' docking sequence in the initiator protein Orc6 provides an origin-localized replication control switchPreprint

Wilmes, G. M., Archambault, V., Austin, R. J., et al. (2004) · Genes & Development · doi:10.1101/gad.1202304 · Cited by 146 · see citing works

Xe-p9, a Xenopus Suc1/Cks protein, is essential for the Cdc2-dependent phosphorylation of the anaphase- promoting complex at mitosisPreprint

Patra, D., & Dunphy, W. G. (1998) · Genes & Development · doi:10.1101/gad.12.16.2549 · Cited by 145 · see citing works

MAP kinase dynamics in response to pheromones in budding yeast

van Drogen, F., Stucke, V. M., Jorritsma, G., & Peter, M. (2001) · Nature Cell Biology · doi:10.1038/ncb1201-1051 · Cited by 143 · see citing works

The Localization of Human Cyclins B1 and B2 Determines Cdk1 Substrate Specificity and Neither Enzyme Requires Mek to Disassemble the Golgi Apparatus

Draviam, V. M., Orrechia, S., Lowe, M., Pardi, R., & Pines, J. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.5.945 · Cited by 143 · see citing works

Multisite Phosphorylation and the Countdown to S Phase

Deshaies, R. J., & Ferrell, J. E. (2001) · Cell · doi:10.1016/s0092-8674(01)00620-1 · Cited by 136 · see citing works

Comprehensive analysis of amino acid and nucleotide composition in eukaryotic genomes, comparing genes and pseudogenes

Echols, N. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.11.2515 · Cited by 135 · see citing works

Unmasking the S-Phase-Promoting Potential of Cyclin B1

Moore, J. D., Kirk, J. A., & Hunt, T. (2003) · Science · doi:10.1126/science.1081418 · Cited by 132 · see citing works

A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAPKs

Bardwell, L., & Thorner, J. W. (1996) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(96)30032-7 · Cited by 127 · see citing works

Protein modification: Docking sites for kinases

Holland, P. M., & Cooper, J. A. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80205-x · Cited by 125 · see citing works

A Bipartite Substrate Recognition Motif for Cyclin-dependent Kinases

Takeda, D. Y., Wohlschlegel, J. A., & Dutta, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m005719200 · Cited by 124 · see citing works

Spatially Separate Docking Sites on ERK2 Regulate Distinct Signaling Events In Vivo

Dimitri, C. A., Dowdle, W., MacKeigan, J. P., Blenis, J., & Murphy, L. O. (2005) · Current Biology · doi:10.1016/j.cub.2005.06.037 · Cited by 114 · see citing works

The JNK-interacting Protein-1 Scaffold Protein Targets MAPK Phosphatase-7 to Dephosphorylate JNK

Willoughby, E. A., Perkins, G. R., Collins, M. K., & Whitmarsh, A. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207324200 · Cited by 109 · see citing works

Gain-of-Function Mutations in the Caenorhabditis elegans lin-1 ETS Gene Identify a C-Terminal Regulatory Domain Phosphorylated by ERK MAP Kinase

Jacobs, D., Beitel, G. J., Clark, S. G., Horvitz, H. R., & Kornfeld, K. (1998) · Genetics · doi:10.1093/genetics/149.4.1809 · Cited by 109 · see citing works

Cyclin specificity: how many wheels do you need on a unicycle?

Miller, M. E., & Cross, F. R. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.10.1811 · Cited by 106 · see citing works

MAPK specificity in the yeast pheromone response independent of transcriptional activation

Breitkreutz, A., Boucher, L., & Tyers, M. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00370-0 · Cited by 106 · see citing works

The Cdk-associated protein Cks1 functions both in G1 and G2 in Saccharomyces cerevisiae.Preprint

Tang, Y., & Reed, S. I. (1993) · Genes & Development · doi:10.1101/gad.7.5.822 · Cited by 102 · see citing works

Specialization and Targeting of B-Type Cyclins

Cross, F. R., Yuste-Rojas, M., Gray, S., et al. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80183-5 · Cited by 101 · see citing works

Synthetic substrate for cyclic AMP-dependent protein kinase

Daile, P., CARNEGIE, P. R., & YOUNG, J. D. (1975) · Nature · doi:10.1038/257416a0 · Cited by 97 · see citing works

Targeting of PKA, PKC and protein phosphatases to cellular microdomains

Sim, A. T. R., & Scott, J. D. (1999) · Cell Calcium · doi:10.1054/ceca.1999.0072 · Cited by 96 · see citing works

A conserved motif at the amino termini of MEKs might mediate high-affinity interaction with the cognate MAPKs

Bardwell, L. (1996) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(96)30032-7 · Cited by 95 · see citing works

The Role of the Phospho-CDK2/Cyclin A Recruitment Site in Substrate Recognition

Cheng, K. Y., Noble, M. E. M., Skamnaki, V., Brown, N. R., Lowe, E. D., Kontogiannis, L., Shen, K., Cole, P. A., Siligardi, G., & Johnson, L. N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600480200 · Cited by 93 · see citing works

Redirecting tyrosine kinase signaling to an apoptotic caspase pathway through chimeric adaptor proteins

Howard, P. L., Chia, M. C., Rizzo, S. D., Liu, F., & Pawson, T. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1934711100 · Cited by 92 · see citing works

Identification of B-KSR1, a Novel Brain-Specific Isoform of KSR1 That Functions in Neuronal Signaling

Müller, J., Cacace, A. M., Lyons, W. E., McGill, C. B., & Morrison, D. K. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.15.5529-5539.2000 · Cited by 89 · see citing works

Purification and characterization of a protein-tyrosine kinase encoded by the Abelson murine leukemia virus.

Foulkes, J. G., Chow, M., Gorka, C., et al. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39565-0 · Cited by 88 · see citing works

Structural Basis for Substrate Specificity of Protein-tyrosine Phosphatase SHP-1

Yang, J. P., Cheng, Z., Niu, T., Liang, X., Zhao, Z. J., & Zhou, G. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.6.4066 · Cited by 83 · see citing works

Phosphorylated synthetic peptides as tools for studying protein phosphatases

Pinna, L. A., & Donella‐Deana, A. (1994) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/0167-4889(94)90050-7 · Cited by 82 · see citing works

Networks for the allosteric control of protein kinases

Shi, Z., Resing, K. A., & Ahn, N. G. (2006) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2006.10.011 · Cited by 78 · see citing works

The Role of Proofreading in Signal Transduction Specificity

Swain, P. S., & Siggia, E. D. (2002) · Biophysical Journal · doi:10.1016/s0006-3495(02)75633-6 · Cited by 78 · see citing works

Crystal Structure of the Human Cell Cycle Protein CksHs1: Single Domain Fold with Similarity to Kinase N-lobe Domain

Arvai, A. S., Bourne, Y., Hickey, M. J., & Tainer, J. A. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0341 · Cited by 72 · see citing works

2.0 Å refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with a peptide inhibitor and detergent

Knighton, D. R., Bell, S. M., Zheng, J., et al. (1993) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444993000502 · Cited by 72 · see citing works

Genetic analysis of the kinome and phosphatome in cancer

Arena, S., Benvenuti, S., & Bardelli, A. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5205-1 · Cited by 70 · see citing works

Characterization of the proto-oncogene Pim-1: Kinase activity and substrate recognition sequence

Friedmann, M., Nissen, M. S., Hoover, D. S., Reeves, R., & Magnuson, N. S. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90454-5 · Cited by 69 · see citing works

Dynamic Interaction between the Dual Specificity Phosphatase MKP7 and theJNK3 Scaffold Protein β-Arrestin2

Willoughby, E. A., & Collins, M. K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501926200 · Cited by 64 · see citing works

Distinct Subcellular Localization Patterns Contribute to Functional Specificity of the Cln2 and Cln3 Cyclins of Saccharomyces cerevisiae

Miller, M. E., & Cross, F. R. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.2.542-555.2000 · Cited by 63 · see citing works

PDZ-containing proteins: alternative splicing as a source of functional diversity

Sierralta, J. A., & Mendoza, C. (2004) · Brain Research Reviews · doi:10.1016/j.brainresrev.2004.06.002 · Cited by 46 · see citing works

Two-Faced Cyclins with Eyes on the Targets

Archambault, V., Buchler, N. E. G., Wilmes, G. M., et al. (2004) · Cell Cycle · doi:10.4161/cc.4.1.1402 · Cited by 37 · see citing works

Engineering the Substrate Specificity of the Abl Tyrosine Kinase

Till, J. H., Chan, P. M., & Miller, W. T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.8.4995 · Cited by 33 · see citing works

The role of Thr160 phosphorylation of Cdk2 in substrate recognition

Holmes, J. K., & Solomon, M. J. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02392.x · Cited by 29 · see citing works

Phosphorylated seryl and threonyl, but not tyrosyl, residues are efficient specificity determinants for GSK‐3β and Shaggy

Williams, D. D., Marin, O., Pinna, L. A., & Proud, C. G. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00342-7 · Cited by 20 · see citing works

Proteomics by Mass Spectrometry: Approaches, Advances, and Applications

Yates, J. R., Ruse, C. I., & Nakorchevsky, A. (2009) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-061008-124934 · Cited by 1,078 · see citing works

Integrated Proteogenomic Characterization of Clear Cell Renal Cell Carcinoma

Clark, D. J., Dhanasekaran, S. M., Petralia, F., Pan, J., Song, X., Hu, Y., da Veiga Leprevost, F., Reva, B., Lih, T.-S. M., Chang, H.-Y., et al. (2019) · Cell · doi:10.1016/j.cell.2019.10.007 · Cited by 730 · see citing works

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 · see citing works

Tau and tauopathies

Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609 · see citing works

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle

Daub, H., Olsen, J. V., Bairlein, M., Gnad, F., Oppermann, F. S., Körner, R., Greff, Z., Kéri, G., Stemmann, O., & Mann, M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.007 · Cited by 594 · see citing works

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442 · see citing works

Formation of stable attachments between kinetochores and microtubules depends on the B56-PP2A phosphatase

Foley, E. A., Maldonado, M., & Kapoor, T. M. (2011) · Nature Cell Biology · doi:10.1038/ncb2327 · Cited by 267 · see citing works

ERK1/2 Phosphorylate Raptor to Promote Ras-dependent Activation of mTOR Complex 1 (mTORC1)

Carriere, A., Romeo, Y., Acosta-Jaquez, H. A., Moreau, J., Bonneil, E., Thibault, P., Fingar, D. C., & Roux, P. P. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.159046 · Cited by 268 · see citing works

The GAIT system: a gatekeeper of inflammatory gene expression

Mukhopadhyay, R., Jia, J., Arif, A., Ray, P. S., & Fox, P. L. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.03.004 · Cited by 216 · see citing works

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 · see citing works

Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove

Garai, Á., Zeke, A., Gógl, G., Törő, I., Fördős, F., Blankenburg, H., Bárkai, T., Varga, J., Alexa, A., Emig, D., et al. (2012) · Science Signaling · doi:10.1126/scisignal.2003004 · Cited by 177 · see citing works

Arsenic targets Pin1 and cooperates with retinoic acid to inhibit cancer-driving pathways and tumor-initiating cells

Kozono, S., Lin, Y.-M., Seo, H.-S., Pinch, B., Lian, X., Qiu, C., Herbert, M. K., Chen, C.-H., Tan, L., Gao, Z. J., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05402-2 · Cited by 168 · see citing works

Diverse Regulation of the CreA Carbon Catabolite Repressor in <i>Aspergillus nidulans</i>

Ries, L. N. A., Beattie, S. R., Espeso, E. A., Cramer, R. A., & Goldman, G. H. (2016) · Genetics · doi:10.1534/genetics.116.187872 · Cited by 162 · see citing works

Mechanisms of site‐specific dephosphorylation and kinase opposition imposed by PP2A regulatory subunits

Kruse, T., Gnosa, S. P., Nasa, I., Garvanska, D. H., Hein, J. B., Nguyen, H., Samsøe‐Petersen, J., Lopez‐Mendez, B., Hertz, E. P. T., Schwarz, J., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019103695 · Cited by 97 · see citing works

Ion Activation Methods for Peptides and Proteins

Macias, L. A., Santos, I. C., & Brodbelt, J. S. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b04859 · Cited by 107 · see citing works

In Vivo Phosphorylation Site Mapping and Functional Characterization of Arabidopsis Phototropin 1

Sullivan, S., Thomson, C. E., Lamont, D. J., Jones, M. A., & Christie, J. M. (2008) · Molecular Plant · doi:10.1093/mp/ssm017 · Cited by 107 · see citing works

PP2A-B′ holoenzyme substrate recognition, regulation and role in cytokinesis

Wu, C.-G., Chen, H., Guo, F., Yadav, V. K., Mcilwain, S. J., Rowse, M., Choudhary, A., Lin, Z., Li, Y., Gu, T., et al. (2017) · Cell Discovery · doi:10.1038/celldisc.2017.27 · Cited by 85 · see citing works

Theoretical and experimental analysis links isoform-specific ERK signalling to cell fate decisions

Schilling, M., Maiwald, T., Hengl, S., Winter, D., Kreutz, C., Kolch, W., Lehmann, W. D., Timmer, J., & Klingmüller, U. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.91 · Cited by 79 · see citing works

Clinical protein science in translational medicine targeting malignant melanoma

Gil, J., Betancourt, L. H., Pla, I., Sanchez, A., Appelqvist, R., Miliotis, T., Kuras, M., Oskolas, H., Kim, Y., Horvath, Z., et al. (2019) · Cell Biology and Toxicology · doi:10.1007/s10565-019-09468-6 · Cited by 45 · see citing works

Capillary Zone Electrophoresis–Tandem Mass Spectrometry for Large-Scale Phosphoproteomics with the Production of over 11,000 Phosphopeptides from the Colon Carcinoma HCT116 Cell Line

Chen, D., Ludwig, K. R., Krokhin, O. V., Spicer, V., Yang, Z., Shen, X., Hummon, A. B., & Sun, L. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b04770 · Cited by 34 · see citing works

Biophysical Evidence for Intrinsic Disorder in the C-terminal Tails of the Epidermal Growth Factor Receptor (EGFR) and HER3 Receptor Tyrosine Kinases

Keppel, T. R., Sarpong, K., Murray, E. M., Monsey, J., Zhu, J., & Bose, R. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.747485 · Cited by 29 · see citing works

Presence and utility of intrinsically disordered regions in kinases

Kathiriya, J. J., Pathak, R. R., Clayman, E., Xue, B., Uversky, V. N., & Davé, V. (2014) · Molecular BioSystems · doi:10.1039/c4mb00224e · Cited by 30 · see citing works

Single-Shot Capillary Zone Electrophoresis–Tandem Mass Spectrometry Produces over 4400 Phosphopeptide Identifications from a 220 ng Sample

Zhang, Z., Hebert, A. S., Westphall, M. S., Coon, J. J., & Dovichi, N. J. (2019) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00244 · Cited by 22 · see citing works

Targeted protein modification as a paradigm shift in drug discovery

Amirian, R., Azadi Badrbani, M., Izadi, Z., Samadian, H., Bahrami, G., Sarvari, S., Abdolmaleki, S., Nabavi, S. M., Derakhshankhah, H., & Jaymand, M. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115765 · Cited by 18 · see citing works

Evolutionary crossroads of cell signaling: PP1 and PP2A substrate sites in intrinsically disordered regions

Hoermann, B., & Köhn, M. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200175 · Cited by 14 · see citing works

Repeated nicotine exposure increases the intracellular interaction between ERK‐mGluR5 in the nucleus accumbens more in adult than adolescent rats

Yang, J. H., Sohn, S., Kim, S., Kim, J., Oh, J. H., Ryu, I. S., Go, B. S., & Choe, E. S. (2021) · Addiction Biology · doi:10.1111/adb.12913 · Cited by 14 · see citing works

Serum/glucocorticoid regulated kinase 1 (SGK1) in neurological disorders: pain or gain

Howard, P. G., Zou, P., Zhang, Y., Huang, F., Tesic, V., Wu, C. Y.-C., & Lee, R. H.-C. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114973 · Cited by 13 · see citing works

KSR--A Regulator and Scaffold Protein of the MAPK Pathway

Raabe, T., & Rapp, U. R. (2002) · Science s STKE · doi:10.1126/stke.2002.136.pe28 · Cited by 29 · see citing works

KSR--A Regulator and Scaffold Protein of the MAPK Pathway

Raabe, T., & Rapp, U. R. (2002) · Science Signaling · doi:10.1126/scisignal.1362002pe28 · Cited by 5 · see citing works

Signaling Through Scaffold, Anchoring, and Adaptor Proteins

Pawson, T., & Scott, J. D. (1997) · Science · doi:10.1126/science.278.5346.2075 · Cited by 2,256 · see citing works

Localization of the MP1-MAPK Scaffold Complex to Endosomes Is Mediated by p14 and Required for Signal Transduction

Teis, D., Wunderlich, W., & Huber, L. A. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00364-7 · Cited by 371 · see citing works

Crystal structure of the p14/MP1 scaffolding complex: How a twin couple attaches mitogen-activated protein kinase signaling to late endosomes

Kurzbauer, R., Teis, D., de Araujo, M. E. G., Maurer-Stroh, S., Eisenhaber, F., Bourenkov, G. P., Bartunik, H. D., Hekman, M., Rapp, U. R., Huber, L. A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403435101 · Cited by 95 · see citing works