Analysis of Binding Site Hot Spots on the Surface of Ras GTPase
about
RAS isoforms and mutations in cancer at a glancepMD-Membrane: A Method for Ligand Binding Site Identification in Membrane-Bound ProteinsIntrinsic K-Ras dynamics: A novel molecular dynamics data analysis method shows causality between residue pair motionsEvaluation of a DLA-79 allele associated with multiple immune-mediated diseases in dogs.Mechanism of the exchange reaction in HRAS from multiscale modelingDrugging the undruggable RAS: Mission possible?How proteins bind macrocycles.Binding hotspots on K-ras: consensus ligand binding sites and other reactive regions from probe-based molecular dynamics analysis.Ligand deconstruction: Why some fragment binding positions are conserved and others are notNew Frontiers in DruggabilityTyrosine phosphorylation of RAS by ABL allosterically enhances effector bindingOverview of simulation studies on the enzymatic activity and conformational dynamics of the GTPase Ras.Inhibition of prenylated KRAS in a lipid environmentNeutron Crystal Structure of RAS GTPase Puts in Question the Protonation State of the GTP γ-Phosphate.Focused grid-based resampling for protein docking and mapping.Relationship between hot spot residues and ligand binding hot spots in protein-protein interfaces.Andrographolide derivatives inhibit guanine nucleotide exchange and abrogate oncogenic Ras function.KRAS - An Evolving Cancer TargetNRAS germline variant G138R and multiple rare somatic mutations on APC in colorectal cancer patients in Taiwan by next generation sequencing.Driving Structure-Based Drug Discovery through Cosolvent Molecular Dynamics.Computational allosteric ligand binding site identification on Ras proteins.Analysis of correlated mutations in Ras G-domain.The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects.Distinct dynamics and interaction patterns in H- and K-Ras oncogenic P-loop mutants.Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view.Dynamic studies of H-Ras•GTPγS interactions with nucleotide exchange factor Sos reveal a transient ternary complex formation in solution.Single-molecule fluorescence imaging of RalGDS on cell surfaces during signal transduction from Ras to Ral.Hot-spot identification on a broad class of proteins and RNA suggest unifying principles of molecular recognition.Study of the correlation between H-ras mutation and primary hepatocellular carcinomaRas: structural details to guide direct targeting.Allosteric activation of the Par-6 PDZ via a partial unfolding transition.Development of a Nucleotide Exchange Inhibitor That Impairs Ras Oncogenic Signaling.Design, synthesis and biological evaluation of renin inhibitors guided by simulated annealing of chemical potential simulations.Exploring the structural origins of cryptic sites on proteins.
P2860
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P2860
Analysis of Binding Site Hot Spots on the Surface of Ras GTPase
description
2011 nî lūn-bûn
@nan
2011 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Analysis of Binding Site Hot Spots on the Surface of Ras GTPase
@ast
Analysis of Binding Site Hot Spots on the Surface of Ras GTPase
@en
Analysis of Binding Site Hot Spots on the Surface of Ras GTPase
@nl
type
label
Analysis of Binding Site Hot Spots on the Surface of Ras GTPase
@ast
Analysis of Binding Site Hot Spots on the Surface of Ras GTPase
@en
Analysis of Binding Site Hot Spots on the Surface of Ras GTPase
@nl
prefLabel
Analysis of Binding Site Hot Spots on the Surface of Ras GTPase
@ast
Analysis of Binding Site Hot Spots on the Surface of Ras GTPase
@en
Analysis of Binding Site Hot Spots on the Surface of Ras GTPase
@nl
P2093
P2860
P3181
P1476
Analysis of Binding Site Hot Spots on the Surface of Ras GTPase
@en
P2093
Bradley M Kearney
Brandon Zerbe
Carla Mattos
Casey O'Connor
Elizaveta A Kovrigina
Evgenii L Kovrigin
Greg Buhrman
Raeanne Napoleon
Sandor Vajda
P2860
P304
P3181
P356
10.1016/J.JMB.2011.09.011
P407
P50
P577
2011-11-04T00:00:00Z