SIGNAL TRANSDUCTION. Structural basis for nucleotide exchange in heterotrimeric G proteins. - Wikidata - awgldk - TriplyDB

SIGNAL TRANSDUCTION. Structural basis for nucleotide exchange in heterotrimeric G proteins.

SIGNAL TRANSDUCTION. Structural basis for nucleotide exchange in heterotrimeric G proteins.

http://www.wikidata.org/entity/Q42390741

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Revealing Atomic-Level Mechanisms of Protein Allostery with Molecular Dynamics Simulations Extended Phase-Space Methods for Enhanced Sampling in Molecular Simulations: A Review Thematic Minireview Series: New Directions in G Protein-coupled Receptor Pharmacology Computational Simulation of the Activation Cycle of Gα Subunit in the G Protein Cycle Using an Elastic Network Model The Quantum Nature of Drug-Receptor Interactions: Deuteration Changes Binding Affinities for Histamine Receptor Ligands A Conserved Hydrophobic Core in Gαi1 Regulates G Protein Activation and Release from Activated Receptor Beyond Membrane Protein Structure: Drug Discovery, Dynamics and Difficulties.Role of Structural Dynamics at the Receptor G Protein Interface for Signal Transduction Optimization of a Nucleic Acids united-RESidue 2-Point model (NARES-2P) with a maximum-likelihood approach Dynamic Coupling and Allosteric Networks in the α Subunit of Heterotrimeric G Proteins.Probing Gαi1 protein activation at single-amino acid resolution.Conformational dynamics of a G-protein α subunit is tightly regulated by nucleotide binding.Diverse activation pathways in class A GPCRs converge near the G-protein-coupling region The structural basis of the dominant negative phenotype of the Gαi1β1γ2 G203A/A326S heterotrimer.GIV/Girdin activates Gαi and inhibits Gαs via the same motif Ric-8A, a G protein chaperone with nucleotide exchange activity induces long-range secondary structure changes in Gα.Recent Progress in Understanding the Conformational Mechanism of Heterotrimeric G Protein Activation DIRECT-ID: An automated method to identify and quantify conformational variations--application to β2 -adrenergic GPCR.The ins and outs of adrenergic signaling.Computational Membrane Biophysics: From Ion Channels Interactions with Drugs to Cellular Function.Homology modeling of FFA2 identifies novel agonists that potentiate insulin secretion.Single-molecule analysis of ligand efficacy in β2AR-G-protein activation.Invited review: Activation of G proteins by GTP and the mechanism of Gα-catalyzed GTP hydrolysis.Hitchhiking on the heptahelical highway: structure and function of 7TM receptor complexes.Mechanistic insights into GPCR-G protein interactions.The GAPs, GEFs, GDIs and…now, GEMs: New kids on the heterotrimeric G protein signaling block.Capturing Invisible Motions in the Transition from Ground to Rare Excited States of T4 Lysozyme L99A.A PII-Like Protein Regulated by Bicarbonate: Structural and Biochemical Studies of the Carboxysome-Associated CPII Protein.Engineering a minimal G protein to facilitate crystallisation of G protein-coupled receptors in their active conformation.A test on reactive force fields for the study of silica dimerization reactions.Nanosecond Dynamics of Gαi1 Bound to Nucleotides or Ric-8A, a Gα Chaperone with GEF Activity.Biased Allostery ER/K linked GPCR-G protein fusions systematically modulate second messenger response in cells Expression and Purification of the Pain Receptor TRPV1 for Spectroscopic Analysis Lipid interaction sites on channels, transporters and receptors: Recent insights from molecular dynamics simulations.Molecular mechanism of Gαi activation by non-GPCR proteins with a Gα-Binding and Activating motif.Exploring the inhibition mechanism of adenylyl cyclase type 5 by n-terminal myristoylated Gαi1 Single-molecule imaging reveals receptor-G protein interactions at cell surface hot spots.Intracellular Transfer of Na+ in an Active-State G-Protein-Coupled Receptor.Finding the needle in the haystack: towards solving the protein-folding problem computationally.

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P2860

SIGNAL TRANSDUCTION. Structural basis for nucleotide exchange in heterotrimeric G proteins.

http://www.wikidata.org/entity/Q42390741

description

2015 nî lūn-bûn

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2015年论文

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2015年论文

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name

SIGNAL TRANSDUCTION. Structura ...... in heterotrimeric G proteins.

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SIGNAL TRANSDUCTION. Structura ...... in heterotrimeric G proteins.

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type

label

SIGNAL TRANSDUCTION. Structura ...... in heterotrimeric G proteins.

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SIGNAL TRANSDUCTION. Structura ...... in heterotrimeric G proteins.

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prefLabel

SIGNAL TRANSDUCTION. Structura ...... in heterotrimeric G proteins.

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SIGNAL TRANSDUCTION. Structura ...... in heterotrimeric G proteins.

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SIGNAL TRANSDUCTION. Structura ...... in heterotrimeric G proteins.

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Ansgar Philippsen

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Daniel H Arlow

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Nicolas Villanueva

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Ron O Dror

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Thomas J Mildorf

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Zhongyu Yang

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P2860

Structure and function of an irreversible agonist-β(2) adrenoceptor complex

CHARMM general force field: A force field for drug-like molecules compatible with the CHARMM all-atom additive biological force fields

Crystal structure of the β2 adrenergic receptor-Gs protein complex

Identification of two distinct inactive conformations of the beta2-adrenergic receptor reconciles structural and biochemical observations

Signal activation and inactivation by the Gα helical domain: a long-neglected partner in G protein signaling

Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A

Structural Determinants of Affinity Enhancement between GoLoco Motifs and G-Protein Subunit Mutants

The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S

The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2

The 2.0 A crystal structure of a heterotrimeric G protein

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David W. Borhani

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