Perturbation of the conformational equilibria in Ras by selective mutations as studied by 31P NMR spectroscopy
Open accessAbstract
Ras regulates a variety of different signal transduction pathways acting as molecular switch. It was shown by liquid and solid‐state 31 P NMR spectroscopy that Ras exists in the guanosine‐5′‐(β,γ‐imido)triphosphate bound form in at least two conformational states interconverting in millisecond time scale. The relative population between the two conformational states affects drastically the affinity of Ras to its effectors. 31 P NMR spectroscopy shows that the conformational equilibrium can be shifted specifically by point mutations, including mutations with oncogenic potential, thus modifying the effector interactions and their coupling to dynamic properties of the protein.
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Additional biochemical, structural, and signaling distinctions have been identified between different mutant KRAS alleles, including between those at the same amino acid position.
“Additional biochemical, structural, and signaling distinctions have been identified between different mutant alleles, including between those at the same amino acid position4,8,13–20.”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [18]
Switch-I displays highly dynamic characteristics manifested as two different states when GTP is bound to RAS, and the distribution between these states is altered in mutants.
“Overall, switch-I displays highly dynamic characteristics manifested as two different states when GTP is bound to RAS, and the distribution between these states is altered in mutants [19–22].”
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Cites
Computer-optimized decoupling scheme for wideband applications and low-level operation
Shaka, A. J., Barker, P. B., & Freeman, R. (1985) · Journal of Magnetic Resonance (1969) · doi:10.1016/0022-2364(85)90122-2 · Cited by 1,114 · see citing works
Nassar, N. N., Horn, G., Herrmann, C., Scherer, A., McCormick, F. P., & Wittinghofer, A. (1995) · Nature · doi:10.1038/375554a0 · Cited by 631 · see citing works
Self-citationKinetics of interaction of nucleotides with nucleotide-free H-ras p21
John, J., Sohmen, R., Feuerstein, J., Linke, R., Wittinghofer, A., & Goody, R. S. (1990) · Biochemistry · doi:10.1021/bi00477a025 · Cited by 429 · see citing works
Self-citationCalibration of methanol and ethylene glycol nuclear magnetic resonance thermometers
Raiford, D. S., Fisk, C. L., & Becker, E. D. (1979) · Analytical Chemistry · doi:10.1021/ac50048a040 · Cited by 378 · see citing works
Herrmann, C., Martin, G. A., & Wittinghofer, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.7.2901 · Cited by 350 · see citing works
Self-citationDynamic properties of the Ras switch I region and its importance for binding to effectors
Spoerner, M., Herrmann, C., Vetter, I. R., Kalbitzer, H. R., & Wittinghofer, A. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081441398 · Cited by 324 · see citing works
Self-citationExpression of p21 proteins in Escherichia coli and stereochemistry of the nucleotide‐binding site.
Tucker, J., Sczakiel, G., Feuerstein, J., John, J., Goody, R. S., & Wittinghofer, A. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04366.x · Cited by 285 · see citing works
Self-citationKraulis, P. J., Domaille, P. J., Campbell, S. L., Aken, T. V., & Laue, E. D. (1994) · Biochemistry · doi:10.1021/bi00178a008 · Cited by 267 · see citing works
Geyer, M., Schweins, T., Herrmann, C., Prisner, T. F., Wittinghofer, A., & Kalbitzer, H. R. (1996) · Biochemistry · doi:10.1021/bi952858k · Cited by 227 · see citing works
Self-citationRas/Rap effector specificity determined by charge reversal
Nassar, N. N., Horn, G., Herrmann, C., Block, C., Janknecht, R., & Wittinghofer, A. (1996) · Nature Structural & Molecular Biology · doi:10.1038/nsb0896-723 · Cited by 214 · see citing works
Self-citationRegional Polysterism in the GTP-Bound Form of the Human c-Ha-Ras Protein,
Ito, Y., Yamasaki, K., Iwahara, J., Terada, T., Kamiya, A., Shirouzu, M., Muto, Y., Kawai, G., Yokoyama, S., Laue, E. D., et al. (1997) · Biochemistry · doi:10.1021/bi970296u · Cited by 163 · see citing works
Linnemann, T., Geyer, M., Jaitner, B. K., Block, C., Kalbitzer, H. R., Wittinghofer, A., & Herrmann, C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13556 · Cited by 133 · see citing works
Self-citationStructure of the Ras-binding domain of RalGEF and implications for Ras binding and signalling
Geyer, M., Herrmann, C., Wohlgemuth, S., Wittinghofer, A., & Kalbitzer, H. R. (1997) · Nature Structural Biology · doi:10.1038/nsb0997-694 · Cited by 123 · see citing works
Self-citationC-terminal Truncation of p21H Preserves Crucial Kinetic and Structural Properties
John, J., Schlichting, I., SCHILTZ, E., ROSCH, P. J., & Wittinghofer, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)51599-4 · Cited by 111 · see citing works
Self-citationStructural and biochemical analysis of Ras‐effector signaling via RalGDS
Vetter, I. R., Linnemann, T., Wohlgemuth, S., Geyer, M., Kalbitzer, H. R., Herrmann, C., & Wittinghofer, A. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00555-4 · Cited by 103 · see citing works
Self-citationSpoerner, M., Nuehs, A., Ganser, P., Herrmann, C., Wittinghofer, A., & Kalbitzer, H. R. (2005) · Biochemistry · doi:10.1021/bi0488000 · Cited by 89 · see citing works
Self-citationIndirect Referencing of31P and19F NMR Spectra
Maurer, T., & Kalbitzer, H. R. (1996) · Journal of Magnetic Resonance Series B · doi:10.1006/jmrb.1996.0172 · Cited by 62 · see citing works
Self-citationGronwald, W., Huber, F., Grünewald, P., Spoerner, M., Wohlgemuth, S., Herrmann, C., & Kalbitzer, H. R. (2001) · Structure · doi:10.1016/s0969-2126(01)00671-2 · Cited by 55 · see citing works
Self-citationStumber, M., Geyer, M., Graf, R., Robert Kalbitzer, H., Scheffzek, K., & Haeberlen, U. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01010-0 · Cited by 22 · see citing works
Self-citationIndirect Referencing of ³¹P and ¹⁹F NMR Spectra
Maurer, T., & Kalbitzer, H. R. (1996) · University of Regensburg Publication Server (University of Regensburg) · Cited by 3 · see citing works
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Ras Conformational Ensembles, Allostery, and Signaling
Lu, S., Jang, H., Muratcioglu, S., Gursoy, A., Keskin, O., Nussinov, R., & Zhang, J. (2016) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00542 · Cited by 355 · see citing works
Mazhab-Jafari, M. T., Marshall, C. B., Smith, M. J., Gasmi-Seabrook, G. M. C., Stathopulos, P. B., Inagaki, F., Kay, L. E., Neel, B. G., & Ikura, M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1419895112 · Cited by 220 · see citing works
Mapping the Nucleotide and Isoform-Dependent Structural and Dynamical Features of Ras Proteins
Gorfe, A. A., Grant, B. J., & McCammon, J. A. (2008) · Structure · doi:10.1016/j.str.2008.03.009 · Cited by 216 · see citing works
Small-molecule modulation of Ras signaling
Spiegel, J., Cromm, P. M., Zimmermann, G., Grossmann, T. N., & Waldmann, H. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1560 · Cited by 215 · see citing works
The origins and genetic interactions of KRAS mutations are allele- and tissue-specific
Cook, J. H., Melloni, G. E. M., Gulhan, D. C., Park, P. J., & Haigis, K. M. (2021) · Nature Communications · doi:10.1038/s41467-021-22125-z · Cited by 208 · see citing works
Gorfe, A. A., Hanzal‐Bayer, M., Abankwa, D., Hancock, J. F., & McCammon, J. A. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm061053f · Cited by 209 · see citing works
Spoerner, M., Hozsa, C., Poetzl, J. A., Reiss, K., Ganser, P., Geyer, M., & Kalbitzer, H. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145235 · Cited by 148 · see citing works
Self-citationStructural Basis for Conformational Dynamics of GTP-bound Ras Protein
Shima, F., Ijiri, Y., Muraoka, S., Liao, J., Ye, M., Araki, M., Matsumoto, K., Yamamoto, N., Sugimoto, T., Yoshikawa, Y., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.125161 · Cited by 148 · see citing works
Drewry, J. A., & Gunning, P. T. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.10.018 · Cited by 145 · see citing works
Andrographolide derivatives inhibit guanine nucleotide exchange and abrogate oncogenic Ras function
Hocker, H. J., Cho, K.-J., Chen, C.-Y. K., Rambahal, N., Sagineedu, S. R., Shaari, K., Stanslas, J., Hancock, J. F., & Gorfe, A. A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300016110 · Cited by 144 · see citing works
Chen, J., Zhang, S., Wang, W., Pang, L., Zhang, Q., & Liu, X. (2021) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c01470 · Cited by 140 · see citing works
Ras Binder Induces a Modified Switch-II Pocket in GTP and GDP States
Gentile, D. R., Rathinaswamy, M. K., Jenkins, M. L., Moss, S. M., Siempelkamp, B. D., Renslo, A. R., Burke, J. E., & Shokat, K. M. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.08.025 · Cited by 111 · see citing works
Stabilizing a Weak Binding State for Effectors in the Human Ras Protein by Cyclen Complexes
Rosnizeck, I. C., Gräf, T., Spoerner, M., Traenkle, J., Filchtinski, D., Herrmann, C., Gremer, L., Vetter, I. R., Wittinghofer, A., König, B., et al. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.200907002 · Cited by 107 · see citing works
Self-citationAraki, M., Shima, F., Yoshikawa, Y., Muraoka, S., Ijiri, Y., Nagahara, Y., Shirono, T., Kataoka, T., & Tamura, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.227074 · Cited by 105 · see citing works
Integrated RAS signaling defined by parallel NMR detection of effectors and regulators
Smith, M. J., & Ikura, M. (2014) · Nature Chemical Biology · doi:10.1038/nchembio.1435 · Cited by 87 · see citing works
Pantsar, T., Rissanen, S., Dauch, D., Laitinen, T., Vattulainen, I., & Poso, A. (2018) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1006458 · Cited by 85 · see citing works
Muraoka, S., Shima, F., Araki, M., Inoue, T., Yoshimoto, A., Ijiri, Y., Seki, N., Tamura, A., Kumasaka, T., Yamamoto, M., et al. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.04.058 · Cited by 81 · see citing works
Direct Modulation of Small GTPase Activity and Function
Cromm, P. M., Spiegel, J., Grossmann, T. N., & Waldmann, H. (2015) · Angewandte Chemie International Edition · doi:10.1002/anie.201504357 · Cited by 78 · see citing works
Global Conformational Dynamics in Ras
O’Connor, C., & Kovrigin, E. L. (2008) · Biochemistry · doi:10.1021/bi801076c · Cited by 74 · see citing works
Two conformational states of Ras GTPase exhibit differential GTP-binding kinetics
Liao, J., Shima, F., Araki, M., Ye, M., Muraoka, S., Sugimoto, T., Kawamura, M., Yamamoto, N., Tamura, A., & Kataoka, T. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.01.169 · Cited by 68 · see citing works
Metal–Bis(2‐picolyl)amine Complexes as State 1(T) Inhibitors of Activated Ras Protein
Rosnizeck, I. C., Spoerner, M., Harsch, T., Kreitner, S., Filchtinski, D., Herrmann, C., Engel, D., König, B., & Kalbitzer, H. R. (2012) · Angewandte Chemie International Edition · doi:10.1002/anie.201204148 · Cited by 65 · see citing works
Self-citationSolid state NMR: new tools for insight into enzyme function
McDermott, A. E., & Polenova, T. E. (2007) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2007.10.001 · Cited by 60 · see citing works
Krukenberg, K. A., Southworth, D. R., Street, T. O., & Agard, D. A. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.04.080 · Cited by 57 · see citing works
Phillips, M. J., Calero, G. A., Chan, B., Ramachandran, S., & Cerione, R. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706271200 · Cited by 58 · see citing works
Spoerner, M., Nuehs, A., Herrmann, C., Steiner, G., & Kalbitzer, H. R. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05681.x · Cited by 56 · see citing works
Self-citationLessons from computer simulations of Ras proteins in solution and in membrane
Prakash, P., & Gorfe, A. A. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.07.024 · Cited by 49 · see citing works
A novel mechanism for the modulation of the Ras-effector interaction by small molecules
Spoerner, M., Gräf, T., König, B., & Kalbitzer, H. R. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.06.144 · Cited by 49 · see citing works
Self-citationMatsumoto, S., Miyano, N., Baba, S., Liao, J., Kawamura, T., Tsuda, C., Takeda, A., Yamamoto, M., Kumasaka, T., Kataoka, T., et al. (2016) · Scientific Reports · doi:10.1038/srep25931 · Cited by 47 · see citing works
Fenwick, R. B., Prasannan, S., Campbell, L. J., Nietlispach, D., Evetts, K. A., Camonis, J., Mott, H. R., & Owen, D. (2009) · Biochemistry · doi:10.1021/bi802129d · Cited by 47 · see citing works
Cdc42p GDP/GTP Cycling Is Necessary for Efficient Cell Fusion during Yeast Mating
Barale, S., McCusker, D., & Arkowitz, R. A. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-11-1040 · Cited by 45 · see citing works
Improved Binding of Raf to Ras·GDP Is Correlated with Biological Activity
Kiel, C., Filchtinski, D., Spoerner, M., Schreiber, G., Kalbitzer, H. R., & Herrmann, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.031153 · Cited by 44 · see citing works
Self-citationExceptionally high-affinity Ras binders that remodel its effector domain
McGee, J. H., Shim, S. Y., Lee, S., Swanson, P. K., Jiang, S. Y., Durney, M. A., & Verdine, G. L. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.816348 · Cited by 39 · see citing works
Li, Y., Zhang, Y., Großerueschkamp, F., Stephan, S., Cui, Q., Kötting, C., Xia, F., & Gerwert, K. B. (2018) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.8b00342 · Cited by 35 · see citing works
Holzapfel, G. A., Buhrman, G., & Mattos, C. (2012) · Biochemistry · doi:10.1021/bi300509j · Cited by 35 · see citing works
Aramini, J. M., Vorobiev, S. M., Tuberty, L., Janjua, H., Campbell, E., Seetharaman, J., Su, M., Huang, Y. J., Acton, T., Xiao, R., et al. (2015) · Structure · doi:10.1016/j.str.2015.06.003 · Cited by 33 · see citing works
Kobayashi, C., & Saito, S. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.09.063 · Cited by 33 · see citing works
Delineating the RAS Conformational Landscape
Parker, M. I., Meyer, J. E., Golemis, E. A., & Dunbrack (2022) · Cancer Research · doi:10.1158/0008-5472.can-22-0804 · Cited by 30 · see citing works
Hansen, A. L., Xiang, X., Yuan, C., Bruschweiler‐Li, L., & Brüschweiler, R. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01070-z · Cited by 27 · see citing works
Johansen, J., Kavaliauskas, D., Pfeil, S. H., Blaise, M., Cooperman, B. S., Goldman, Y. E., Thirup, S., & Knudsen, C. R. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky697 · Cited by 26 · see citing works
Structure of an inactive conformation of GTP-bound RhoA GTPase
Lin, Y., Lu, S., Zhang, J., & Zheng, Y. (2021) · Structure · doi:10.1016/j.str.2020.12.015 · Cited by 27 · see citing works
Chao, F.-A., Dharmaiah, S., Taylor, T. E., Messing, S. A. J., Gillette, W., Esposito, D., Nissley, D. V., McCormick, F. P., Byrd, R. A., Simanshu, D. K., et al. (2022) · Journal of the American Chemical Society · doi:10.1021/jacs.2c00007 · Cited by 26 · see citing works
Dynamic conformational equilibria in the active states of KRAS and NRAS
Rennella, E., Henry, C., Dickson, C. J., Georgescauld, F., Wales, T. E., Erdmann, D., Cotesta, S., Maira, S.-M., Sedrani, R. C., Brachmann, S. M., et al. (2024) · RSC Chemical Biology · doi:10.1039/d4cb00233d · Cited by 24 · see citing works
COMBINE analysis of the specificity of binding of Ras proteins to their effectors
Tomić, S., Bertoša, B., Wang, T., & Wade, R. C. (2007) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.21321 · Cited by 24 · see citing works
How Anionic Lipids Affect Spatiotemporal Properties of KRAS4B on Model Membranes.
Ngo, V. A., Sarkar, S., Neale, C., & Garcia, A. (2020) · Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.0c02642 · Cited by 23 · see citing works
Girard, É., Lopes, P., Spoerner, M., Dhaussy, A., Prangé, T., Kalbitzer, H. R., & Colloc’h, N. (2022) · Chemical Science · doi:10.1039/d1sc05488k · Cited by 23 · see citing works
Self-citationSharma, A. K., Pei, J., Yang, Y., Dyba, M. D., Smith, B. D., Rabara, D., Larsen, E. K., Lightstone, F. C., Esposito, D., Stephen, A. G., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105650 · Cited by 24 · see citing works
Sacco, E., Metalli, D., Spinelli, M., Manzoni, R., Šamalíková, M., Grandori, R., Morrione, A., Traversa, S., Alberghina, L., & Vanoni, M. (2011) · Biotechnology Advances · doi:10.1016/j.biotechadv.2011.05.011 · Cited by 22 · see citing works
High Pressure NMR Methods for Characterizing Functional Substates of Proteins
Kalbitzer, H. R. (2015) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-017-9918-8_9 · Cited by 21 · see citing works
Self-citationElucidating the Mode of Action of a Typical Ras State 1(T) Inhibitor
Rosnizeck, I. C., Filchtinski, D., Lopes, R. P., Kieninger, B., Herrmann, C., Kalbitzer, H. R., & Spoerner, M. (2014) · Biochemistry · doi:10.1021/bi401689w · Cited by 21 · see citing works
Self-citationXiong, Y., Zeng, J., Xia, F., Cui, Q., Deng, X., & Xu, X. (2022) · Journal of Computational Chemistry · doi:10.1002/jcc.26846 · Cited by 20 · see citing works
Cu2+-cyclen as Probe to Identify Conformational States in Guanine Nucleotide Binding Proteins
Meierhofer, T., Rosnizeck, I. C., Gräf, T., Reiß, K., König, B., Kalbitzer, H. R., & Spoerner, M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja108779j · Cited by 19 · see citing works
Self-citationState 1(T) Inhibitors of Activated Ras
Kalbitzer, H. R., & Spoerner, M. (2013) · The Enzymes · doi:10.1016/b978-0-12-416749-0.00004-x · Cited by 17 · see citing works
Self-citationZeng, J., Chen, J., Xia, F., Cui, Q., Deng, X., & Xu, X. (2022) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp00274d · Cited by 16 · see citing works
Rosnizeck, I. C., Gräf, T., Spoerner, M., Traenkle, J., Filchtinski, D., Herrmann, C., Gremer, L., Vetter, I. R., Wittinghofer, A., König, B., et al. (2010) · Angewandte Chemie · doi:10.1002/ange.200907002 · Cited by 15 · see citing works
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Matsumoto, K., Shima, F., Muraoka, S., Araki, M., Hu, L., Ijiri, Y., Hirai, R., Liao, J., Yoshioka, T., Kumasaka, T., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.204933 · Cited by 15 · see citing works
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Rosnizeck, I. C., Spoerner, M., Harsch, T., Kreitner, S., Filchtinski, D., Herrmann, C., Engel, D., König, B., & Kalbitzer, H. R. (2012) · Angewandte Chemie · doi:10.1002/ange.201204148 · Cited by 14 · see citing works
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Ader, C., Spoerner, M., Kalbitzer, H. R., & Brunner, E. (2007) · The Journal of Physical Chemistry B · doi:10.1021/jp067792p · Cited by 5 · see citing works
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Kötting, C., Rudack, T., & Gerwert, K. B. (2025) · Biological Chemistry · doi:10.1515/hsz-2025-0227 · Cited by 1 · see citing works
Salamh, S., & Sayyed–Ahmad, A. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2238080 · Cited by 1 · see citing works
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Baker, R. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/g51t-2216
Gräf, T. (2007) · University of Regensburg Publication Server (University of Regensburg) · doi:10.5283/epub.10503
- Authors
- Spoerner, M., Wittinghofer, A., & Kalbitzer, H. R.
- Affiliations
- University of Regensburg (DE)
- Max Planck Institute of Molecular Physiology (DE)
- Corresponding author
- Kalbitzer, Hans Robert
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2004-11-23
- Volume
- 578
- Issue
- 3
- Pages
- 305-310
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2018019331
- Cited by
- 70
- References
- 20
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 3 · 2023: 2 · 2022: 5 · 2021: 3 · 2020: 2 · 2019: 1 · 2018: 3 · 2017: 2 · 2016: 3 · 2015: 5 · 2014: 4 · 2013: 3 · 2012: 4
- FWCI
- 1.07
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (GRK760)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Physical Sciences › Chemistry › Spectroscopy › Advanced NMR Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- Ras, conformational equilibrium, point mutations, oncogenic mutations, GTP, GTP-bound state, effector binding, signal transduction, protein dynamics, 31P NMR
- MeSH terms
- Amino Acid Sequence, Escherichia coli, Guanosine Diphosphate, Humans, Hydrogen-Ion Concentration, Kinetics, Models, Molecular, Phosphorus, Phosphorus Isotopes, Protein Binding, Protein Conformation, Genes, ras, Temperature, Threonine, Genetic Variation, Signal Transduction, Point Mutation, Protein Structure, Tertiary, ras Proteins, Nuclear Magnetic Resonance, Biomolecular, Amino Acid Substitution, GTPase-Activating Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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