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

[20] Processing of X-ray diffraction data collected in oscillation mode

Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475 · see citing works

<i>Coot</i> : model-building tools for molecular graphics

Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571 · see citing works

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

<i>Phaser</i> crystallographic software

McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612 · see citing works

<i>PHENIX</i> : building new software for automated crystallographic structure determination

Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361 · see citing works

Mitogen-Activated Protein Kinase Pathways Mediated by ERK, JNK, and p38 Protein Kinases

Johnson, G. L., & Lapadat, R. (2002) · Science · doi:10.1126/science.1072682 · Cited by 4,295 · see citing works

Signal transduction by the JNK group of MAP kinases

Davis, R. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00116-1 · Cited by 4,237 · see citing works

ERK and p38 MAPK-Activated Protein Kinases: a Family of Protein Kinases with Diverse Biological Functions

Roux, P. P., & Blenis, J. (2004) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.68.2.320-344.2004 · Cited by 2,494 · 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

[1] Assays of protein kinase

Roskoski, R. J. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(83)99034-1 · Cited by 831 · 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

Differential regulation of MAP kinase signalling by dual-specificity protein phosphatases

Owens, D. M., & Keyse, S. M. (2007) · Oncogene · doi:10.1038/sj.onc.1210412 · Cited by 777 · see citing works

A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems.

Webb, M. (1992) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.89.11.4884 · Cited by 540 · see citing works

Structure and regulation of MAPK phosphatases

Farooq, A., & Zhou, M. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2003.12.008 · Cited by 452 · 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

The Dual Specificity Phosphatases M3/6 and MKP-3 Are Highly Selective for Inactivation of Distinct Mitogen-activated Protein Kinases

Muda, M., Theodosiou, A. M., Rodrigues, N. R., Boschert, U., Camps, M., Gilliéron, C., Davies, K. E., Ashworth, A., & Arkinstall, S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27205 · Cited by 375 · see citing works

MAP kinase phosphatases.

Theodosiou, A. M., & Ashworth, A. (2002) · Genome biology · doi:10.1186/gb-2002-3-7-reviews3009 · Cited by 321 · 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

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

MAP kinase pathways: The first twenty years

Avruch, J. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.11.006 · Cited by 283 · 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 · 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

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

p38 Pathway Kinases as Anti-inflammatory Drug Targets

Schindler, J. F., Monahan, J. B., & Smith, W. G. (2007) · Journal of Dental Research · doi:10.1177/154405910708600902 · Cited by 228 · see citing works

Molecular Cloning and Characterization of a Novel Dual Specificity Phosphatase, MKP-5

Tanoue, T., Moriguchi, T., & Nishida, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19949 · Cited by 225 · see citing works

Mechanisms of MAPK signalling specificity

Bardwell, L. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340837 · Cited by 213 · see citing works

A Novel MAPK Phosphatase MKP-7 Acts Preferentially on JNK/SAPK and p38α and β MAPKs

Tanoue, T., Yamamoto, T., Maeda, R., & Nishida, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101981200 · Cited by 165 · see citing works

Docking Interactions Induce Exposure of Activation Loop in the MAP Kinase ERK2

Zhou, T., Sun, L., Humphreys, J., & Goldsmith, E. J. (2006) · Structure · doi:10.1016/j.str.2006.04.006 · Cited by 164 · see citing works

Novel strategies for inhibition of the p38 MAPK pathway

ZHANG, J., SHEN, B., & Lin, A. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.04.008 · Cited by 162 · 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

MKP-7, a Novel Mitogen-activated Protein Kinase Phosphatase, Functions as a Shuttle Protein

Masuda, K., Shima, H., Watanabe, M., & Kikuchi, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104600200 · Cited by 151 · see citing works

Mitogen-activated protein kinases as therapeutic targets in osteoarthritis

Loeser, R. F., Erickson, E. A., & Long, D. L. (2008) · Current Opinion in Rheumatology · doi:10.1097/bor.0b013e3283090463 · Cited by 147 · see citing works

MKP5, a new member of the MAP kinase phosphatase family, which selectively dephosphorylates stress-activated kinases

Theodosiou, A. M., Smith, A., Gillieron, C., Arkinstall, S., & Ashworth, A. (1999) · Oncogene · doi:10.1038/sj.onc.1203185 · Cited by 145 · see citing works

Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3

Liu, S., Sun, J.-P., Zhou, B., & Zhang, Z.-Y. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510506103 · Cited by 140 · see citing works

New Approaches to the Treatment of Inflammatory Disorders Small Molecule inhibitors of p38 MAP Kinase

Peifer, C., Wagner, G. K., & Laufer, S. (2006) · Current Topics in Medicinal Chemistry · doi:10.2174/156802606775270323 · Cited by 127 · see citing works

Solution Structure of ERK2 Binding Domain of MAPK Phosphatase MKP-3

Farooq, A., Chaturvedi, G., Mujtaba, S., Plotnikova, O., Zeng, L., Dhalluin, C., Ashton, R., & Zhou, M.-M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00186-1 · Cited by 119 · 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

Crystal Structure of the P38α-MAPKAP Kinase 2 Heterodimer

Haar, E. T., Prabakhar, P., Liu, X., & Lepre, C. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611165200 · Cited by 100 · see citing works

Enzymatic Activity and Substrate Specificity of Mitogen-activated Protein Kinase p38α in Different Phosphorylation States

Zhang, Y., Mei, Z., Wu, J., & Wang, Z. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801703200 · Cited by 84 · see citing works

Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5

Tao, X., & Tong, L. (2007) · Protein Science · doi:10.1110/ps.062712807 · Cited by 31 · see citing works

A Continuous Spectrophotometric Method for the Determination of Glycogen Phosphorylase-Catalyzed Reaction in the Direction of Glycogen Synthesis

Sergienko, E. A., & Srivastava, D. K. (1994) · Analytical Biochemistry · doi:10.1006/abio.1994.1424 · Cited by 28 · see citing works

A Continuous Spectrophotometric Assay for Protein Phosphatases

Cheng, Q., Wang, Z. X., & Killilea, S. D. (1995) · Analytical Biochemistry · doi:10.1006/abio.1995.1192 · Cited by 24 · see citing works

Dual‐specificity MAP kinase phosphatases (MKPs): Shaping the outcome of MAP kinase signalling

Caunt, C. J., & Keyse, S. M. (2013) · The FEBS Journal · doi:10.1111/j.1742-4658.2012.08716.x · Cited by 535 · see citing works

JNK Signaling: Regulation and Functions Based on Complex Protein-Protein Partnerships

Zeke, A., Misheva, M., Reményi, A., & Bogoyevitch, M. A. (2016) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00043-14 · Cited by 524 · 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

A Toxoplasma dense granule protein, GRA24, modulates the early immune response to infection by promoting a direct and sustained host p38 MAPK activation

Braun, L., Brenier‐Pinchart, M., Yogavel, M., Curt, A., Bertini, R., Hussain, T., Kieffer‐Jaquinod, S., Couté, Y., Pelloux, H., Tardieux, I., et al. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20130103 · Cited by 274 · see citing works

Dual-Specificity Phosphatases in Immunity and Infection: An Update

Lang, R., & Raffi, F. A. M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20112710 · Cited by 153 · see citing works

Diversity and specificity of the mitogen-activated protein kinase phosphatase-1 functions

Lawan, A., Shi, H., Gatzke, F., & Bennett, A. M. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1041-2 · Cited by 81 · see citing works

The Dual-Specificity Phosphatase 10 (DUSP10): Its Role in Cancer, Inflammation, and Immunity

Jiménez-Martínez, M., Stamatakis, K., & Fresno, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20071626 · Cited by 78 · see citing works

New Therapeutic Targets in Cardiology

Martin, E. D., Nicola, G. F. D., & Marber, M. S. (2012) · Circulation · doi:10.1161/circulationaha.111.071886 · Cited by 77 · see citing works

Revisiting protein kinase–substrate interactions: Toward therapeutic development

de Oliveira, P. S. L., Ferraz, F. A. N., Pena, D. A., Pramio, D. T., Morais, F. A., & Schechtman, D. (2016) · Science Signaling · doi:10.1126/scisignal.aad4016 · Cited by 68 · see citing works

Systematic discovery of linear binding motifs targeting an ancient protein interaction surface on MAP kinases

Zeke, A., Bastys, T., Alexa, A., Garai, Á., Mészáros, B., Kirsch, K., Dosztányi, Z., Kalinina, O. V., & Reményi, A. (2015) · Molecular Systems Biology · doi:10.15252/msb.20156269 · Cited by 66 · see citing works

Changes in the free-energy landscape of p38α MAP kinase through its canonical activation and binding events as studied by enhanced molecular dynamics simulations

Kuzmanic, A., Sutto, L., Saladino, G., Nebreda, Á. R., Gervasio, F. L., & Orozco, M. (2017) · eLife · doi:10.7554/elife.22175 · Cited by 64 · see citing works

A conserved motif in JNK/p38-specific MAPK phosphatases as a determinant for JNK1 recognition and inactivation

Liu, X., Zhang, C., Lu, C., Lin, S., Wu, J., & Wang, Z. (2016) · Nature Communications · doi:10.1038/ncomms10879 · Cited by 55 · see citing works

The family-wide structure and function of human dual-specificity protein phosphatases

Jeong, D. G., Wei, C. H., Ku, B., Jeon, T. J., Chien, P. N., Kim, J. K., Park, S. Y., Hwang, H. S., Ryu, S. Y., Park, H., et al. (2014) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004713029866 · Cited by 50 · see citing works

Architecture of the MKK6-p38α complex defines the basis of MAPK specificity and activation

Juyoux, P., Galdadas, I., Gobbo, D., von Velsen, J., Pelosse, M., Tully, M. D., Vadas, O., Gervasio, F. L., Pellegrini, E., & Bowler, M. W. (2023) · Science · doi:10.1126/science.add7859 · Cited by 49 · see citing works

Dual-Specificity Phosphatase 12 Targets p38 MAP Kinase to Regulate Macrophage Response to Intracellular Bacterial Infection

Cho, S. L. S., Han, J., James, S. J., Png, C. W., Weerasooriya, M., Alonso, S., & Zhang, Y. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01259 · Cited by 44 · see citing works

An in vitro attempt at precision toxicology reveals the involvement of DNA methylation alteration in ochratoxin A-induced G0/G1 phase arrest

Zhang, B., Zhu, L., Dai, Y., Li, H., Huang, K., Luo, Y., & Xu, W. (2019) · Epigenetics · doi:10.1080/15592294.2019.1644878 · Cited by 41 · see citing works

Expanding the horizons of microRNA bioinformatics

Huntley, R. P., Kramarz, B., Sawford, T., Umrao, Z., Kalea, A. Z., Acquaah, V., Martin, M. J., Mayr, M., & Lovering, R. C. (2018) · RNA · doi:10.1261/rna.065565.118 · Cited by 36 · see citing works

Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs

Kliche, J., & Ivarsson, Y. (2022) · Biochemical Journal · doi:10.1042/bcj20200714 · Cited by 34 · see citing works

Predicted mechanistic impacts of human protein missense variantsPreprint

Jänes, J., Müller, M., Selvaraj, S., Manoel, D., Stephenson, J. D., Gonçalves, C. I., Lafita, A., Polacco, B. J., Obernier, K., Alasoo, K., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.29.596373 · Cited by 26 · see citing works

A High-throughput Assay for Phosphoprotein-specific Phosphatase Activity in Cellular Extracts

Bose, A. K., & Janes, K. A. (2012) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o112.024059 · Cited by 26 · see citing works

p38α Mitogen-Activated Protein Kinase Is a Druggable Target in Pancreatic Adenocarcinoma

Yang, L., Sun, X., Ye, Y., Lu, Y., Zuo, J., Liu, W., Elcock, A. H., & Zhu, S. N. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01294 · Cited by 25 · see citing works

MAP Kinase Modules: The Excursion Model and the Steps that Count

Piala, A. T., Humphreys, J. M., & Goldsmith, E. J. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.09.024 · Cited by 24 · see citing works

Functional divergence caused by mutations in an energetic hotspot in ERK2

Taylor, C. A., Cormier, K. W., Keenan, S. E., Earnest, S. A., Stippec, S., Wichaidit, C., Juang, Y.-C. A., Wang, J., Shvartsman, S. Y., Goldsmith, E. J., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1905015116 · Cited by 23 · see citing works

STYXL1 regulates CCT complex assembly and flagellar tubulin folding in sperm formation

Chen, Y., Luo, M., Tu, H.-X., Qi, Y.-L., Guo, Y.-S., Zhang, X.-Z., Cui, Y., Gao, M.-M., Zhou, X., Zhu, T., et al. (2024) · Nature Communications · doi:10.1038/s41467-023-44337-1 · Cited by 22 · see citing works

An allosteric site on MKP5 reveals a strategy for small-molecule inhibition

Gannam, Z. T. K., Min, K., Shillingford, S. R., Zhang, L., Herrington, J. B., Abriola, L., Gareiss, P. C., Pantouris, G., Tzouvelekis, A., Kaminski, N., et al. (2020) · Science Signaling · doi:10.1126/scisignal.aba3043 · Cited by 21 · see citing works

Functional interrogation and therapeutic targeting of protein tyrosine phosphatases

Krabill, A. D., & Zhang, Z. (2021) · Biochemical Society Transactions · doi:10.1042/bst20201308 · Cited by 20 · see citing works

Docking Interactions of Hematopoietic Tyrosine Phosphatase with MAP Kinases ERK2 and p38α

Piserchio, A., Francis, D. M., Koveal, D., Dalby, K. N., Page, R., Peti, W., & Ghose, R. (2012) · Biochemistry · doi:10.1021/bi3012725 · Cited by 19 · see citing works

Proteome-wide screening for mitogen-activated protein kinase docking motifs and interactors

Shi, G., Song, C. D., Robles, J. T., Salichos, L., Lou, H. J., Lam, T. T., Gerstein, M., & Turk, B. E. (2023) · Science Signaling · doi:10.1126/scisignal.abm5518 · Cited by 19 · see citing works

Rat ERK2 E320K

th, C. A. T., Cormier, K. W., Juang, Y.-C., Goldsmith, E. J., & Cobb, M. H. (2019) · Worldwide Protein Data Bank · doi:10.2210/pdb6ots/pdb · Cited by 18 · see citing works

Interaction of Kinase-Interaction-Motif Protein Tyrosine Phosphatases with the Mitogen-Activated Protein Kinase ERK2

Francis, D. M., Koveal, D., Tortajada, A., Page, R., & Peti, W. (2014) · PLoS ONE · doi:10.1371/journal.pone.0091934 · Cited by 16 · see citing works

A novel retro-inverso peptide is a preferential JNK substrate-competitive inhibitor

Ngoei, K. R. W., Catimel, B., Milech, N., Watt, P. M., & Bogoyevitch, M. A. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.06.006 · Cited by 16 · 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

Structure of human dual-specificity phosphatase 7, a potential cancer drug target

Lountos, G. T., Austin, B. P., Tropea, J. E., & Waugh, D. S. (2015) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x1500504x · Cited by 14 · see citing works

Profiling Subcellular Protein Phosphatase Responses to Coxsackievirus B3 Infection of Cardiomyocytes

Shah, M., Smolko, C. M., Kinicki, S., Chapman, Z. D., Brautigan, D. L., & Janes, K. A. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o116.063487 · Cited by 14 · see citing works

Kinetic and mechanistic studies of p38α MAP kinase phosphorylation by MKK 6

Wang, Y., Zhang, Y., Lu, C., Zhang, W., Deng, H., Wu, J., Wang, J., & Wang, Z. (2019) · FEBS Journal · doi:10.1111/febs.14762 · Cited by 12 · see citing works

Not your Mother’s MAPKs: Apicomplexan MAPK function in daughter cell budding

O’Shaughnessy, W. J., Dewangan, P. S., Paiz, E. A., & Reese, M. L. (2022) · PLoS Pathogens · doi:10.1371/journal.ppat.1010849 · Cited by 10 · see citing works

Three-dimensional docking in the MAPK p38α

Goldsmith, E. J. (2011) · Science Signaling · doi:10.1126/scisignal.2002697 · Cited by 8 · see citing works

Linear motif specificity in signaling through p38α and ERK2 mitogen–activated protein kinases

Robles, J. T., Lou, H. J., Shi, G., Pan, P. L., & Turk, B. E. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2316599120 · Cited by 7 · see citing works

Effects of methylation of deiodinase 3 gene on gene expression and severity of Kashin–Beck disease

Li, Z., Zhang, D., Li, Q., Yang, X., Zhang, R., Zhang, D., Yang, X., Wang, C., Tan, X., & Xiong, Y. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.29809 · Cited by 8 · see citing works

De novo germline mutation in the dual specificity phosphatase 10 gene accelerates autoimmune diabetes

Foray, A., Candon, S., Hildebrand, S., Marquet, C., Valette, F., Pecquet, C., Lemoine, S., Vives, F. L., Dumas, M., Hu, P., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2112032118 · Cited by 7 · see citing works

Label Transfer Reagents to Probe p38 MAPK Binding Partners

Andrews, S., Hill, Z. B., Perera, B. G. K., & Maly, D. J. (2013) · ChemBioChem · doi:10.1002/cbic.201200673 · Cited by 6 · see citing works

Dynamic and structural insights into allosteric regulation on MKP5 a dual-specificity phosphatase

Skeens, E., Maschietto, F., Manjula, R., Shillingford, S. R., Murphy, J., Lolis, E., Batista, V. S., Bennett, A. M., & Lisi, G. P. (2025) · Nature Communications · doi:10.1038/s41467-025-62150-w · Cited by 5 · see citing works

Cancer hotspot mutations rewire ERK2 specificity by selective exclusion of docking interactions

Robles, J. T., Stiegler, A. L., Boggon, T. J., & Turk, B. E. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108348 · Cited by 5 · see citing works

Structural analysis of dual specificity phosphatases, the only type of protein tyrosine phosphatases found in humans and across diverse microorganisms

Ku, B. (2025) · The Journal of Microbiology · doi:10.71150/jm.2506006 · Cited by 3 · see citing works

Mitogen-Activated Protein Kinase Phosphatases in Metabolism

Lawan, A., & Bennett, A. M. (2013) · Springer eBooks · doi:10.1007/978-1-4614-7855-3_12 · Cited by 2 · see citing works

BCI inhibits MKP3 by targeting the kinase-binding domain and disrupting ERK2 interaction

Qiu, S.-J., Zhang, Y., Gong, W., Ding, Y.-H., Wu, J., Wang, Z., & Yao, H. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110570 · Cited by 1 · see citing works

MAP Kinase Modules in Signaling☆

Elion, E. A. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-801238-3.98742-7 · Cited by 1 · see citing works

De novo germline mutation in the Dual Specificity Phosphatase 10 gene accelerates autoimmune diabetes in Non-Obese Diabetic (NOD) micePreprint

Foray, A., Candon, S., Hildebrand, S., Marquet, C., Valette, F., Pecquet, C., Lemoine, S., Vives, F. L., Dumas, M., Hu, P., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.30.424747

1H, 15N and 13C sequence specific backbone assignment of the MAP kinase binding domain of the dual specificity phosphatase 1 and its interaction with the MAPK p38

Kumar, G. S., Page, R., & Peti, W. (2021) · Biomolecular NMR Assignments · doi:10.1007/s12104-021-10012-z

Non-canonical interactions of the Mitogen Activated Protein (MAP) kinases

Kirsch, K. P. (2021) · Eötvös Loránd Tudományegyetem · doi:10.15476/elte.2021.040

Rare genetic variants affect course of autoimmune diabetes : impact on immunotherapy sensitivity

Hu, P. (2024) · theses.fr (ABES) · doi:10.70675/f76ba1c9z523cz4c73z9d2bzfbd00b292ba8

Structural and dynamic insights into the allosteric activation of p38α MAP kinase via specific docking interactions

Zhang, Y., Pei, C.-J., Luo, Z., Zhu, Z., Wu, J., & Wang, Z. (2026) · Communications Biology · doi:10.1038/s42003-026-10502-7

STELLAR: A Fragment-Based Docking Workflow for Highly Flexible Long-Chain Biopolymers

Martínez, A. R., Nelen, J., Carmena‐Bargueño, M., Martínez-Cortés, C., & Pérez‐Sánchez, H. (2026) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6c00987

Three-dimensional docking in the MAPK p38α

Goldsmith, E. J. (2011) · Science Signaling · doi:10.1126/scisignal.2002697 · Cited by 8 · see citing works

Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5

Tao, X., & Tong, L. (2007) · Protein Science · doi:10.1110/ps.062712807 · Cited by 31 · 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

Structural and dynamic insights into the allosteric activation of p38α MAP kinase via specific docking interactions

Zhang, Y., Pei, C.-J., Luo, Z., Zhu, Z., Wu, J., & Wang, Z. (2026) · Communications Biology · doi:10.1038/s42003-026-10502-7

Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3

Liu, S., Sun, J.-P., Zhou, B., & Zhang, Z.-Y. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510506103 · Cited by 140 · see citing works