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Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis.
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“In each case, we began with the crystal structures of wild-type H-Ras bound to GTP or GDP (PDB codes 5P21 and 4Q21, respectively [Milburn et al., 1990; Pai et al., 1990]), replacing the appropriate sidechains by alanine for each simulation of a mutant protein.”
BackgroundMethodTyrosyl phosphorylation of KRAS stalls GTPase cycle via alteration of switch I and II conformation
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Inhibitors of Ras–SOS Interactions
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MethodIntrinsic GTPase activity of K-RAS monitored by native mass spectrometry
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Scalable emulation of protein equilibrium ensembles with generative deep learning
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(2000) · PubMed
Metadata
- Authors
- Pai, E. F., Krengel, U., Petsko, G. A., Goody, R. S., Kabsch, W., & Wittinghofer, A.
- Venue
- The EMBO Journal
- Published
- 1990-08
- Volume
- 9
- Issue
- 8
- Pages
- 2351-2359
- ISSN
- 0261-4189 (ISSN-L)
- OpenAlex
- W2152561142
- Cited by
- 1,074
- References
- 2
- FWCI
- 22.83
- Type
- journal article
- Language
- en
- Open access
- bronze
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