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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, Wendt KU, Schwalbe H
Angew Chem Int Ed Engl 45 993-7 (2006)
Cited: 75 times
EuropePMC logo PMID: 16374788

Articles - 2ewa mentioned but not cited (8)

  1. Dynamics of protein kinases: insights from nuclear magnetic resonance. Xiao Y, Liddle JC, Pardi A, Ahn NG. Acc Chem Res 48 1106-1114 (2015)
  2. Fluorophore labeled kinase detects ligands that bind within the MAPK insert of p38α kinase. Getlik M, Simard JR, Termathe M, Grütter C, Rabiller M, van Otterlo WA, Rauh D. PLoS One 7 e39713 (2012)
  3. Accurate calculation of mutational effects on the thermodynamics of inhibitor binding to p38α MAP kinase: a combined computational and experimental study. Zhu S, Travis SM, Elcock AH. J Chem Theory Comput 9 3151-3164 (2013)
  4. Kinase Inhibitory Activities and Molecular Docking of a Novel Series of Anticancer Pyrazole Derivatives. Nossier ES, Abd El-Karim SS, Khalifa NM, El-Sayed AS, Hassan ESI, El-Hallouty SM. Molecules 23 E3074 (2018)
  5. 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, Zhu S. Front Oncol 9 1294 (2019)
  6. Virtual screening using a conformationally flexible target protein: models for ligand binding to p38α MAPK. Vinh NB, Simpson JS, Scammells PJ, Chalmers DK. J Comput Aided Mol Des 26 409-423 (2012)
  7. Design, Synthesis, and Biological Evaluation of Tetra-Substituted Thiophenes as Inhibitors of p38α MAPK. Vinh NB, Devine SM, Munoz L, Ryan RM, Wang BH, Krum H, Chalmers DK, Simpson JS, Scammells PJ. ChemistryOpen 4 56-64 (2015)
  8. Structural basis of a redox-dependent conformational switch that regulates the stress kinase p38α. Pous J, Baginski B, Martin-Malpartida P, González L, Scarpa M, Aragon E, Ruiz L, Mees RA, Iglesias-Fernández J, Orozco M, Nebreda AR, Macias MJ. Nat Commun 14 7920 (2023)


Reviews citing this publication (10)

  1. Molecular basis of MAP kinase regulation. Peti W, Page R. Protein Sci 22 1698-1710 (2013)
  2. New therapeutic targets in cardiology: p38 alpha mitogen-activated protein kinase for ischemic heart disease. Denise Martin E, De Nicola GF, Marber MS. Circulation 126 357-368 (2012)
  3. Proteus in the world of proteins: conformational changes in protein kinases. Rabiller M, Getlik M, Klüter S, Richters A, Tückmantel S, Simard JR, Rauh D. Arch Pharm (Weinheim) 343 193-206 (2010)
  4. Investigating metabolite-protein interactions: an overview of available techniques. Yang GX, Li X, Snyder M. Methods 57 459-466 (2012)
  5. Design principles underpinning the regulatory diversity of protein kinases. Oruganty K, Kannan N. Philos Trans R Soc Lond B Biol Sci 367 2529-2539 (2012)
  6. Single versus dual-binding conformations in cellulosomal cohesin-dockerin complexes. Nash MA, Smith SP, Fontes CM, Bayer EA. Curr Opin Struct Biol 40 89-96 (2016)
  7. Biomolecular NMR: a chaperone to drug discovery. Betz M, Saxena K, Schwalbe H. Curr Opin Chem Biol 10 219-225 (2006)
  8. Studies of metabolite-protein interactions: a review. Matsuda R, Bi C, Anguizola J, Sobansky M, Rodriguez E, Vargas Badilla J, Zheng X, Hage B, Hage DS. J Chromatogr B Analyt Technol Biomed Life Sci 966 48-58 (2014)
  9. Computational insights for the discovery of non-ATP competitive inhibitors of MAP kinases. Schnieders MJ, Kaoud TS, Yan C, Dalby KN, Ren P. Curr Pharm Des 18 1173-1185 (2012)
  10. Probing Protein-Protein Interactions Using Asymmetric Labeling and Carbonyl-Carbon Selective Heteronuclear NMR Spectroscopy. Larsen EK, Olivieri C, Walker C, V S M, Gao J, Bernlohr DA, Tonelli M, Markley JL, Veglia G. Molecules 23 E1937 (2018)

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  6. NMR reveals the allosteric opening and closing of Abelson tyrosine kinase by ATP-site and myristoyl pocket inhibitors. Skora L, Mestan J, Fabbro D, Jahnke W, Grzesiek S. Proc Natl Acad Sci U S A 110 E4437-45 (2013)
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  8. Structural basis of p38α regulation by hematopoietic tyrosine phosphatase. Francis DM, Różycki B, Koveal D, Hummer G, Page R, Peti W. Nat Chem Biol 7 916-924 (2011)
  9. A potent and selective p38 inhibitor protects against bone damage in murine collagen-induced arthritis: a comparison with neutralization of mouse TNFalpha. Mihara K, Almansa C, Smeets RL, Loomans EE, Dulos J, Vink PM, Rooseboom M, Kreutzer H, Cavalcanti F, Boots AM, Nelissen RL. Br J Pharmacol 154 153-164 (2008)
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  18. Contributions of water transfer energy to protein-ligand association and dissociation barriers: Watermap analysis of a series of p38α MAP kinase inhibitors. Pearlstein RA, Sherman W, Abel R. Proteins 81 1509-1526 (2013)
  19. Elucidation of a four-site allosteric network in fibroblast growth factor receptor tyrosine kinases. Chen H, Marsiglia WM, Cho MK, Huang Z, Deng J, Blais SP, Gai W, Bhattacharya S, Neubert TA, Traaseth NJ, Mohammadi M. Elife 6 e21137 (2017)
  20. Insights from free-energy calculations: protein conformational equilibrium, driving forces, and ligand-binding modes. Huang YM, Chen W, Potter MJ, Chang CE. Biophys J 103 342-351 (2012)
  21. Predicting the Conformational Variability of Abl Tyrosine Kinase using Molecular Dynamics Simulations and Markov State Models. Meng Y, Gao C, Clawson DK, Atwell S, Russell M, Vieth M, Roux B. J Chem Theory Comput 14 2721-2732 (2018)
  22. Dynamics of human protein kinase Aurora A linked to drug selectivity. Pitsawong W, Buosi V, Otten R, Agafonov RV, Zorba A, Kern N, Kutter S, Kern G, Pádua RA, Meniche X, Kern D. Elife 7 e36656 (2018)
  23. Developing small molecules to inhibit kinases unkind to the heart: p38 MAPK as a case in point. Marber MS, Molkentin JD, Force T. Drug Discov Today Dis Mech 7 e123-e127 (2010)
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