about
The Significance of Ras Activity in Pancreatic Cancer InitiationH-Ras forms dimers on membrane surfaces via a protein-protein interface.Ras Dimer Formation as a New Signaling Mechanism and Potential Cancer Therapeutic Target.Molecular kinetics. Ras activation by SOS: allosteric regulation by altered fluctuation dynamics.Oligomerization and nanocluster organization render specificity.Binding hotspots on K-ras: consensus ligand binding sites and other reactive regions from probe-based molecular dynamics analysis.Ras-GTP dimers activate the Mitogen-Activated Protein Kinase (MAPK) pathway.GTP-Dependent K-Ras DimerizationLipoprotein insertion into membranes of various complexity: lipid sorting, interfacial adsorption and protein clustering.Seeing is believing: Ras dimers observed in live cellsSpecific cancer-associated mutations in the switch III region of Ras increase tumorigenicity by nanocluster augmentation.Overview of simulation studies on the enzymatic activity and conformational dynamics of the GTPase Ras.The disordered hypervariable region and the folded catalytic domain of oncogenic K-Ras4B partner in phospholipid binding.Oncogenic K-Ras Binds to an Anionic Membrane in Two Distinct Orientations: A Molecular Dynamics Analysis.Plasma membrane regulates Ras signaling networks.Membrane extraction of Rab proteins by GDP dissociation inhibitor characterized using attenuated total reflection infrared spectroscopyLessons from computer simulations of Ras proteins in solution and in membraneInhibition of RAS function through targeting an allosteric regulatory site.Computational and biochemical characterization of two partially overlapping interfaces and multiple weak-affinity K-Ras dimersThe efficacy of Raf kinase recruitment to the GTPase H-ras depends on H-ras membrane conformer-specific nanoclustering.MicroRNA-Based Therapeutic Strategies for Targeting Mutant and Wild Type RAS in CancerModeling of RAS complexes supports roles in cancer for less studied partners.The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects.Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view.Membrane orientation dynamics of lipid-modified small GTPases.RAS Proteins and Their Regulators in Human Disease.Cooperative Clustering Digitizes Biochemical Signaling and Enhances its Fidelity.ATP binding to neighbouring subunits and intersubunit allosteric coupling underlie proteasomal ATPase function.The Ras G Domain Lacks the Intrinsic Propensity to Form Dimers.Covalent Ras Dimerization on Membrane Surfaces through Photosensitized Oxidation.Aggregation of lipid-anchored full-length H-Ras in lipid bilayers: simulations with the MARTINI force field.Phosphorylation of the C-Raf N-region promotes Raf dimerization.Characterization of a membrane-active peptide from the Bordetella pertussis CyaA toxin.Dimerization opens new avenues into Ras signaling research.K-Ras4B Remains Monomeric on Membranes over a Wide Range of Surface Densities and Lipid Compositions.Spatiotemporal Analysis of K-Ras Plasma Membrane Interactions Reveals Multiple High Order Homo-oligomeric Complexes.Targeting the α4-α5 interface of RAS results in multiple levels of inhibition.Lipid-Sorting Specificity Encoded in K-Ras Membrane Anchor Regulates Signal Output.The Protonation States of GTP and GppNHp in Ras Proteins.RAS signaling: Divide and conquer.
P2860
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P2860
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
N-Ras forms dimers at POPC membranes.
@en
N-Ras forms dimers at POPC membranes.
@nl
type
label
N-Ras forms dimers at POPC membranes.
@en
N-Ras forms dimers at POPC membranes.
@nl
prefLabel
N-Ras forms dimers at POPC membranes.
@en
N-Ras forms dimers at POPC membranes.
@nl
P2093
P2860
P50
P1433
P1476
N-Ras forms dimers at POPC membranes.
@en
P2093
Jörn Güldenhaupt
Peter Bachler
Till Rudack
P2860
P304
P356
10.1016/J.BPJ.2012.08.043
P407
P577
2012-10-02T00:00:00Z