Atomic structure of the MAP kinase ERK2 at 2.3 A resolution

Improved methods for building protein models in electron density maps and the location of errors in these models

Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,650 · 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

Stereochemistry of Cooperative Effects in Haemoglobin: Haem–Haem Interaction and the Problem of Allostery

Perutz, M. F. (1970) · Nature · doi:10.1038/228726a0 · Cited by 2,931 · see citing works

Crystallographic R Factor Refinement by Molecular Dynamics

Brünger, A. T., Kuriyan, J., & Karplus, M. (1987) · Science · doi:10.1126/science.235.4787.458 · Cited by 1,965 · see citing works

ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF

Boulton, T. G., Nye, S. H., Robbins, D. J., Ip, N. Y., Radzlejewska, E., Morgenbesser, S. D., DePinho, R. A., Panayotatos, N., Cobb, M. H., & Yancopoulos, G. D. (1991) · Cell · doi:10.1016/0092-8674(91)90098-j · Cited by 1,876 · see citing works

A graphics model building and refinement system for macromolecules

Jones, T. A. (1978) · Journal of Applied Crystallography · doi:10.1107/s0021889878013308 · Cited by 1,848 · 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

Phosphorylation of c-jun mediated by MAP kinases

Pulverer, B., Kyriakis, J. M., Avruch, J., Nikolakaki, E., & Woodgett, J. R. (1991) · Nature · doi:10.1038/353670a0 · Cited by 1,470 · see citing works

MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo.

Sun, H., Charles, C. H., Lau, L. F., & Tonks, N. K. (1993) · Cell · doi:10.1016/0092-8674(93)90383-2 · Cited by 1,156 · see citing works

Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase

Anderson, N. G., Maller, J. L., Tonks, N. K., & Sturgill, T. W. (1990) · Nature · doi:10.1038/343651a0 · Cited by 1,064 · see citing works

A Divergence in the MAP Kinase Regulatory Network Defined by MEK Kinase and Raf

Lange, C. A., Pleiman, C., Gardner, A. M., Blumer, K., & Johnson, G. L. (1993) · Science · doi:10.1126/science.8385802 · Cited by 1,059 · see citing works

Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II

Sturgill, T. W., Ray, L. B., ERIKSON, E., & Maller, J. L. (1988) · Nature · doi:10.1038/334715a0 · Cited by 1,017 · 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

Complexes of Ras⋅GTP with Raf-1 and Mitogen-Activated Protein Kinase Kinase

Moodie, S. A., Willumsen, B. M., Weber, M. J., & Wolfman, A. (1993) · Science · doi:10.1126/science.8503013 · Cited by 968 · see citing works

Phosphorylation of transcription factor p62TCF by MAP kinase stimulates ternary complex formation at c-fos promoter

Gille, H., Sharrocks, A. D., & Shaw, P. E. (1992) · Nature · doi:10.1038/358414a0 · Cited by 966 · see citing works

Structure of a Peptide Inhibitor Bound to the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

Knighton, D. R., Zheng, J., Eyck, L. F. T., Xuong, N., Taylor, S. S., & Sowadski, J. M. (1991) · Science · doi:10.1126/science.1862343 · Cited by 960 · see citing works

The Primary Structure of MEK, a Protein Kinase that Phosphorylates the ERK Gene Product

Crews, C. M., Alessandrini, A., & Erikson, R. L. (1992) · Science · doi:10.1126/science.1411546 · Cited by 930 · see citing works

An Insulin-Stimulated Protein Kinase Similar to Yeast Kinases Involved in Cell Cycle Control

Boulton, T. G., Yancopoulos, G. D., Gregory, J. S., Slaughter, C. A., Moomaw, C. R., Hsu, J., & Cobb, M. H. (1990) · Science · doi:10.1126/science.2164259 · Cited by 707 · see citing works

Rapid stimulation by insulin of a serine/threonine kinase in 3T3-L1 adipocytes that phosphorylates microtubule-associated protein 2 in vitro.

Ray, L. B., & Sturgill, T. W. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.6.1502 · Cited by 592 · see citing works

Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer‐like state.

Drewes, G., Lichtenberg‐Kraag, B., Döring, F., Mandelkow, E. M., Biernat, J., Goris, J., Dorée, M., & Mandelkow, E. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05272.x · Cited by 565 · see citing works

Ribbon models of macromolecules

Carson, M. (1987) · Journal of Molecular Graphics · doi:10.1016/0263-7855(87)80010-3 · Cited by 518 · see citing works

The interaction of SV40 small tumor antigen with protein phosphatase 2A stimulates the map kinase pathway and induces cell proliferation

Sontag, E., Fedorov, S. A., Kamibayashi, C., Robbins, D. J., Cobb, M. H., & Mumby, M. C. (1993) · Cell · doi:10.1016/0092-8674(93)90533-v · Cited by 510 · see citing works

Extracellular signal-regulated kinases: ERKs in progress.

Cobb, M. H., Boulton, T. G., & Robbins, D. J. (1991) · Cell Regulation · doi:10.1091/mbc.2.12.965 · Cited by 508 · see citing works

Regulation and properties of extracellular signal-regulated protein kinases 1 and 2 in vitro.

Robbins, D. J., Zhen, E., Owaki, H., Vanderbilt, C. A., Ebert, D. J., Geppert, T. D., & Cobb, M. H. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53507-9 · Cited by 499 · see citing works

Multiple components in an epidermal growth factor-stimulated protein kinase cascade

Ahn, N. G., Seger, R., Bratlien, R. L., Diltz, C. D., Tonks, N. K., & Krebs, E. G. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)64310-1 · Cited by 492 · see citing works

Isolation of the human cdk2 gene that encodes the cyclin A- and adenovirus E1A-associated p33 kinase

Tsai, L., Harlow, E., & Meyerson, M. M. (1991) · Nature · doi:10.1038/353174a0 · Cited by 461 · see citing works

Identification of substrate recognition determinants for human ERK1 and ERK2 protein kinases.

Gonzalez, F. A., Raden, D. L., & Davis, R. J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54548-8 · Cited by 454 · see citing works

Definition of a consensus sequence for peptide substrate recognition by p44mpk, the meiosis-activated myelin basic protein kinase

Clark‐Lewis, I., Sanghera, J. S., & Pelech, S. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98601-1 · Cited by 406 · see citing works

Identification of multiple extracellular signal-regulated kinases (ERKs) with antipeptide antibodies.

Boulton, T. G., & Cobb, M. H. (1991) · Cell Regulation · doi:10.1091/mbc.2.5.357 · Cited by 390 · 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

Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation.

Seger, R., Ahn, N. G., Boulton, T. G., Yancopoulos, G. D., Panayotatos, N., Radziejewska, E., Ericsson, L. H., Bratlien, R. L., Cobb, M. H., & Krebs, E. G. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.14.6142 · Cited by 336 · see citing works

Glucose-induced conformational change in yeast hexokinase.

Bennett, W. S., & Steitz, T. A. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.10.4848 · Cited by 308 · see citing works

The human CL100 gene encodes a Tyr/Thr-protein phosphatase which potently and specifically inactivates MAP kinase and suppresses its activation by oncogenic ras in Xenopus oocyte extracts.

Alessi, D. R., Smythe, C., & Keyse, S. M. (1993) · PubMed · Cited by 306 · see citing works

Isolation of cDNA clones coding for the catalytic subunit of mouse cAMP-dependent protein kinase.

Uhler, M. D., Carmichael, D. F., Lee, D. C., Chrivia, J. C., Krebs, E. G., & McKnight, G. S. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.5.1300 · Cited by 271 · see citing works

ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ.

Haycock, J. W., Ahn, N. G., Cobb, M. H., & Krebs, E. G. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.6.2365 · Cited by 261 · see citing works

[28] Software for a diffractometer with multiwire area detector

Howard, A. J., Nielsen, C., & Xuong, N. H. (1985) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(85)14030-9 · Cited by 259 · see citing works

Isolation and characterization of two growth factor-stimulated protein kinases that phosphorylate the epidermal growth factor receptor at threonine 669

Northwood, I. C., Gonzalez, F. A., Wartmann, M., Raden, D. L., & Davis, R. J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98612-6 · Cited by 209 · see citing works

Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase.

Hurley, J. H., Thorsness, P. E., Ramalingam, V., Helmers, N. S., Koshland, D. E., & Stroud, R. M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.22.8635 · Cited by 207 · see citing works

A template for the protein kinase family

Taylor, S. S., Knighton, D. R., Zheng, J., Sowadski, J. M., Gibbs, C. S., & Zoller, M. J. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)80001-r · Cited by 194 · see citing works

Dephosphorylation and inactivation of the mitogen-activated protein kinase by a mitogen-induced Thr/Tyr protein phosphatase

Zheng, C., & Guan, K. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85396-6 · Cited by 170 · see citing works

A dominant-negative mutant of raf blocks mitogen-activated protein kinase activation by growth factors and oncogenic p21ras.

Schaap, D., van der Wal, J., Howe, L. R., Marshall, C., & BLITTERSWIJK, W. J. V. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80719-4 · Cited by 160 · see citing works

Epidermal growth factor (EGF) receptor T669 peptide kinase from 3T3-L1 cells is an EGF-stimulated "MAP" kinase.

Takishima, K., Griswold‐Prenner, I., Ingebritsen, T. S., & Rosner, M. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.6.2520 · Cited by 159 · see citing works

Mapping protein dynamics by X-ray diffraction

Ringe, D., & Petsko, G. A. (1985) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(85)90002-1 · Cited by 155 · see citing works

Eukaryotic protein kinases

Hanks, S. K. (1991) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(91)90035-r · Cited by 137 · see citing works

Nerve growth factor and fibroblast growth factor selectively activate a protein kinase that phosphorylates high molecular weight microtubule-associated proteins. Detection, partial purification, and characterization in PC12 cells.

Tsao, H., Aletta, J. M., & Greene, L. A. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55420-x · Cited by 116 · see citing works

Structural Basis for the Activation of Glycogen Phosphorylase b by Adenosine Monophosphate

Sprang, S. R., Withers, S. G., Goldsmith, E. J., Fletterick, R. J., & Madsen, N. B. (1991) · Science · doi:10.1126/science.1962195 · Cited by 111 · see citing works

Evidence that extracellular signal-regulated kinases are the insulin-activated Raf-1 kinase kinases.

Lee, R., Cobb, M. H., & Blackshear, P. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48399-8 · Cited by 104 · see citing works

Map Kinases Erk1 And Erk2: Pleiotropic Enzymes In A Ubiquitous Signaling Network

Robbins, D. J., Zhen, E., Cheng, M. M., Xu, S., Ebert, D. J., & Cobb, M. H. (1994) · Advances in cancer research · doi:10.1016/s0065-230x(08)60399-1 · Cited by 73 · see citing works

Structure of the mammalian catalytic subunit of cAMP-dependent protein kinase and an inhibitor peptide displays an open conformation

Karlsson, R., Zheng, J., Xuong, N., Taylor, S. S., & Sowadski, J. M. (1993) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444993002306 · Cited by 65 · see citing works

Identification of Tyr-185 as the site of tyrosine autophosphorylation of recombinant mitogen-activated protein kinase p42mapk.

Rossomando, A. J., Wu, J., Michel, H., Shabanowitz, J., Hunt, D. F., Weber, M. J., & Sturgill, T. W. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.13.5779 · Cited by 61 · see citing works

Domain motions in proteins

Schulz, G. E. (1991) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(91)90082-5 · Cited by 57 · see citing works

Crystallization and Preliminary X-ray Studies of Extracellular Signal-regulated Kinase-2/MAP Kinase with an Incorporated His-tag

Zhang, F. P. Y., Robbins, D. J., Cobb, M. H., & Goldsmith, E. J. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1532 · Cited by 31 · see citing works

Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*

Pearson, G. W., Robinson, F. L., Gibson, T. B., Xu, B.-E., Karandikar, M. S., Berman, K. S., & Cobb, M. H. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.2.0428 · Cited by 4,044 · see citing works

Mutation of the mouse klotho gene leads to a syndrome resembling ageing

Kuro-o, M., Matsumura, Y., Aizawa, H., Kawaguchi, H., Suga, T., Utsugi, T., Ohyama, Y., Kurabayashi, M., Kaname, T., Kume, E., et al. (1997) · Nature · doi:10.1038/36285 · Cited by 3,837 · see citing works

A protein kinase involved in the regulation of inflammatory cytokine biosynthesis

Lee, J. C., Laydon, J. T., McDonnell, P., Gallagher, T. F., Kumar, S., Green, D., McNulty, D. E., Blumenthal, M. J., Keys, J., vatter, S. W. L., et al. (1994) · Nature · doi:10.1038/372739a0 · Cited by 3,266 · see citing works

A MAP Kinase Targeted by Endotoxin and Hyperosmolarity in Mammalian Cells

Han, J., Lee, J. D., Bibbs, L., & Ulevitch, R. J. (1994) · Science · doi:10.1126/science.7914033 · Cited by 2,647 · see citing works

The Conformational Plasticity of Protein Kinases

Huse, M., & Kuriyan, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00741-9 · Cited by 1,760 · see citing works

Signal Transduction through MAP Kinase Cascades

Lewis, T. S., Shapiro, P. S., & Ahn, N. G. (1998) · Advances in cancer research · doi:10.1016/s0065-230x(08)60765-4 · Cited by 1,746 · see citing works

How MAP Kinases Are Regulated

Cobb, M. H., & Goldsmith, E. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.25.14843 · Cited by 1,718 · see citing works

ERK1/2 MAP kinases: Structure, function, and regulation

Roskoski, R. J. (2012) · Pharmacological Research · doi:10.1016/j.phrs.2012.04.005 · Cited by 1,642 · see citing works

Mitogen-Activated Protein Kinases: Specific Messages from Ubiquitous Messengers

Schaeffer, H. J., & Weber, M. J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2435 · Cited by 1,600 · see citing works

Mechanisms of specificity in protein phosphorylation

Ubersax, J. A., & Ferrell Jr, J. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2203 · Cited by 1,451 · see citing works

Receptor-Dependent Mechanisms of Cell Stimulation by Bacterial Endotoxin

Ulevitch, R. J., & Tobias, P. S. (1995) · Annual Review of Immunology · doi:10.1146/annurev.iy.13.040195.002253 · Cited by 1,442 · 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

Active and Inactive Protein Kinases: Structural Basis for Regulation

Johnson, L. N., Noble, M. E. M., & Owen, D. J. (1996) · Cell · doi:10.1016/s0092-8674(00)81092-2 · Cited by 1,396 · see citing works

The CLAVATA1Gene Encodes a Putative Receptor Kinase That Controls Shoot and Floral Meristem Size in Arabidopsis

Clark, S. E., Williams, R. W., & Meyerowitz, E. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80239-1 · Cited by 1,373 · see citing works

Oxidative stress and gene regulation

Allen, R. G., & Tresini, M. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00242-7 · Cited by 1,297 · see citing works

ERK signalling: A master regulator of cell behaviour, life and fate

Lavoie, H., Gagnon, J., & Therrien, M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0255-7 · Cited by 1,185 · see citing works

Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus.

Shamu, C. E., & Walter, P. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00666.x · Cited by 1,258 · see citing works

Regulation of Protein Kinases

Nolen, B. J., Taylor, S. S., & Ghosh, G. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.08.024 · Cited by 1,171 · see citing works

CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF THE HUMAN INSULIN RECEPTOR

Hubbard, S. R., Wei, L., Ellis, L., & Hendrickson, W. A. (1994) · Nature · doi:10.1038/372746a0 · Cited by 1,080 · 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

Tyrosine Phosphorylation of Focal Adhesion Kinase at Sites in the Catalytic Domain Regulates Kinase Activity: a Role for Src Family Kinases

Calalb, M. B., Polte, T. R., & Hanks, S. K. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.2.954 · Cited by 987 · see citing works

MAPKs: new JNK expands the group

Davis, R. J. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90132-5 · Cited by 944 · see citing works

The MEK/ERK cascade: From signaling specificity to diverse functions

Shaul, Y. D., & Seger, R. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.10.005 · Cited by 934 · see citing works

MAP kinase pathways

Cobb, M. H. (1999) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(98)00056-x · Cited by 869 · see citing works

Disease Resistance and Abiotic Stress Tolerance in Rice Are Inversely Modulated by an Abscisic Acid–Inducible Mitogen-Activated Protein Kinase[W]

Xiong, L., & Yang, Y. (2003) · The Plant Cell · doi:10.1105/tpc.008714 · Cited by 830 · 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

MAP Kinases

Chen, Z., Gibson, T. B., Robinson, F. L., Silvestro, L., Pearson, G. W., Xu, B.-E., Wright, A., Vanderbilt, C. A., & Cobb, M. H. (2001) · Chemical Reviews · doi:10.1021/cr000241p · Cited by 790 · see citing works

Activation of the Mitogen-Activated Protein Kinase/Extracellular Signal-Regulated Kinase Pathway by Conventional, Novel, and Atypical Protein Kinase C Isotypes

Schönwaßer, D. C., Marais, R., Marshall, C. J., & Parker, P. J. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.2.790 · Cited by 760 · see citing works

Characterization of the Structure and Function of a New Mitogen-activated Protein Kinase (p38β)

Jiang, Y., Chen, C., Li, Z., Guo, W., Gegner, J. A., Lin, S., & Han, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.17920 · Cited by 746 · see citing works

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., & Goldsmith, E. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80351-7 · Cited by 729 · see citing works

GS domain mutations that constitutively activate T beta R‐I, the downstream signaling component in the TGF‐beta receptor complex.

Wieser, R., Wrana, J. L., & Massagué, J. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07214.x · Cited by 689 · 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

Phosphorylation of the MAP Kinase ERK2 Promotes Its Homodimerization and Nuclear Translocation

Khokhlatchev, A. V., Canagarajah, B. J., Wilsbacher, J. L., Robinson, M. J., Atkinson, M. A., Goldsmith, E. J., & Cobb, M. H. (1998) · Cell · doi:10.1016/s0092-8674(00)81189-7 · Cited by 675 · 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

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

Structural Basis of Aurora-A Activation by TPX2 at the Mitotic Spindle

Bayliss, R. W., Sardón, T., Vernos, I., & Conti, E. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00392-7 · Cited by 644 · see citing works

Structural Basis for Control by Phosphorylation

Johnson, L. N., & Lewis, R. J. (2001) · Chemical Reviews · doi:10.1021/cr000225s · Cited by 643 · 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

Structural basis of cyclin-dependent kinase activation by phosphorylation

Russo, A. A., Jeffrey, P. D., & Pavletich, N. P. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0896-696 · Cited by 599 · see citing works

Targeting JNK for therapeutic benefit: from junk to gold?

Manning, A. M., & Davis, R. J. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd1132 · Cited by 585 · see citing works

The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution.

Colwill, K., Pawson, T. J., Andrews, B., Prasad, J., Manley, J. L., Bell, J. C., & Duncan, P. I. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00357.x · Cited by 583 · see citing works

Pyridinyl Imidazole Inhibitors of p38 Mitogen-activated Protein Kinase Bind in the ATP Site

Young, P. R., McLaughlin, M. M., Kumar, S., Kassis, S., Doyle, M. L., McNulty, D. E., Gallagher, T. F., Fisher, S., McDonnell, P., Carr, S. A., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.18.12116 · Cited by 570 · see citing works

The ERK Cascade: Distinct Functions within Various Subcellular Organelles

Wortzel, I., & Seger, R. (2011) · Genes & Cancer · doi:10.1177/1947601911407328 · Cited by 563 · 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

NF-κB-inducing kinase activates IKK-α by phosphorylation of Ser-176

Lei, L., Cao, Z., & Goeddel, D. V. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.7.3792 · Cited by 536 · see citing works

Network Analysis of Protein Structures Identifies Functional Residues

Amitai, G., Shemesh, A., Sitbon, E., Shklar, M., Netanely, D., Venger, I., & Pietrokovski, S. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.10.055 · Cited by 504 · 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

Protein kinase C is regulated in vivo by three functionally distinct phosphorylations

Keranen, L. M., Sonnenburg, E. D., & Newton, A. C. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00277-6 · Cited by 470 · see citing works

The ERK Cascade: A Prototype of MAPK Signaling

Rubinfeld, H., & Seger, R. (2005) · Molecular Biotechnology · doi:10.1385/mb:31:2:151 · Cited by 460 · see citing works

MECHANOTRANSDUCTION INVOLVING MULTIMODULAR PROTEINS: Converting Force into Biochemical Signals

Viola Vogel, B. (2006) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.35.040405.102013 · Cited by 447 · see citing works

New Insights into the Control of MAP Kinase Pathways

English, J. M., Pearson, G. W., Wilsbacher, J. L., Swantek, J. L., Karandikar, M. S., Xu, S., & Cobb, M. H. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4687 · Cited by 434 · see citing works

The Structural Basis for Control of Eukaryotic Protein Kinases

Endicott, J., Noble, M. E. M., & Johnson, L. N. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052410-090317 · Cited by 431 · see citing works

MAP Kinases with Distinct Inhibitory Functions Impart Signaling Specificity during Yeast Differentiation

Madhani, H. D., Styles, C. A., & Fink, G. R. (1997) · Cell · doi:10.1016/s0092-8674(00)80454-7 · Cited by 428 · see citing works

Structural basis of inhibitor selectivity in MAP kinases

Wang, Z., Canagarajah, B. J., Boehm, J. C., Kassisà, S., Cobb, M. H., Young, P. R., Abdel‐Meguid, S. S., Adams, J. L., & Goldsmith, E. J. (1998) · Structure · doi:10.1016/s0969-2126(98)00113-0 · Cited by 426 · see citing works

Mutations of the TGF-β type II receptorBMPR2 in pulmonary arterial hypertension

Machado, R. D., Aldred, M. A., James, V. M., Harrison, R. E., Patel, B., Schwalbe, E. C., Grünig, E., Janssen, B. J., Koehler, R., Seeger, W., et al. (2006) · Human Mutation · doi:10.1002/humu.20285 · Cited by 401 · see citing works

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 394 · see citing works

Dynamics of cAMP-Dependent Protein Kinase

Johnson, D. A., Akamine, P., Radzio-Andzelm, E., Madhusudan, & Taylor, S. S. (2001) · Chemical Reviews · doi:10.1021/cr000226k · Cited by 393 · see citing works

A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket

Tong, L., Pav, S., White, D. M., Rogers, S., Crane, K. M., Cywin, C. L., Brown, M. L., & Pargellis, C. A. (1997) · Nature Structural Biology · doi:10.1038/nsb0497-311 · Cited by 386 · see citing works

Structures of Src-family tyrosine kinases

Sicheri, F., & Kuriyan, J. (1997) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(97)80146-7 · Cited by 381 · see citing works

Protein Analysis by Hydrogen Exchange Mass Spectrometry

Hoofnagle, A. N., Resing, K. A., & Ahn, N. G. (2003) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.32.110601.142417 · Cited by 381 · see citing works

Structure of the FGF Receptor Tyrosine Kinase Domain Reveals a Novel Autoinhibitory Mechanism

Mohammadi, M., Schlessinger, J., & Hubbard, S. R. (1996) · Cell · doi:10.1016/s0092-8674(00)80131-2 · Cited by 371 · see citing works

Three protein kinase structures define a common motif

Taylor, S. S., & Radzio-Andzelm, E. (1994) · Structure · doi:10.1016/s0969-2126(00)00036-8 · Cited by 371 · see citing works

Inactivation of p42 MAP kinase by protein phosphatase 2A and a protein tyrosine phosphatase, but not CL100, in various cell lines

Alessi, D. R., Gomez, N., Moorhead, G., Lewis, T., Keyse, S. M., & Cohen, P. (1995) · Current Biology · doi:10.1016/s0960-9822(95)00059-5 · Cited by 365 · see citing works

Structural basis for activation of the titin kinase domain during myofibrillogenesis

Mayans, O. M., van der Ven, P. F. M., Wilm, M. S., Mues, A., Young, P. W., Fürst, D. O., Wilmanns, M., & Gautel, M. (1998) · Nature · doi:10.1038/27603 · Cited by 362 · 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

Crystal Structure of a Complex Between the Catalytic and Regulatory (RIα) Subunits of PKA

Kim, C., Xuong, N., & Taylor, S. S. (2005) · Science · doi:10.1126/science.1104607 · Cited by 343 · see citing works

p38 MAP kinase: a convergence point in cancer therapy

Olson, J. M., & Hallahan, A. R. (2004) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2004.01.007 · Cited by 335 · see citing works

Molecular Cloning and Characterization of a Novel p38 Mitogen-activated Protein Kinase

Wang, X. S., Diener, K., Manthey, C. L., Wang, S., Rosenzweig, B., Bray, J., Delaney, J., Cole, C. N., Chan-Hui, P.-Y., Mantlo, N. B., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.38.23668 · Cited by 331 · see citing works

Regulation of the ERK Subgroup of MAP Kinase Cascades Through G Protein-Coupled Receptors

Sugden, P. H., & Clerk, A. (1997) · Cellular Signalling · doi:10.1016/s0898-6568(96)00191-x · Cited by 326 · see citing works

Structural Basis for the Autoinhibition of Calcium/Calmodulin-Dependent Protein Kinase I

Goldberg, J. D., Nairn, A. C., & Kuriyan, J. (1996) · Cell · doi:10.1016/s0092-8674(00)81066-1 · Cited by 324 · see citing works

Molecular basis of MAP kinase regulation

Peti, W., & Page, R. (2013) · Protein Science · doi:10.1002/pro.2374 · Cited by 302 · see citing works

PTP‐SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal‐regulated kinases ERK1 and ERK2 by association through a kinase interaction motif

Pulido, R., Zúñiga, Á., & Ullrich, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7337 · Cited by 320 · see citing works

Tyrosine Kinase Inhibitors. 8. An Unusually Steep Structure−Activity Relationship for Analogues of 4-(3-Bromoanilino)-6,7-dimethoxyquinazoline (PD 153035), a Potent Inhibitor of the Epidermal Growth Factor Receptor

Bridges, A. J., Zhou, H., Cody, D. R., Rewcastle, G. W., McMichael, A., Showalter, H. D. H., Fry, D. W., Kraker, A. J., & Denny, W. A. (1996) · Journal of Medicinal Chemistry · doi:10.1021/jm9503613 · Cited by 320 · see citing works

Protein kinase CK2 (“casein kinase-2”) and its implication in cell division and proliferation

Pinna, L. A., & Meggio, F. (1997) · Springer eBooks · doi:10.1007/978-1-4615-5371-7_7 · Cited by 320 · see citing works

Molecular recognitions in the MAP kinase cascades

Tanoue, T., & Nishida, E. (2003) · Cellular Signalling · doi:10.1016/s0898-6568(02)00112-2 · Cited by 318 · see citing works

MAPK machinery in plants

Taj, G., Agarwal, P., Grant, M., & Kumar, A. (2010) · Plant Signaling & Behavior · doi:10.4161/psb.5.11.13020 · Cited by 314 · see citing works

Targeting ERK1/2 protein-serine/threonine kinases in human cancers

Roskoski, R. J. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.01.039 · Cited by 310 · 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

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

Catalytic Control in the EGF Receptor and Its Connection to General Kinase Regulatory Mechanisms

Jura, N., Zhang, X., Endres, N. F., Seeliger, M. A., Schindler, T., & Kuriyan, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.004 · Cited by 310 · see citing works

Signalling in the Yeasts: An Informational Cascade with Links to the Filamentous Fungi

Banuett, F. (1998) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.62.2.249-274.1998 · Cited by 297 · see citing works

Different Susceptibility of Protein Kinases to Staurosporine Inhibition

Meggio, F., Deana, A. D., Ruzzene, M., Brunati, A. M., Cesaro, L., Guerra, B., Meyer, T., Mett, H., Fabbro, D., Furet, P., et al. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.317_c.x · Cited by 296 · see citing works

Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions

Tanoue, T., Maeda, R., Adachi, M., & Nishida, E. (2001) · The EMBO Journal · doi:10.1093/emboj/20.3.466 · Cited by 285 · 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

ERK1 and ERK2 Map Kinases: Specific Roles or Functional Redundancy?

Buscà, R., Pouysségur, J., & Lenormand, P. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00053 · Cited by 282 · see citing works

Multiple modes of ligand recognition: Crystal structures of cyclin‐dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopentenyladenine

Schulze‐Gahmen, U., Brandsen, J., Jones, H. D., Morgan, D. O., Meijer, L., Veselý, J., & Kim, S. (1995) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340220408 · Cited by 281 · see citing works

The structure of mitogen-activated protein kinase p38 at 2.1-Å resolution

Wang, Z., Harkins, P. C., Ulevitch, R. J., Han, J., Cobb, M. H., & Goldsmith, E. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2327 · Cited by 275 · see citing works

The structural basis for the specificity of pyridinylimidazole inhibitors of p38 MAP kinase

Wilson, K. P., McCaffrey, P. G., Hsiao, K., Pazhanisamy, S., Galullo, V., Bemis, G. W., Fitzgibbon, M. J., Caron, P. R., Murcko, M. A., & Su, M. S. S. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90194-0 · Cited by 275 · see citing works

Replicative senescence: a critical review

Cristofalo, V. J., Lorenzini, A., Allen, R. G., Torres, C. A., & Tresini, M. (2004) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2004.07.010 · Cited by 275 · see citing works

Autophosphorylation in the Activation Loop Is Required for Full Kinase Activity In Vivo of Human and Yeast Eukaryotic Initiation Factor 2α Kinases PKR and GCN2

Romano, P. R., Garcia-Barrio, M. T., Zhang, X., Wang, Q., Taylor, D. R., Zhang, F., Herring, C., Mathews, M. B., Qin, J., & Hinnebusch, A. G. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.4.2282 · Cited by 272 · see citing works

The regulation of tyrosine kinase signalling pathways by growth factor and G-protein-coupled receptors

Malarkey, K., BELHAM, C. M., Paul, A., Graham, A. M., McLees, A., Scott, P., & Plevin, R. J. (1995) · Biochemical Journal · doi:10.1042/bj3090361 · Cited by 268 · see citing works

ERK5 Is a Novel Type of Mitogen-Activated Protein Kinase Containing a Transcriptional Activation Domain

Kasler, H. G., Victoria, J. G., Duramad, O., & Winoto, A. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.22.8382-8389.2000 · Cited by 267 · see citing works

Crystal Structure of p38 Mitogen-activated Protein Kinase

Wilson, K. P., Fitzgibbon, M. J., Caron, P. R., Griffith, J. P., Chen, W., McCaffrey, P. G., Chambers, S. P., & Su, M. S. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27696 · Cited by 262 · see citing works

Cell cycle analysis of the activity, subcellular localization, and subunit composition of human CAK (CDK-activating kinase).

Tassan, J., Schultz, S. J., Bártek, J., & Nigg, E. A. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.127.2.467 · Cited by 252 · see citing works

A unique inhibitor binding site in ERK1/2 is associated with slow binding kinetics

Chaikuad, A., Tacconi, E. M., Zimmer, J., Liang, Y., Gray, N. S., Tarsounas, M., & Knapp, S. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1629 · Cited by 247 · see citing works

Myosin light chain kinases

Gallagher, P. J., Herring, B. P., & Stull, J. T. (1997) · Journal of Muscle Research and Cell Motility · doi:10.1023/a:1018616814417 · Cited by 246 · see citing works

Structure of an Enzyme Required for Aminoglycoside Antibiotic Resistance Reveals Homology to Eukaryotic Protein Kinases

Hon, W., McKay, G. A., Thompson, P. R., Sweet, R. M., Yang, D. S. C., Wright, G. D., & Berghuis, A. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80274-3 · Cited by 241 · 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

Evolution of the eukaryotic protein kinases as dynamic molecular switches

Taylor, S. S., Keshwani, M. M., Steichen, J. M., & Kornev, A. P. (2012) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2012.0054 · Cited by 235 · see citing works

Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases

Young, T. A., Delagoutte, B., Endrizzi, J. A., Falick, A. M., & Alber, T. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb897 · Cited by 230 · see citing works

Activation mechanism of the MAP kinase ERK2 by dual phosphorylation

Canagarajah, B. J., Khokhlatchev, A., Cobb, M. H., & Goldsmith, E. J. (1997) · Cell · doi:10.1016/s0092-8674(00)80351-7 · Cited by 729 · see citing works

Activity of the MAP kinase ERK2 is controlled by a flexible surface loop

Zhang, J., Zhang, F. P. Y., Ebert, D. J., Cobb, M. H., & Goldsmith, E. J. (1995) · Structure · doi:10.1016/s0969-2126(01)00160-5 · Cited by 121 · see citing works

Understanding the Allosteric Control of Kinase Activation by Phosphorylation‐Regulated Protein Dynamics

Iverson, D. B., & Ahn, N. G. (2017) · The FASEB Journal · doi:10.1096/fasebj.31.1_supplement.607.3

Effects of Phosphorylation of ERK2 Kinase on the Properties of Active Site Amino Acids

Sun, J., Trumble, J. M., Barnsley, K. K., & Ondrechen, M. J. (2022) · The FASEB Journal · doi:10.1096/fasebj.2022.36.s1.r4097

Activation Loop Plasticity and Active Site Coupling in the MAP Kinase, ERK2

Pegram, L. M., Riccardi, D., & Ahn, N. G. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168309 · Cited by 17 · see citing works