NMR backbone assignment of the mitogen-activated protein (MAP) kinase p38
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The quality of 2D [1H,15N] TROSY spectra of MAPKs is significantly different from one another, with often many fewer peaks detected than expected, despite their nearly identical 3D structures.
“Interestingly, the quality of the 2D [ 1 H, 15 N] TROSY spectra of MAPKs are significantly different from one another, with often many fewer peaks detected than expected, despite their nearly identical 3D structures.58,61,65”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [61]
Sequence-specific backbone assignment has been achieved for p38a (82%), activated pTpYp38a (56%), and ERK2 (65%), including key MAPK regulatory elements.
“The basis of any NMR spectroscopy analysis is the sequence-specific backbone assignment, which has been achieved for p38a 47,58,61 (82%), activated pTpYp38a 69 (56%) and ERK2 65 (65%) and include key MAPK regulatory elements, especially the KIM binding pockets (93%/95% for p38a/ERK2) the glycine-rich loops (100%/100% for p38a/ERK2) and the activation loops (83%/none for p38a/ERK2).”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [61]
Differences in the NMR spectra of MAPKs (p38a > ERK2 > JNK1) provide the first indications that dynamics likely plays a key role in their biological function.
“The latter point seems to be especially critical for MAPKs and the differences in their NMR spectra (spectra quality of MAPKs tested by the authors is p38a>ERK2JNK1) 58,61,65 are providing the first indications that dynamics likely plays a key role in their biological function.”
From Molecular basis of MAP kinase regulation (2013) · cites this paper as [61]
Cites
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
Langer, T., Vogtherr, M., Elshorst, B., Betz, M., Schieborr, U., Saxena, K., & Schwalbe, H. (2004) · ChemBioChem · doi:10.1002/cbic.200400129 · Cited by 60 · see citing works
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Molecular basis of MAP kinase regulation
Peti, W., & Page, R. (2013) · Protein Science · doi:10.1002/pro.2374 · Cited by 302 · see citing works
“Interestingly, the quality of the 2D [(1)H,(15)N] TROSY spectra of MAPKs are significantly different from one another, with often many fewer peaks detected than expected, despite their nearly identical 3D structures.(58,61,65) Peaks in NMR spectra can be missing due to: (1) fast solvent (H2O) amide exchange on the NMR…”
BackgroundNMR 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
Self-citationStructural basis of p38α regulation by hematopoietic tyrosine phosphatase
Francis, D. M., Różycki, B., Koveal, D., Hummer, G., Page, R., & Peti, W. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.707 · Cited by 79 · see citing works
Tokunaga, Y., Takeuchi, K., Takahashi, H. K., & Shimada, I. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2861 · Cited by 50 · see citing works
X-ray structure of p38α bound to TAK-715: comparison with three classic inhibitors
Azevedo, R., van Zeeland, M., Raaijmakers, H. C. A., Kazemier, B., de Vlieg, J., & Oubrie, A. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744491201997x · Cited by 39 · see citing works
Chen, J., Wang, W., Sun, H., Pang, L., & Bao, H. (2021) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2021.104485 · Cited by 36 · see citing works
Maisonneuve, P., Caillet‐Saguy, C., Vaney, M. C., Bibi-Zainab, E., Sawyer, K. M., Raynal, B. D. E., Haouz, A., Delepierre, M., Lafon, M., Cordier, F., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.707208 · 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
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
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
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
Vogtherr, M., Saxena, K., Hoelder, S., Grimme, S., Betz, M., Schieborr, U., Pescatore, B., Robin, M. J. L., Delarbre, L., Langer, T., et al. (2005) · Angewandte Chemie · doi:10.1002/ange.200502770 · Cited by 18 · see citing works
Self-citationNMR 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
Self-citationTonelli, M., Masterson, L. R., Hallenga, K., Veglia, G., & Markley, J. L. (2007) · Journal of Biomolecular NMR · doi:10.1007/s10858-007-9185-3 · Cited by 14 · see citing works
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Peti, W., & Page, R. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-3746-2_11 · Cited by 13 · see citing works
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
Larsen, E. K., Olivieri, C., Walker, C., Subrahmanian, M. V., Gao, J., Bernlohr, D., Tonelli, M., Markley, J. L., & Veglia, G. (2018) · Molecules · doi:10.3390/molecules23081937 · Cited by 12 · see citing works
Rapid Identification of Ligand-Binding Sites by Using an Assignment-Free NMR Approach
Kodama, Y., Takeuchi, K., Shimba, N., Ishikawa, K., Suzuki, E., Shimada, I., & Takahashi, H. K. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm4014357 · Cited by 12 · see citing works
Backbone assignment of the tyrosine kinase Src catalytic domain in complex with imatinib
Campos‐Olivas, R., Marenchino, M., Scapozza, L., & Gervasio, F. L. (2011) · Biomolecular NMR Assignments · doi:10.1007/s12104-011-9304-7 · Cited by 11 · see citing works
NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1
Vajpai, N., Schott, A.-K., Vogtherr, M., & Breeze, A. L. (2013) · Biomolecular NMR Assignments · doi:10.1007/s12104-013-9458-6 · Cited by 8 · see citing works
Self-citationCumming, J. G., Debreczeni, J. E., Edfeldt, F., Evertsson, E., Harrison, M., Holdgate, G. A., James, M. J., Lamont, S. G., Oldham, K., Sullivan, J. E., et al. (2014) · Journal of Medicinal Chemistry · doi:10.1021/jm501038s · Cited by 8 · see citing works
Honndorf, V. S., Coudevylle, N., Laufer, S., Becker, S., Griesinger, C., & Habeck, M. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201105241 · Cited by 7 · 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 · doi:10.1002/ange.200705614 · Cited by 3 · see citing works
Honndorf, V. S., Coudevylle, N., Laufer, S., Becker, S., Griesinger, C., & Habeck, M. (2012) · Angewandte Chemie · doi:10.1002/ange.201105241 · Cited by 2 · see citing works
Ghouil, R., Bouguechtouli, C., Chérot, H., Marcelot, A., Roche, M., & Theillet, F. (2023) · Journal of Magnetic Resonance Open · doi:10.1016/j.jmro.2023.100126 · Cited by 2 · see citing works
Tong, M., Jeeves, M., Rajesh, S., Ludwig, C., Lenoir, M., Kumar, J., McClelland, D. M., Berditchevski, F., Hubbard, J., Kenyon, C. P., et al. (2020) · Biomolecular NMR Assignments · doi:10.1007/s12104-020-09950-x · Cited by 1 · see citing works
NMR : Applications in Chemical Biology
Nielsen, G., Stadler, M., Jonker, H. R. A., Betz, M., & Schwalbe, H. (2008) · Wiley Encyclopedia of Chemical Biology · doi:10.1002/9780470048672.wecb393 · Cited by 1 · see citing works
Self-citationChemical Biology of Kinases Studied by NMR Spectroscopy
Betz, M., Vogtherr, M., Schieborr, U., Elshorst, B., Grimme, S., Pescatore, B., Langer, T., Saxena, K., & Schwalbe, H. (2007) · Chemical biology · doi:10.1002/9783527619375.ch15b · Cited by 1 · see citing works
Self-citationStructure-based Drug Design Using NMR
Jeeves, M., Quill, L., & Overduin, M. (2015) · Encyclopedia of Magnetic Resonance · doi:10.1002/9780470034590.emrstm1430 · Cited by 1 · see citing works
Kinase and Phosphatase Signaling Enzymes: Structure and Dynamics in Solution
Peti, W., Clarkson, M. W., & Page, R. (2015) · Encyclopedia of Magnetic Resonance · doi:10.1002/9780470034590.emrstm1411
- Authors
- Vogtherr, M., Saxena, K., Grimme, S., Betz, M., Schieborr, U., Pescatore, B., Langer, T., & Schwalbe, H.
- Affiliations
- Goethe University Frankfurt (DE)
- Venue
- Journal of Biomolecular NMR
- Published
- 2005-06
- Volume
- 32
- Issue
- 2
- Pages
- 175-175
- ISSN
- 0925-2738 (ISSN-L)
- 1573-5001
- OpenAlex
- W1981416533
- Cited by
- 30
- References
- 2
- Citations by year
- 2023: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 1 · 2016: 2 · 2015: 2 · 2014: 2 · 2013: 5 · 2012: 4
- FWCI
- 1.06
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Journal of Biomolecular NMR (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- p38 MAPK, mitogen-activated protein kinase, protein backbone assignment, protein structure
- MeSH terms
- Amides, Magnetic Resonance Spectroscopy, Protein Conformation, Cyclic AMP-Dependent Protein Kinases, p38 Mitogen-Activated Protein Kinases
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