H-Ras forms dimers on membrane surfaces via a protein-protein interface. - Wikidata - wikimedia - TriplyDB

H-Ras forms dimers on membrane surfaces via a protein-protein interface.

H-Ras forms dimers on membrane surfaces via a protein-protein interface.

http://www.wikidata.org/entity/Q30573159

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The Significance of Ras Activity in Pancreatic Cancer Initiation Vibrio cholerae FeoA, FeoB, and FeoC Interact To Form a Complex Phosphotyrosine-mediated LAT assembly on membranes drives kinetic bifurcation in recruitment dynamics of the Ras activator SOS.One-way membrane trafficking of SOS in receptor-triggered Ras activation.A Bayesian cluster analysis method for single-molecule localization microscopy data.Mechanism of SOS PR-domain autoinhibition revealed by single-molecule assays on native protein from lysate.Ras Dimer Formation as a New Signaling Mechanism and Potential Cancer Therapeutic Target.The structural basis for cancer treatment decisions.Nanoclustering as a dominant feature of plasma membrane organization.Drugging the undruggable RAS: Mission possible?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 Dimerization Seeing is believing: Ras dimers observed in live cells Specific cancer-associated mutations in the switch III region of Ras increase tumorigenicity by nanocluster augmentation.E-cadherin junction formation involves an active kinetic nucleation process.Using supported bilayers to study the spatiotemporal organization of membrane-bound proteins.Farnesylated and methylated KRAS4b: high yield production of protein suitable for biophysical studies of prenylated protein-lipid interactions.The disordered hypervariable region and the folded catalytic domain of oncogenic K-Ras4B partner in phospholipid binding.K-Ras at Anionic Membranes: Orientation, Orientation…Orientation. Recent Simulations and Experiments.Oncogenic K-Ras Binds to an Anionic Membrane in Two Distinct Orientations: A Molecular Dynamics Analysis.Plasma membrane regulates Ras signaling networks.Computational and biochemical characterization of two partially overlapping interfaces and multiple weak-affinity K-Ras dimers MicroRNA-Based Therapeutic Strategies for Targeting Mutant and Wild Type RAS in Cancer Modeling of RAS complexes supports roles in cancer for less studied partners.With or without rafts? Alternative views on cell membranes.The renewed battle against RAS-mutant cancers.Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view.KSR as a therapeutic target for Ras-dependent cancers.RAS Proteins and Their Regulators in Human Disease.Cooperative Clustering Digitizes Biochemical Signaling and Enhances its Fidelity.The Ras G Domain Lacks the Intrinsic Propensity to Form Dimers.Covalent Ras Dimerization on Membrane Surfaces through Photosensitized Oxidation.Biochemical characterization of essential cell division proteins FtsX and FtsE that mediate peptidoglycan hydrolysis by PcsB in Streptococcus pneumoniae.Analysis of K-Ras Interactions by Biotin Ligase Tagging.Molecular mechanism of activation of class IA phosphoinositide 3-kinases (PI3Ks) by membrane-localized HRas.Phosphorylation of the C-Raf N-region promotes Raf dimerization.TCL/RhoJ Plasma Membrane Localization and Nucleotide Exchange Is Coordinately Regulated by Amino Acids within the N Terminus and a Distal Loop Region.Dimerization of lipocalin allergens.Dimerization opens new avenues into Ras signaling research.

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P2860

H-Ras forms dimers on membrane surfaces via a protein-protein interface.

http://www.wikidata.org/entity/Q30573159

description

2014 nî lūn-bûn

@nan

2014 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年学术文章

@wuu

2014年学术文章

@zh-cn

2014年学术文章

@zh-hans

2014年学术文章

@zh-my

2014年学术文章

@zh-sg

2014年學術文章

@yue

name

H-Ras forms dimers on membrane surfaces via a protein-protein interface.

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H-Ras forms dimers on membrane surfaces via a protein-protein interface.

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type

label

H-Ras forms dimers on membrane surfaces via a protein-protein interface.

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H-Ras forms dimers on membrane surfaces via a protein-protein interface.

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prefLabel

H-Ras forms dimers on membrane surfaces via a protein-protein interface.

@ast

H-Ras forms dimers on membrane surfaces via a protein-protein interface.

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PNAS.1321155111

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Proceedings of the National Academy of Sciences of the United States of America

P1476

H-Ras forms dimers on membrane surfaces via a protein-protein interface

@en

P2093

Christopher Rhodes

http://www.w3.org/2001/XMLSchema#string

Hsiung-Lin Tu

http://www.w3.org/2001/XMLSchema#string

Jay T Groves

http://www.w3.org/2001/XMLSchema#string

Jeffrey S Iwig

http://www.w3.org/2001/XMLSchema#string

Lars Iversen

http://www.w3.org/2001/XMLSchema#string

Scott D Hansen

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Wan-Chen Lin

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William Y C Huang

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P2860

A novel switch region regulates H-ras membrane orientation and signal output

Negative regulation of Rho family GTPases Cdc42 and Rac2 by homodimer formation

Crystal structure and functional analysis of Ras binding to its effector phosphoinositide 3-kinase gamma

Structural Basis for Conformational Dynamics of GTP-bound Ras Protein

Ras oncogenes: split personalities

The Ras superfamily at a glance

Activation of Raf as a result of recruitment to the plasma membrane

Ras history: The saga continues.

The Rsr1/Bud1 GTPase interacts with itself and the Cdc42 GTPase during bud-site selection and polarity establishment in budding yeast

Membrane curvature induced by Arf1-GTP is essential for vesicle formation.

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2996-3001

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scholarly article

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10.1073/PNAS.1321155111

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8

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111

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Sune M Christensen

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2014-02-10T00:00:00Z

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24516166

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3939930

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