The crystal structure of a self-activating G protein alpha subunit reveals its distinct mechanism of signal initiation.
about
Ternary WD40 Repeat-Containing Protein Complexes: Evolution, Composition and Roles in Plant ImmunitySignal activation and inactivation by the Gα helical domain: a long-neglected partner in G protein signalingComputational Simulation of the Activation Cycle of Gα Subunit in the G Protein Cycle Using an Elastic Network ModelHeterotrimeric G-proteins in Picea abies and their regulation in response to Heterobasidion annosum s.l. infectionA Conserved Hydrophobic Core in Gαi1 Regulates G Protein Activation and Release from Activated ReceptorEndocytosis of the seven-transmembrane RGS1 protein activates G-protein-coupled signalling in Arabidopsis.Heterotrimeric G proteins control stem cell proliferation through CLAVATA signaling in Arabidopsis.Proteogenomic convergence for understanding cancer pathways and networks.A knockout mutation of a constitutive GPCR in Tetrahymena decreases both G-protein activity and chemoattraction.G protein activation without a GEF in the plant kingdom.Signaling specificity provided by the Arabidopsis thaliana heterotrimeric G-protein γ subunits AGG1 and AGG2 is partially but not exclusively provided through transcriptional regulationFunctional reconstitution of an atypical G protein heterotrimer and regulator of G protein signaling protein (RGS1) from Arabidopsis thaliana.Adaptive evolution of signaling partnersMore (G-proteins) please! Identification of an elaborate network of G-proteins in soybeanDifferences in intradomain and interdomain motion confer distinct activation properties to structurally similar Gα proteins.The UniProtKB guide to the human proteome.Dynamic Coupling and Allosteric Networks in the α Subunit of Heterotrimeric G Proteins.Heterotrimeric G protein-coupled signaling in plants.Eukaryotic G protein signaling evolved to require G protein-coupled receptors for activation.Probing Gαi1 protein activation at single-amino acid resolution.Heterotrimeric G protein signalling in the plant kingdom.Structural Aspects of GPCR-G Protein Coupling."Round up the usual suspects": a comment on nonexistent plant G protein-coupled receptors.Proteomic Screening and Lasso Regression Reveal Differential Signaling in Insulin and Insulin-like Growth Factor I (IGF1) Pathways.Phospholipases as GTPase activity accelerating proteins (GAPs) in plants.Plant G-Proteins Come of Age: Breaking the Bond with Animal Models.Phosphatidic acid binding inhibits RGS1 activity to affect specific signaling pathways in Arabidopsis.Rice heterotrimeric G-protein gamma subunits (RGG1 and RGG2) are differentially regulated under abiotic stress.Extra-Large G Proteins Expand the Repertoire of Subunits in Arabidopsis Heterotrimeric G Protein Signaling.Predicted Functional Implications of Phosphorylation of Regulator of G Protein Signaling Protein in Plants.Two chimeric regulators of G-protein signaling (RGS) proteins differentially modulate soybean heterotrimeric G-protein cycle.Activation of an unusual G-protein in the simple protist Trichomonas vaginalisDo plants contain g protein-coupled receptors?Recently duplicated plant heterotrimeric Gα proteins with subtle biochemical differences influence specific outcomes of signal-response coupling.Gα and regulator of G-protein signaling (RGS) protein pairs maintain functional compatibility and conserved interaction interfaces throughout evolution despite frequent loss of RGS proteins in plants.Membrane-localized extra-large G proteins and Gbg of the heterotrimeric G proteins form functional complexes engaged in plant immunity in Arabidopsis.Characterization of the heterotrimeric G-protein complex and its regulator from the green alga Chara braunii expands the evolutionary breadth of plant G-protein signaling.Type B Heterotrimeric G Protein γ-Subunit Regulates Auxin and ABA Signaling in Tomato.Duplicated RGS (Regulator of G-protein signaling) proteins exhibit conserved biochemical but differential transcriptional regulation of heterotrimeric G-protein signaling in Brassica species.Cloning, expression, purification, crystallization and X-ray crystallographic analysis of recombinant human C1ORF123 protein.
P2860
Q26771443-FECCF30F-8C08-4328-B61E-CF89E1A157E2Q27021549-EE0E2423-97D3-4DF6-B698-ED075F4573BDQ27334008-028F2A03-3D2C-433F-84AF-2CC18F4B4E17Q28606467-6685179C-51DC-4DCA-BD1D-6FF0660EB6A9Q30391013-3AEFC96E-8195-45F0-B9DB-6203FEB74982Q30525510-7F71DD7C-0F5D-474F-BC00-1655667E3C6AQ33359165-0F091E15-D60C-45ED-AFEC-F50B48F6469FQ33792433-3DBB5B69-92DA-492C-91DB-6746910E7D28Q34091207-E7AF45C7-CB59-42E0-99A1-F8730DA90847Q34325541-5D511840-8C75-4937-A3F4-19968F91B775Q34631839-5E28F5B1-1A69-4044-947A-7F3D5B8601ACQ34787092-ACCD2CB5-883B-4785-8CF6-4409662914BEQ35232369-21A5C2B9-CBE0-4D3B-B2D8-8519CE4EDF20Q35556696-7AD06A77-FCA7-4D7D-B6A2-F52827C78310Q35982809-7B2E6C34-90E4-4042-B28D-3E5EB00E4A60Q36599701-01B18821-4243-48A3-B27C-934B03D36706Q36744582-8B748E2C-5BB8-48F3-9ED7-54AF42068C0AQ36883853-E0288E4B-2FC6-44BB-8C42-83BAC61EF3E4Q36913114-E98C594B-A0E3-497D-AC8A-6FCD1C6B51A2Q36926766-BDCA1275-2394-46E2-91E1-25C8CBF8FBE8Q37032335-CA81E794-260E-4218-AA3A-517929FDEFB2Q37425225-9429FB9B-982F-4F18-868A-DE59C9A8E773Q38072680-607ECA9E-C3F0-461C-A3FE-56D9646B2625Q38760614-6E5BC2B7-B383-4ECB-A3C2-1578C76567B3Q38819828-D67BB14C-C667-45FD-8153-CA75830BB258Q38851305-178C7852-DE52-4A59-8FCE-5DD6D2B332A1Q38978553-777F30DA-D720-4627-904E-6AC7435A6E56Q39609863-015E8F34-468D-4083-B8B2-45892D78A61BQ40756016-7C143133-2598-4283-9CD2-92A2034D430EQ41553972-36177E4D-440F-44D9-A6ED-DFDE68997F17Q42183560-54B510D6-0B37-448D-A304-0F02DEF02BE0Q42790901-8322F5FE-2260-469E-919A-4FECC83546F6Q45920467-AA2D7E12-247F-4FCF-93F9-6C3B3DEACBDBQ46318346-14828C35-6211-4CCF-8B4D-AFD643DC384CQ46488922-EF7DB869-95AA-4BA5-AF35-8D78B3750DFFQ46786611-9F835E33-1E1C-44F4-B8D1-BBA29B57DBD3Q46976540-8C2D3711-1315-4A14-9FFC-90718D47730AQ48088364-CA387420-3F75-47C3-A72E-F66CE2528853Q48120681-E91FFFD3-0283-4950-A658-B517E8FE09BCQ48875627-C5AC34A8-A0CB-4ED8-B73A-5265D65890DB
P2860
The crystal structure of a self-activating G protein alpha subunit reveals its distinct mechanism of signal initiation.
description
2011 nî lūn-bûn
@nan
2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի փետրվարին 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
The Crystal Structure of a Sel ...... Mechanism of Signal Initiation
@nl
The crystal structure of a sel ...... echanism of signal initiation.
@ast
The crystal structure of a sel ...... echanism of signal initiation.
@en
type
label
The Crystal Structure of a Sel ...... Mechanism of Signal Initiation
@nl
The crystal structure of a sel ...... echanism of signal initiation.
@ast
The crystal structure of a sel ...... echanism of signal initiation.
@en
prefLabel
The Crystal Structure of a Sel ...... Mechanism of Signal Initiation
@nl
The crystal structure of a sel ...... echanism of signal initiation.
@ast
The crystal structure of a sel ...... echanism of signal initiation.
@en
P2093
P2860
P3181
P1433
P1476
The crystal structure of a sel ...... echanism of signal initiation.
@en
P2093
Alan M Jones
Brenda R S Temple
Henrik G Dohlman
Janice C Jones
Jeffrey W Duffy
P2860
P3181
P356
10.1126/SCISIGNAL.2001446
P577
2011-02-08T00:00:00Z