Structural and dynamical changes in an alpha-subunit of a heterotrimeric G protein along the activation pathway.
about
β-Arrestin-1 directly interacts with Gαs and regulates its functionComputational Simulation of the Activation Cycle of Gα Subunit in the G Protein Cycle Using an Elastic Network ModelStructural determinants of nitroxide motion in spin-labeled proteins: Solvent-exposed sites in helix B of T4 lysozymeHelix Dipole Movement and Conformational Variability Contribute to Allosteric GDP Release in Gα i Subunits † , ‡Structural origin of weakly ordered nitroxide motion in spin-labeled proteinsStructural origins of nitroxide side chain dynamics on membrane protein α-helical sites.A transient interaction between the phosphate binding loop and switch I contributes to the allosteric network between receptor and nucleotide in Gαi1.Chemogenomic analysis of G-protein coupled receptors and their ligands deciphers locks and keys governing diverse aspects of signallingActivation of G protein-coupled receptors: beyond two-state models and tertiary conformational changes.Trp fluorescence reveals an activation-dependent cation-pi interaction in the Switch II region of Galphai proteins.Myristoylation exerts direct and allosteric effects on Gα conformation and dynamics in solution.Principles and determinants of G-protein coupling by the rhodopsin-like thyrotropin receptor.RETRACTED: Structural basis for nucleotide exchange on G alpha i subunits and receptor coupling specificity.Exploring the correlation between the sequence composition of the nucleotide binding G5 loop of the FeoB GTPase domain (NFeoB) and intrinsic rate of GDP release.Interaction of a G protein with an activated receptor opens the interdomain interface in the alpha subunit.The guanine nucleotide exchange factor Ric-8A induces domain separation and Ras domain plasticity in Gαi1.A positive genotype-phenotype correlation in a large cohort of patients with Pseudohypoparathyroidism Type Ia and Pseudo-pseudohypoparathyroidism and 33 newly identified mutations in the GNAS geneStructure and dynamics of a conformationally constrained nitroxide side chain and applications in EPR spectroscopy.Mapping allosteric connections from the receptor to the nucleotide-binding pocket of heterotrimeric G proteinsVisual rhodopsin sees the light: structure and mechanism of G protein signaling.Conformational flexibility and structural dynamics in GPCR-mediated G protein activation: a perspective.Linking receptor activation to changes in Sw I and II of Gα proteins.Conformational dynamics of a G-protein α subunit is tightly regulated by nucleotide binding.Ric-8A, a G protein chaperone with nucleotide exchange activity induces long-range secondary structure changes in Gα.Probing structural transitions in both structured and disordered proteins using site-directed spin-labeling EPR spectroscopy.Allosteric mechanisms of G protein-Coupled Receptor signaling: a structural perspective.GPCR: G protein complexes--the fundamental signaling assembly.Structural Elements in the Gαs and Gαq C Termini That Mediate Selective G Protein-coupled Receptor (GPCR) Signaling.Invited review: Activation of G proteins by GTP and the mechanism of Gα-catalyzed GTP hydrolysis.Exploring allosteric coupling in the alpha-subunit of heterotrimeric G proteins using evolutionary and ensemble-based approaches.Nanosecond Dynamics of Gαi1 Bound to Nucleotides or Ric-8A, a Gα Chaperone with GEF Activity.Structure of the parathyroid hormone receptor C terminus bound to the G-protein dimer Gbeta1gamma2.From molecular details of the interplay between transmembrane helices of the thyrotropin receptor to general aspects of signal transduction in family a G-protein-coupled receptors (GPCRs).Defects in vesicle core induced by escherichia coli dihydroorotate dehydrogenase.Dynamic regulation of GDP binding to G proteins revealed by magnetic field-dependent NMR relaxation analyses.Electron paramagnetic resonance studies of functionally active, nitroxide spin-labeled peptide analogues of the C-terminus of a G-protein alpha subunitA GTPase chimera illustrates an uncoupled nucleotide affinity and release rate, providing insight into the activation mechanism.Site-directed spin labeling electron paramagnetic resonance study of the ORF1 protein from a mouse L1 retrotransposon.Gi- and Gs-coupled GPCRs show different modes of G-protein binding.Development of an antibody fragment that stabilizes GPCR/G-protein complexes
P2860
Q24311927-0E39366B-441A-4579-8943-2BA0ADA516BDQ27334008-BDC610AC-C191-48F8-88F0-A4EA84E1DA28Q27649381-00CBB21F-F436-4095-BB22-05BECDF93F43Q27653830-5A99F534-84B3-4A08-9359-48439B395661Q27655050-7631B41B-F0D5-4838-9FEB-AF08884DAC66Q27665260-EA4D5665-2D46-40D2-8748-1E584D450538Q27681985-FDB45EB0-C8FE-491D-BB51-6DADF3EB299DQ28477082-C8D17C17-A814-45F4-A5AE-15CD9126B5F0Q30364526-35787E32-224E-4B8A-AB34-6A30FF047A5DQ30380798-FA41AD51-1B76-47C5-916B-40752A54DA3FQ30413000-EC3D6279-0976-4CC5-B2AE-01E4C5208E89Q33543757-19C0527E-AF87-4783-BBA5-670243DBA380Q34607766-E86D7398-159B-43B5-B4DF-8E52D411FB15Q34706791-4C265A2E-0B5C-48B1-A4E5-2F00943F04ABQ35034989-B9CB7550-D1C1-404B-88A7-68D21A848E47Q35062664-82DC8DF5-5EA9-4B32-9786-94469D537639Q35198908-8D8BDA8E-A8AB-492E-85DE-4474F0B4D24EQ35239853-9B547814-654B-4125-B6D5-9B6A4BDB5325Q35808811-FBA4A547-F1D6-46FC-AEA1-A5D507EED50DQ36731889-E8A5F8F6-EDE3-48EC-ADCC-F779886E14DCQ36941174-610A4A55-20E5-4A99-AAD7-2EE2CB08C88FQ37053797-26E54CFB-677D-475C-85BC-FDC820DF3F10Q37065226-DFB287E0-3190-472D-942F-D692D857578DQ37530904-B87BE7D1-90FB-4163-99A9-752C78F163A1Q37847124-159D2577-2D6E-4223-9BA3-0DBCE6B1F6F6Q37952607-E8E1CE73-AD92-41E3-8084-6965B22BE232Q38139871-C04FD831-10A2-4BF8-BCD2-3D5D3C3CFDA6Q38762896-6F427A3C-9C2C-47BC-B45A-F366FDCE58BAQ38782431-01330032-B7DC-4530-81AA-FD9E8BA71FC0Q39019427-51337AFB-8204-4445-83C7-845BE0E30D29Q40960224-D98878F8-5F90-4A43-BDFB-B64F9CA895CFQ41791755-AE1C187A-47E1-40A7-951F-4C65E657D80CQ41883243-CE183BB3-CE4E-4E22-AFE5-E322DEF05A21Q42017507-7A7F8918-7C5E-4890-8F52-4976DF8E4004Q42320264-AF09D11E-44E0-4D06-861D-8FFDE98DC0AEQ42543408-4CD7CC29-2970-41B0-AF9D-EBA3B6AD99B7Q42552204-89DB11FC-F992-4C88-A4D7-323F8BD18A59Q42600586-EB7C079B-C534-452E-989F-0343F5570953Q49790548-D34F6B7A-BF13-4ADA-BCE1-79C96784A1C4Q58743879-487C08B4-BA4E-4F73-91B6-F420D489E8ED
P2860
Structural and dynamical changes in an alpha-subunit of a heterotrimeric G protein along the activation pathway.
description
2006 nî lūn-bûn
@nan
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Structural and dynamical chang ...... along the activation pathway.
@ast
Structural and dynamical chang ...... along the activation pathway.
@en
type
label
Structural and dynamical chang ...... along the activation pathway.
@ast
Structural and dynamical chang ...... along the activation pathway.
@en
prefLabel
Structural and dynamical chang ...... along the activation pathway.
@ast
Structural and dynamical chang ...... along the activation pathway.
@en
P2093
P2860
P356
P1476
Structural and dynamical chang ...... along the activation pathway.
@en
P2093
Heidi E Hamm
Ned Van Eps
William M Oldham
P2860
P304
16194-16199
P356
10.1073/PNAS.0607972103
P407
P577
2006-10-19T00:00:00Z