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

PROCHECK: a program to check the stereochemical quality of protein structures

Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581 · see citing works

The CCP4 suite: programs for protein crystallography

Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,299 · see citing works

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011 · 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

AMoRe: an automated package for molecular replacement

Navaza, J. (1994) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767393007597 · Cited by 4,941 · 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

JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain

Dérijard, B., Hibi, M., Wu, I.-H., Barrett, T., Su, B., Deng, T., Karin, M., & Davis, R. J. (1994) · Cell · doi:10.1016/0092-8674(94)90380-8 · Cited by 3,188 · 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

Pro-inflammatory Cytokines and Environmental Stress Cause p38 Mitogen-activated Protein Kinase Activation by Dual Phosphorylation on Tyrosine and Threonine

Raingeaud, J., Gupta, S., Rogers, J. S., Dickens, M., Han, J., Ulevitch, R. J., & Davis, R. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7420 · Cited by 2,244 · see citing works

Sparse matrix sampling: a screening method for crystallization of proteins

Jancarik, J., & Kim, S. H. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004430 · Cited by 2,055 · see citing works

Improved Fourier coefficients for maps using phases from partial structures with errors

Read, R. J. (1986) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767386099622 · Cited by 1,885 · 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

A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins

Rouse, J. W., Cohen, P., Trigon, S., Morange, M., Alonso‐Llamazares, A., Zamanillo, D., Hunt, T., & Nebreda, Á. R. (1994) · Cell · doi:10.1016/0092-8674(94)90277-1 · Cited by 1,674 · see citing works

Independent Human MAP-Kinase Signal Transduction Pathways Defined by MEK and MKK Isoforms

Dérijard, B., Raingeaud, J., Barrett, T., Wu, I.-H., Han, J., Ulevitch, R. J., & Davis, R. J. (1995) · Science · doi:10.1126/science.7839144 · Cited by 1,555 · 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

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

Transformation of Mammalian Cells by Constitutively Active MAP Kinase Kinase

Mansour, S. J., Matten, W. T., Hermann, A. S., Candia, J. M., Rong, S., Fukasawa, K., Woude, G. F. V., & Ahn, N. G. (1994) · Science · doi:10.1126/science.8052857 · Cited by 1,355 · see citing works

SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules

Evans, S. V. (1993) · Journal of Molecular Graphics · doi:10.1016/0263-7855(93)87009-t · Cited by 1,287 · see citing works

MKK3- and MKK6-Regulated Gene Expression Is Mediated by the p38 Mitogen-Activated Protein Kinase Signal Transduction Pathway

Raingeaud, J., Whitmarsh, A. J., Barrett, T., Dérijard, B., & Davis, R. J. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.3.1247 · Cited by 1,280 · see citing works

How Proteolysis Drives the Cell Cycle

King, R. W., Deshaies, R. J., Peters, J.-M., & Kirschner, M. W. (1996) · Science · doi:10.1126/science.274.5293.1652 · Cited by 1,273 · 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

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

Identification of the regulatory phosphorylation sites in pp42/mitogen‐activated protein kinase (MAP kinase).

Payne, D. M., Rossomando, A. J., Martino, P. A., Erickson, A. K., Her, J. H., Shabanowitz, J., Hunt, D. F., Weber, M. J., & Sturgill, T. W. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb08021.x · Cited by 1,041 · 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

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

Stress-Induced Phosphorylation and Activation of the Transcription Factor CHOP (GADD153) by p38 MAP Kinase

Wang, X., & Ron, D. (1996) · Science · doi:10.1126/science.272.5266.1347 · Cited by 885 · see citing works

Interleukin-1 activates a novel protein kinase cascade that results in the phosphorylation of hsp27

Freshney, N. W., Rawlinson, L. M., Guesdon, F., Jones, E., Cowley, S. A., Hsuan, J. J., & Saklatvala, J. (1994) · Cell · doi:10.1016/0092-8674(94)90278-x · Cited by 865 · see citing works

Identification of a Dual Specificity Kinase That Activates the Jun Kinases and p38-Mpk2

Lin, A., Minden, A., Martinetto, H., Claret, F.-X., Lange, C. A., Mercurio, F., Johnson, G. L., & Karin, M. (1995) · Science · doi:10.1126/science.7716521 · Cited by 763 · 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

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

Components of a New Human Protein Kinase Signal Transduction Pathway

Zhou, G., Bao, Z., & Dixon, J. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.21.12665 · Cited by 642 · 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

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

Characterization of the Structure and Function of a Novel MAP Kinase Kinase (MKK6)

Han, J., Lee, J., Jiang, Y., Li, Z., Feng, L., & Ulevitch, R. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.6.2886 · Cited by 512 · 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

Structural basis for specificity and potency of a flavonoid inhibitor of human CDK2, a cell cycle kinase.

de Azevedo, W. F., Müller-Dieckmann, H.-J., Schulze‐Gahmen, U., Worland, P. J., Sausville, E. A., & Kim, S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.2735 · Cited by 496 · 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

Pro-Leu-Ser/Thr-Pro is a consensus primary sequence for substrate protein phosphorylation. Characterization of the phosphorylation of c-myc and c-jun proteins by an epidermal growth factor receptor threonine 669 protein kinase

Alvarez, E., Northwood, I. C., Gonzalez, F. A., Latour, D. A., Seth, A., Abate, C., Curran, T., & Davis, R. J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98613-8 · Cited by 472 · see citing works

A Novel Kinase Cascade Mediated by Mitogen-activated Protein Kinase Kinase 6 and MKK3

Moriguchi, T., Kuroyanagi, N., Yamaguchi, T., Gotoh, Y., Irie, K., Takahisa, K. A. N. O., Shirakabe, K., Muro, Y., Shibuyà, H., Matsumoto, K., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.23.13675 · Cited by 449 · 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

Comparative modeling methods: Application to the family of the mammalian serine proteases

Greer, J. (1990) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340070404 · Cited by 384 · see citing works

Primary Structure of BMK1: A New Mammalian MAP Kinase

Lee, J. D., Ulevitch, R. J., & Han, J. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.2189 · Cited by 345 · see citing works

Identification of Mitogen-activated Protein (MAP) Kinase-activated Protein Kinase-3, a Novel Substrate of CSBP p38 MAP Kinase

McLaughlin, M. M., Kumar, S., McDonnell, P., Horn, S. V., Lee, J. C., Livi, G. P., & Young, P. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.14.8488 · Cited by 342 · see citing works

Cloning and characterization of two distinct human extracellular signal-regulated kinase activator kinases, MEK1 and MEK2

Zheng, C. F., & Guan, K. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82142-1 · Cited by 336 · see citing works

ERK6, a mitogen-activated protein kinase involved in C2C12 myoblast differentiation.

Lechner, C., Zahalka, M. A., Giot, J.-F., Møller, N. P. H., & Ullrich, A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4355 · Cited by 327 · 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

Cloning and Characterization of MEK6, a Novel Member of the Mitogen-activated Protein Kinase Kinase Cascade

Stein, B., Brady, H. A., Yang, M. X., Young, D. B., & Barbosa, M. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.19.11427 · Cited by 190 · see citing works

Insights into autoregulation from the crystal structure of twitchin kinase

Hu, S., Parker, M. W., Lei, J. Y., Wilce, M. C. J., Benian, G. M., & Kemp, B. E. (1994) · Nature · doi:10.1038/369581a0 · Cited by 190 · see citing works

Data collection and processing

Turkenburg, J. P., & McAuley, K. E. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444913016107 · Cited by 153 · see citing works

Mxi2, a mitogen-activated protein kinase that recognizes and phosphorylates Max protein.

Zervos, A. S., Faccio, L., Gatto, J., Kyriakis, J. M., & Brent, R. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.23.10531 · Cited by 150 · see citing works

Three-dimensional Structure of Mammalian Casein Kinase I: Molecular Basis for Phosphate Recognition

Longenecker, K. L., Roach, P. J., & Hurley, T. D. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0189 · Cited by 132 · see citing works

Domain movements in protein kinases

Cox, S. E., Radzio-Andzelm, E., & Taylor, S. S. (1994) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(94)90272-0 · Cited by 131 · see citing works

Identification of MAP Kinase Domains by Redirecting Stress Signals into Growth Factor Responses

Brunet, A., & Pouysségur, J. (1996) · Science · doi:10.1126/science.272.5268.1652 · Cited by 125 · 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

Stress-activated protein kinases bind directly to the delta domain of c-Jun in resting cells: implications for repression of c-Jun function.

Dai, T., Rubie, E. A., Franklin, C. C., Kraft, A. S., Gillespie, D. A., Avruch, J., Kyriakis, J. M., & Woodgett, J. R. (1995) · PubMed · Cited by 98 · see citing works

ERK3 Is a Constitutively Nuclear Protein Kinase

Cheng, M. M., Boulton, T. G., & Cobb, M. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.15.8951 · Cited by 93 · see citing works

Contributions of the Mitogen-activated Protein (MAP) Kinase Backbone and Phosphorylation Loop to MEK Specificity

Robinson, M. J., Cheng, M. M., Khokhlatchev, A. V., Ebert, D. J., Ahn, N. G., Guan, K., Stein, B., Goldsmith, E. J., & Cobb, M. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.47.29734 · Cited by 71 · see citing works

Extracellular signal-regulated kinases 2 autophosphorylates on a subset of peptides phosphorylated in intact cells in response to insulin and nerve growth factor: analysis by peptide mapping.

Robbins, D. J., & Cobb, M. H. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.3.299 · Cited by 71 · see citing works

MAP kinase binds to the NH2‐terminal activation domain of c‐Myc

Gupta, S., & Davis, R. J. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01052-8 · Cited by 63 · see citing works

Protein kinases

Goldsmith, E. J., & Cobb, M. H. (1994) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(94)90264-x · Cited by 61 · see citing works

Inhibitors of serine/threonine kinases

Lee, J. C., & Adams, J. L. (1995) · Current Opinion in Biotechnology · doi:10.1016/0958-1669(95)80108-1 · Cited by 46 · see citing works

Inhibitors of protein tyrosine kinases

Fry, D. W., & Bridges, A. J. (1995) · Current Opinion in Biotechnology · doi:10.1016/0958-1669(95)80109-x · Cited by 25 · see citing works

Differential regulation and properties of MAPKs

Raman, M., Chen, W., & Cobb, M. H. (2007) · Oncogene · doi:10.1038/sj.onc.1210392 · Cited by 1,430 · 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

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

Functional roles of p38 mitogen-activated protein kinase in macrophage-mediated inflammatory responses

Yang, Y., Kim, S. C., Yu, T., Yi, Y.-S., Rhee, M. H., Sung, G.-H., Yoo, B. C., & Cho, J. Y. (2014) · Mediators of Inflammation · doi:10.1155/2014/352371 · Cited by 406 · 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

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 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

Substrate and Docking Interactions in Serine/Threonine Protein Kinases

Goldsmith, E. J., Akella, R., Min, X., Zhou, T., & Humphreys, J. M. (2007) · Chemical Reviews · doi:10.1021/cr068221w · Cited by 143 · see citing works

NMR Characterization of Kinase p38 Dynamics in Free and Ligand‐Bound Forms

Vogtherr, M., Saxena, K., Hoelder, S., Grimme, S., Betz, M., Schieborr, U., Pescatore, B., Robin, M., Delarbre, L., Langer, T., et al. (2006) · Angewandte Chemie International Edition · doi:10.1002/anie.200502770 · Cited by 145 · see citing works

Docking interactions in the mitogen-activated protein kinase cascades

Tanoue, T., & Nishida, E. (2002) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(02)00188-2 · Cited by 134 · see citing works

The Evolution of the MAP Kinase Pathways: Coduplication of Interacting Proteins Leads to New Signaling Cascades

Caffrey, D. R., O'Neill, L. A. J., & Shields, D. C. (1999) · Journal of Molecular Evolution · doi:10.1007/pl00006578 · Cited by 124 · see citing works

Unique MAP Kinase binding sites

Akella, R., Moon, T. M., & Goldsmith, E. J. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.09.016 · Cited by 108 · see citing works

Molecular basis of MAPK-activated protein kinase 2:p38 assembly

White, A., Pargellis, C. A., Studts, J. M., Werneburg, B. G., & Farmer, B. T. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701679104 · Cited by 111 · see citing works

Hydrophobic as Well as Charged Residues in Both MEK1 and ERK2 Are Important for Their Proper Docking

Xu, B.-E., Stippec, S., Robinson, F. L., & Cobb, M. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102769200 · Cited by 91 · see citing works

Mitogen-activated Protein Kinase (MAPK) Phosphatase 3-mediated Cross-talk between MAPKs ERK2 and p38α

Zhang, Y.-Y., Wu, J.-W., & Wang, Z.-X. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.203786 · Cited by 63 · see citing works

A Distinct Interaction Mode Revealed by the Crystal Structure of the Kinase p38α with the MAPK Binding Domain of the Phosphatase MKP5

Zhang, Y.-Y., Wu, J.-W., & Wang, Z.-X. (2011) · Science Signaling · doi:10.1126/scisignal.2002241 · Cited by 52 · see citing works

Structural Mechanisms of Allostery and Autoinhibition in JNK Family Kinases

Laughlin, J. D., Nwachukwu, J. C., Figuera-Losada, M., Cherry, L., Nettles, K. W., & LoGrasso, P. V. (2012) · Structure · doi:10.1016/j.str.2012.09.021 · Cited by 50 · see citing works

Understanding the specificity of a docking interaction between JNK1 and the scaffolding protein JIP1

Yan, C., Kaoud, T., Lee, S., Dalby, K. N., & Ren, P. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp1073522 · Cited by 36 · see citing works

Resting and Active States of the ERK2:HePTP Complex

Francis, D. M., Różycki, B., Tortajada, A., Hummer, G., Peti, W., & Page, R. (2011) · Journal of the American Chemical Society · doi:10.1021/ja2075136 · Cited by 32 · see citing works

The Third Conformation of p38α MAP Kinase Observed in Phosphorylated p38α and in Solution

Akella, R., Min, X., Wu, Q., Gardner, K. H., & Goldsmith, E. J. (2010) · Structure · doi:10.1016/j.str.2010.09.015 · Cited by 31 · see citing works

Dynamics in the p38α MAP Kinase–SB203580 Complex Observed by Liquid‐State NMR Spectroscopy

Honndorf, V. S., Coudevylle, N., Laufer, S., Becker, S., & Griesinger, C. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200705614 · Cited by 22 · see citing works

The Differential Regulation of p38α by the Neuronal Kinase Interaction Motif Protein Tyrosine Phosphatases, a Detailed Molecular Study

Francis, D. M., Kumar, G. S., Koveal, D., Tortajada, A., Page, R., & Peti, W. (2013) · Structure · doi:10.1016/j.str.2013.07.003 · Cited by 21 · see citing works

NMR Spectroscopic Investigations of the Activated p38α Mitogen‐Activated Protein Kinase

Nielsen, G., & Schwalbe, H. (2011) · ChemBioChem · doi:10.1002/cbic.201100527 · Cited by 15 · see citing works

Structural Basis for the Regulation of the Mitogen-activated Protein (MAP) Kinase p38α by the Dual Specificity Phosphatase 16 MAP Kinase Binding Domain in Solution

Kumar, G. S., Zettl, H., Page, R., & Peti, W. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.499178 · Cited by 12 · see citing works

Transcriptional regulation by MAP kinases

Davis, R. (1995) · Molecular Reproduction and Development · doi:10.1002/mrd.1080420414 · Cited by 450 · see citing works

Independent Human MAP-Kinase Signal Transduction Pathways Defined by MEK and MKK Isoforms

Dérijard, B., Raingeaud, J., Barrett, T., Wu, I.-H., Han, J., Ulevitch, R. J., & Davis, R. J. (1995) · Science · doi:10.1126/science.7839144 · Cited by 1,555 · see citing works

Molecular structure of a protein-tyrosine/threonine kinase activating p42 mitogen-activated protein (MAP) kinase: MAP kinase kinase.

Wu, J., Harrison, J. K., Vincent, L. A., et al. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.1.173 · Cited by 169 · see citing works

Activation of mitogen-activated protein (MAP) kinase by a MAP kinase-kinase.

Adams, P. D., & Parker, P. J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42181-3 · Cited by 39 · see citing works

Selective Activation of p38 Mitogen-activated Protein (MAP) Kinase Isoforms by the MAP Kinase Kinases MKK3 and MKK6

Enslen, H., Raingeaud, J., & Davis, R. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.3.1741 · Cited by 534 · see citing works