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Ligand Binding Is the Principal Determinant of Stability for the p21H-ras Protein
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1006/abbi.1994.1210openalex-snapshot
Isolation and Refolding of H-ras from Inclusion Bodies of Escherichia coli: Refold Procedure and Comparison of Refolded and Soluble H-ras
inferredcites →https://doi.org/10.1006/jmbi.1995.0365openalex-snapshot
NMR Structure of a Stable “OB-fold” Sub-domain Isolated from Staphylococcal Nuclease
inferredcites →https://doi.org/10.1016/0022-2836(89)90500-7openalex-snapshot
Characterization of the critical state in protein folding
inferredcites →https://doi.org/10.1016/0022-2836(91)90753-sopenalex-snapshot
Crystal structures at 2.2 Å resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP
inferredcites →https://doi.org/10.1016/0022-2836(92)90824-4openalex-snapshot
Absence of the thermal transition in apo-α-lactalbumin in the molten globule state
inferredcites →https://doi.org/10.1016/s0959-440x(96)80091-1openalex-snapshot
Structural analysis of non-native states of proteins by NMR methods
inferredcites →https://doi.org/10.1073/pnas.82.2.376openalex-snapshot
Ha-ras proteins exhibit GTPase activity: point mutations that activate Ha-ras gene products result in decreased GTPase activity.
inferredcites →https://doi.org/10.1096/fasebj.10.1.8566543openalex-snapshot
The denatured state (the other half of the folding equation) and its role in protein stability
inferredcites →https://doi.org/10.1111/j.1432-1033.1987.tb10540.xopenalex-snapshot
Characterisation of the metal‐ion–GDP complex at the active sites of transforming and nontransforming p21 proteins by observation of the 17O‐Mn superhyperfine coupling and by kinetic methods
inferredcites →https://doi.org/10.1126/science.2406906openalex-snapshot
Molecular Switch for Signal Transduction: Structural Differences Between Active and Inactive Forms of Protooncogenic ras Proteins
inferredcites →https://doi.org/10.1126/science.2448879openalex-snapshot
Three-Dimensional Structure of an Oncogene Protein: Catalytic Domain of Human c-H- ras P21
inferredcites →https://doi.org/10.1126/science.3898366openalex-snapshot
A Model for the Tertiary Structure of p21, the Product of the ras Oncogene
inferredcites →https://doi.org/10.1126/science.4035359openalex-snapshot
Z-DNA Forms Without an Alternating Purine-Pyrimidine Sequence in Solution
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.2139/ssrn.3312728openalex-extracted
Isoform-Specific Destabilization of the Active Site Reveals Molecular Mechanism of Intrinsic Activation of KRas G13D
inferred← citeshttps://doi.org/10.1002/9783527610907.ch11openalex-snapshot
Quantification of Protein–Ligand Interactions in Solution by Hydrogen/Deuterium Exchange (PLIMSTEX)
inferred← citeshttps://doi.org/10.1002/bip.21398openalex-snapshot
Semisynthesis of human thymidine monophosphate kinase
inferred← citeshttps://doi.org/10.1002/cbic.200300606openalex-snapshot
Fluorescent Cellular Sensors of Steroid Receptor Ligands
inferred← citeshttps://doi.org/10.1002/pro.115openalex-snapshot
Determining protein stability in cell lysates by pulse proteolysis and Western blotting
inferred← citeshttps://doi.org/10.1002/prot.1107openalex-snapshot
Structured disorder and conformational selection
inferred← citeshttps://doi.org/10.1006/abio.1999.4320openalex-snapshot
Spectroscopic Methods for Analysis of Protein Secondary Structure
inferred← citeshttps://doi.org/10.1006/jmbi.1999.3110openalex-snapshot
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm
inferred← citeshttps://doi.org/10.1006/jmbi.2001.5230openalex-snapshot
Highly divergent dihydrofolate reductases conserve complex folding mechanisms 1 1Edited by P. E. Wright
inferred← citeshttps://doi.org/10.1016/b978-0-12-374984-0.01698-3openalex-snapshot
Intrinsically Disordered Proteins
inferred← citeshttps://doi.org/10.1016/j.bbadis.2009.09.010openalex-snapshot
The R1441C mutation alters the folding properties of the ROC domain of LRRK2
inferred← citeshttps://doi.org/10.1016/j.freeradbiomed.2014.09.027openalex-snapshot
Redox regulation of Rac1 by thiol oxidation
inferred← citeshttps://doi.org/10.1016/j.ijms.2004.09.012openalex-snapshot
PLIMSTEX: a novel mass spectrometric method for the quantification of protein–ligand interactions in solution
inferred← citeshttps://doi.org/10.1016/j.mrl.2024.200168openalex-snapshot
Distinct association of HRAS and KRAS with Mn2+ ion illustrated by paramagnetic NMR
inferred← citeshttps://doi.org/10.1016/j.semcancer.2018.02.006openalex-snapshot
New weapons to penetrate the armor: Novel reagents and assays developed at the NCI RAS Initiative to enable discovery of RAS therapeutics
inferred← citeshttps://doi.org/10.1016/s1093-3263(00)00138-8openalex-snapshot
Intrinsically disordered protein
inferred← citeshttps://doi.org/10.1016/s1357-2725(01)00175-3openalex-snapshot
Urea-induced unfolding studies of free- and ligand-bound tetrameric ATP-dependent Saccharomyces cerevisiae phosphoenolpyruvate carboxykinase
inferred← citeshttps://doi.org/10.1021/ac202723hopenalex-snapshot
Homogeneous Single-Label Biochemical Ras Activation Assay Using Time-Resolved Luminescence
inferred← citeshttps://doi.org/10.1038/sj.emboj.7601044openalex-snapshot
Nucleotide exchange via local protein unfolding—structure of Rab8 in complex with MSS4
inferred← citeshttps://doi.org/10.1038/sj.onc.1203909openalex-snapshot
Oncogenic insertional mutations in the P-loop of Ras are overactive in MAP kinase signaling
inferred← citeshttps://doi.org/10.1046/j.1432-1033.2002.03248.xopenalex-snapshot
Equilibrium unfolding and conformational plasticity of troponin I and T
inferred← citeshttps://doi.org/10.1073/pnas.1413185112openalex-snapshot
Direct inhibition of oncogenic KRAS by hydrocarbon-stapled SOS1 helices
inferred← citeshttps://doi.org/10.1074/jbc.274.23.16052openalex-snapshot
Pseudo-native Motifs in the Noncovalent Heme-Apocytochrome c Complex
inferred← citeshttps://doi.org/10.1074/jbc.c113.525691openalex-snapshot
Differences in the Regulation of K-Ras and H-Ras Isoforms by Monoubiquitination
inferred← citeshttps://doi.org/10.1074/jbc.m009295200openalex-snapshot
γ-Phosphate Protonation and pH-dependent Unfolding of the Ras·GTP·Mg2+ Complex
inferred← citeshttps://doi.org/10.1074/jbc.m211207200openalex-snapshot
Glutamate Counteracts the Denaturing Effect of Urea through Its Effect on the Denatured State
inferred← citeshttps://doi.org/10.1080/20014091074228openalex-snapshot
Protein Folding: Binding of Conformationally Fluctuating Building Blocks Via Population Selection
inferred← citeshttps://doi.org/10.1101/179283openalex-snapshot
Effect of ligands on stability of H-Ras GTPase
inferred← citeshttps://doi.org/10.1101/2023.12.05.570111openalex-snapshot
Ras Activation by Hydrostatic Pressure is Enhanced by GAP and GEF in vitro
inferred← citeshttps://doi.org/10.1110/ps.26601openalex-snapshot
Testing the role of chain connectivity on the stability and structure of dihydrofolate reductase fromE. coli: Fragment complementation and circular permutation reveal stable, alternatively folded forms
inferred← citeshttps://doi.org/10.1110/ps.34101openalex-snapshot
A model of dynamic side‐chain–side‐chain interactions in the α‐lactalbumin molten globule
inferred← citeshttps://doi.org/10.1110/ps.4210102openalex-snapshot
Natively unfolded proteins: A point where biology waits for physics
inferred← citeshttps://doi.org/10.1110/ps.9.1.121openalex-snapshot
Interaction with magnesium and ADP stabilizes both components of nitrogenase fromKlebsiella pneumoniaeagainst urea denaturation
inferred← citeshttps://doi.org/10.1111/febs.14143openalex-snapshot
The nucleotide‐free state of heterotrimeric G proteins α‐subunit adopts a highly stable conformation
inferred← citeshttps://doi.org/10.1111/febs.15235openalex-snapshot
Nucleotide‐induced folding of cell division protein FtsZ from Staphylococcus aureus
inferred← citeshttps://doi.org/10.1126/sciadv.aax1595openalex-snapshot
Decreased conformational stability in the oncogenic N92I mutant of Ras-related C3 botulinum toxin substrate 1
inferred← citeshttps://doi.org/10.1240/sav_gbm_2007_m_001787openalex-snapshot
ATR-FTIR Spectroscopy of Membrane Bound Ras Protein
inferred← citeshttps://doi.org/10.13016/m25d23openalex-snapshot
Probing Allosteric Communication Between Disordered Surfaces in a Protein
inferred← citeshttps://doi.org/10.18388/abp.2001_3850openalex-snapshot
Structure of small G proteins and their regulators.
inferred← citeshttps://doi.org/10.7314/apjcp.2014.15.1.111openalex-snapshot
Identification of a Potential Anticancer Target of Danshensu by Inverse Docking
inferred← citeshttps://doi.org/10.7554/elife.76595openalex-snapshot
A saturation-mutagenesis analysis of the interplay between stability and activation in Ras
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