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Effect of ligands on stability of H-Ras GTPase
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/0471140864.ps2809s79openalex-snapshot
Analysis of Protein Stability and Ligand Interactions by Thermal Shift Assay
inferredcites →https://doi.org/10.1002/0471143030.cb1708s23openalex-snapshot
Isothermal Titration Calorimetry
inferredcites →https://doi.org/10.1002/1097-0134(2000)41:4+<63::aid-prot60>3.0.co;2-6openalex-snapshot
Structural stability of binding sites: Consequences for binding affinity and allosteric effects
inferredcites →https://doi.org/10.1007/978-1-59745-367-7_1openalex-snapshot
Microcalorimetry of Proteins and Their Complexes
inferredcites →https://doi.org/10.1016/0022-2836(89)90540-8openalex-snapshot
Crystallization and preliminary X-ray analysis of the human c-H-ras-oncogene product p21 complexed with GTP analogues
inferredcites →https://doi.org/10.1016/0076-6879(86)31033-4openalex-snapshot
[2]Scanning microcalorimetry in studying temperature-induced changes in proteins
inferredcites →https://doi.org/10.1016/0092-8674(89)90054-8openalex-snapshot
All ras proteins are polyisoprenylated but only some are palmitoylated
inferredcites →https://doi.org/10.1016/j.cell.2007.05.018openalex-snapshot
GEFs and GAPs: Critical Elements in the Control of Small G Proteins
inferredcites →https://doi.org/10.1016/j.jmb.2011.09.011openalex-snapshot
Analysis of Binding Site Hot Spots on the Surface of Ras GTPase
inferredcites →https://doi.org/10.1016/s0021-9258(18)54022-9openalex-snapshot
Kinetic and structural analysis of the Mg(2+)-binding site of the guanine nucleotide-binding protein p21H-ras.
inferredcites →https://doi.org/10.1016/s0021-9258(18)67333-8openalex-snapshot
The effect of Mg2+ on the guanine nucleotide exchange rate of p21N-ras.
inferredcites →https://doi.org/10.1016/s0065-3233(08)60654-3openalex-snapshot
Statistical Thermodynamic Linkage Between Conformational And Binding Equilibria
inferredcites →https://doi.org/10.1016/s0301-4622(98)00149-5openalex-snapshot
Folding under inequilibrium conditions as a possible reason for partial irreversibility of heat-denatured proteins: computer simulation study
inferredcites →https://doi.org/10.1021/bi00477a025openalex-snapshot
Kinetics of interaction of nucleotides with nucleotide-free H-ras p21
inferredcites →https://doi.org/10.1021/bi301304gopenalex-snapshot
Characterization of the Second Ion-Binding Site in the G Domain of H-Ras
inferredcites →https://doi.org/10.1021/bi801076copenalex-snapshot
Global Conformational Dynamics in Ras
inferredcites →https://doi.org/10.1021/bi9811157openalex-snapshot
Ligand Binding Is the Principal Determinant of Stability for the p21H-ras Protein
inferredcites →https://doi.org/10.1038/nprot.2007.321openalex-snapshot
The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
inferredcites →https://doi.org/10.1042/bst20120268openalex-snapshot
The role of palmitoylation in regulating Ras localization and function
inferredcites →https://doi.org/10.1073/pnas.0605224103openalex-snapshot
Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination
inferredcites →https://doi.org/10.1074/jbc.270.7.2901openalex-snapshot
Quantitative Analysis of the Complex between p21 and the Ras-binding Domain of the Human Raf-1 Protein Kinase
inferredcites →https://doi.org/10.1126/stke.2502004re13openalex-snapshot
Human RAS Superfamily Proteins and Related GTPases
inferredcites →https://doi.org/10.1146/annurev-biochem-062708-134043openalex-snapshot
Structure-Function Relationships of the G Domain, a Canonical Switch Motif
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1007/978-1-0716-1190-6_8openalex-snapshot
Methods to Monitor Ras Activation State
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