about
A Molecular Pharmacologist's Guide to G Protein-Coupled Receptor CrystallographyCoronin 1 regulates cognition and behavior through modulation of cAMP/protein kinase A signalingStabilized G protein binding site in the structure of constitutively active metarhodopsin-IIInsights into congenital stationary night blindness based on the structure of G90D rhodopsinSAS-6 engineering reveals interdependence between cartwheel and microtubules in determining centriole architectureStructural role of the T94I rhodopsin mutation in congenital stationary night blindnessTMalphaDB and TMbetaDB: web servers to study the structural role of sequence motifs in α-helix and β-barrel domains of membrane proteins.Relation between sequence and structure in membrane proteins.Molecular basis of ligand dissociation in β-adrenergic receptorsMolecular signatures of G-protein-coupled receptors.Energy landscapes as a tool to integrate GPCR structure, dynamics, and function.Relevance of rhodopsin studies for GPCR activation.Batch crystallization of rhodopsin for structural dynamics using an X-ray free-electron laserThe DRF motif of CXCR6 as chemokine receptor adaptation to adhesion.The role of internal water molecules in the structure and function of the rhodopsin family of G protein-coupled receptors.Conformational complexity of G-protein-coupled receptors.Probing Gαi1 protein activation at single-amino acid resolution.The effect of ligand efficacy on the formation and stability of a GPCR-G protein complex.Diverse activation pathways in class A GPCRs converge near the G-protein-coupling regionConserved activation pathways in G-protein-coupled receptors.Activation of CCR5 by chemokines involves an aromatic cluster between transmembrane helices 2 and 3.Tracking G-protein-coupled receptor activation using genetically encoded infrared probes.Backbone NMR reveals allosteric signal transduction networks in the β1-adrenergic receptor.Ligand-regulated oligomerization of beta(2)-adrenoceptors in a model lipid bilayer.Influence of the g- conformation of Ser and Thr on the structure of transmembrane helices.A structural insight into the reorientation of transmembrane domains 3 and 5 during family A G protein-coupled receptor activation.Coupling ligand structure to specific conformational switches in the beta2-adrenoceptor.Characterization of a conformationally sensitive TOAC spin-labeled substance P.Structural and functional characterization of alternative transmembrane domain conformations in VEGF receptor 2 activation.Molecular dynamics: A stitch in time.Convergent evolution of tertiary structure in rhodopsin visual proteins from vertebrates and box jellyfish.Retinal proteins — You can teach an old dog new tricksConformational activation of visual rhodopsin in native disc membranesStructure of β-Adrenergic ReceptorsLigands Stabilize Specific GPCR Conformations: But How?Charge-charge and cation-π interactions in ligand binding to G protein-coupled receptors3-D Structure of G Protein-coupled ReceptorsCrystal structure of rhodopsin in complex with a mini-G sheds light on the principles of G protein selectivityArrestin-1 engineering facilitates complex stabilization with native rhodopsinGPCR-SAS: A web application for statistical analyses on G protein-coupled receptors sequences
P50
Q27021865-466F5A59-0F05-4C07-A769-827198D7475BQ27315216-240A8C08-A9F2-4EFA-89A1-EC761CAEC457Q27676468-6635C1D5-3B1F-46D1-A7F3-AAB1DF2B344EQ27677322-CAB01210-C099-4A97-B5B2-A11C252F50FEQ27704285-AD265A84-D2FF-49F0-A569-859F4B62D2FAQ27722025-E838FFFC-BB37-4414-B1F4-DCF26AA95FCAQ30152874-21CA39A7-7B3A-4130-86D9-657CB0269B68Q30155090-BF7471D8-83B0-4353-81D6-AB6BDCF968E3Q34018861-DC2DDDCB-B993-4656-ADBD-5E768306587BQ34327700-D891DF56-21BC-4A12-A14F-C51200CEC9CDQ34664404-65CC50CB-4A20-433C-AEAB-15F2F9C03938Q34991031-0AE5C94B-C789-45DC-AF86-CD8E8C1DE5D4Q35841512-D618D5A9-46DF-49A6-B892-7F41EF985324Q36299479-66E74603-6F1A-416C-899E-AD5D4276B464Q36685974-558B14A6-DF5C-4A3A-ADAE-0C35D9DF18B9Q36880905-3541756C-7A3E-4365-839B-0ADCA92563F4Q36926766-944A99C8-89E6-4C69-BC0E-AAA6587A4B0EQ37200963-15E959E8-15B6-4EBD-A498-9B0CCCF44C9BQ37225841-9D1EEAD2-6FBF-4D1D-A5EF-CC262C817656Q37995724-F1E9A1C0-A26B-4198-8190-A076CE75BAA7Q39030338-16DFC19F-FC90-4BF6-8A1F-FD1DBA437FF5Q39716161-C484BB83-2B69-4093-A8B8-A27943890769Q40028443-EF830D90-26DE-4A49-9A1D-BE4A18241B13Q41823093-097B6704-2890-45A9-9439-CFFE18A66471Q43274286-14183103-C69B-4DC7-82A6-3F60059783CAQ43644119-8AA8B82D-4F8E-4176-ABFC-2E77FAA30280Q46120520-11991739-0E22-4C2C-91BF-3E7E0CA4A7D2Q46385416-378082BC-3FDC-4788-941E-68DE1FC62C78Q54341152-C902F40D-C7B0-40D0-A32F-932CFCB8CD5AQ54428377-ED3BB626-A6DF-4E18-8344-036652DDEB5DQ55282337-B8B405FD-B77D-48FB-B08A-DB74ECCF4DB2Q57637142-E461CE9B-17AA-488A-BBFC-96B5E2E1591CQ57667981-469880C3-170C-463C-900A-8A24F6E64CF6Q57667988-3DB866AE-31DD-484D-9EC2-02705DD0C0EDQ57667992-77A0535F-9DF9-4C03-B72C-E4C4DFE9C901Q57901340-FDC0E1BB-BA94-44E1-872F-2B1CE00A5E1CQ57901347-F8F5CE77-2C74-45A7-B54E-35637D2B9291Q58718025-F87D3CCF-72CD-4B40-9505-814921CD963AQ61444237-F28BCB60-5D84-4C2F-B094-B62A006B8AD2Q61737985-1C664A52-0157-4F04-B3E9-A3FA550A928F
P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Xavier Deupí
@ast
Xavier Deupí
@en
Xavier Deupí
@es
Xavier Deupí
@nl
Xavier Deupí
@sl
type
label
Xavier Deupí
@ast
Xavier Deupí
@en
Xavier Deupí
@es
Xavier Deupí
@nl
Xavier Deupí
@sl
prefLabel
Xavier Deupí
@ast
Xavier Deupí
@en
Xavier Deupí
@es
Xavier Deupí
@nl
Xavier Deupí
@sl
P108
P106
P1153
6507252395
P21
P31
P496
0000-0003-4572-9316