about
Crystal structure of a lipid G protein-coupled receptorStructure of a class C GPCR metabotropic glutamate receptor 1 bound to an allosteric modulatorStructural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline.Structure of the human glucagon class B G-protein-coupled receptorThe 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonistHigh-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptorOpportunities for functional selectivity in GPCR antibodiesModeling ligand recognition at the P2Y12 receptor in light of X-ray structural information.An electrostatic mechanism for Ca(2+)-mediated regulation of gap junction channels.Structural adaptations in a membrane enzyme that terminates endocannabinoid signalingCrystal structure of uronate isomerase (TM0064) from Thermotoga maritima at 2.85 A resolutionCrystal structure of gamma-glutamyl phosphate reductase (TM0293) from Thermotoga maritima at 2.0 A resolutionCrystal structure of an iron-containing 1,3-propanediol dehydrogenase (TM0920) from Thermotoga maritima at 1.3 A resolutionCrystal structure of rhodopsin bound to arrestin by femtosecond X-ray laserStructural basis for bifunctional peptide recognition at human δ-opioid receptorNuclear Magnetic Resonance Structure of the N-Terminal Domain of Nonstructural Protein 3 from the Severe Acute Respiratory Syndrome CoronavirusCrystal structure of 2-keto-3-deoxygluconate kinase (TM0067) from Thermotoga maritima at 2.05 A resolutionA Specific Cholesterol Binding Site Is Established by the 2.8 Å Structure of the Human β2-Adrenergic ReceptorStructural and Biochemical Characterization of the Therapeutic Anabaena variabilis Phenylalanine Ammonia LyaseCrystal Structure of Botulinum Neurotoxin Type A in Complex with the Cell Surface Co-Receptor GT1b—Insight into the Toxin–Neuron InteractionFunctional Proteomic and Structural Insights into Molecular Recognition in the Nitrilase Family Enzymes † ‡Conserved Binding Mode of Human β 2 Adrenergic Receptor Inverse Agonists and Antagonist Revealed by X-ray CrystallographySteroid-based facial amphiphiles for stabilization and crystallization of membrane proteins.Structural Basis for Molecular Recognition at Serotonin ReceptorsStructural Features for Functional Selectivity at Serotonin ReceptorsRational Design of Fatty Acid Amide Hydrolase Inhibitors That Act by Covalently Bonding to Two Active Site ResiduesStructure of the human smoothened receptor bound to an antitumour agentStructure of the CCR5 Chemokine Receptor-HIV Entry Inhibitor Maraviroc ComplexThe N-Terminal Sequence of Tyrosine Hydroxylase Is a Conformationally Versatile Motif That Binds 14-3-3 Proteins and MembranesSerial Femtosecond Crystallography of G Protein-Coupled ReceptorsMolecular control of δ-opioid receptor signallingLipidic cubic phase injector facilitates membrane protein serial femtosecond crystallographyStructure of the human P2Y12 receptor in complex with an antithrombotic drugAgonist-bound structure of the human P2Y12 receptorStructural basis for Smoothened receptor modulation and chemoresistance to anticancer drugsCrystal structure of botulinum neurotoxin type A and implications for toxicityGPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor functionStructural Determinants of Binding the Seven-transmembrane Domain of the Glucagon-like Peptide-1 Receptor (GLP-1R)Genetically encoded chemical probes in cells reveal the binding path of urocortin-I to CRF class B GPCRMicroscale NMR screening of new detergents for membrane protein structural biology.
P50
Q24305457-B4CDC6E5-403E-4B5F-A1E2-8E388C46358EQ24338769-6FE5DEFA-ED32-4763-9783-F0F641554E47Q24535595-FF8811E7-91DF-4AC2-B7A4-96FAE2CCFEABQ24601619-8EE421B1-87BC-49A7-9F9B-99E1E4EB148CQ24654563-7FF28210-A71E-491A-9582-A01F27B68457Q24657484-C0DE4EB5-3385-4BFC-87C4-8797EEA59F52Q26859602-0AA49754-E2E5-4BFB-80AE-E79DFAE37EC7Q27316009-73A189D8-54DF-4E96-B9DA-6F54BCF8473AQ27319376-212FE250-75B7-4336-9A77-80B71D1F8D6EQ27640068-8D964989-249D-4D00-A370-2BA0A783F92AQ27641922-37E00CDE-B23E-4213-B2AA-F00E7CF78CF0Q27642894-A5333773-4682-4745-BCED-AD5BCEC4592BQ27642900-5DA78CFC-48D4-47F5-A30D-8EF360E023CEQ27644398-E48BABF1-B58D-4203-B652-7A4C8FE17069Q27644624-02DEF2FF-B284-4FBA-B1E2-23F8C9783045Q27647633-3B5A7BE1-84FD-4C3E-A288-37796714E8B3Q27649051-6FFC24BC-C3DA-4AB1-9F01-2DBC9453CE22Q27650801-0D876E7E-D089-4D1B-BE60-DD0B4C69E9AFQ27650847-D92B99A4-C256-424C-9DCF-5569E7BCC729Q27651618-2EFBC271-21E2-464B-A2FE-00651D2BB363Q27653034-9E97AEEF-6260-44AB-BC34-3F2110B93A61Q27663654-BE9BCC7B-4B73-47A0-B27D-5C8ADBD8CDC4Q27676750-4C82C1E1-638D-4BD6-AC62-4FB7BD6A0942Q27676926-23887A76-B6CD-4B9F-999C-8921101E235BQ27676930-B1778F04-43ED-4DA4-A294-15EC91D092C1Q27677344-270DBD50-F04D-4E8C-B6E3-15BA9F0840CBQ27677951-73AC4A9A-C6DD-463C-A3BB-86E8515E431DQ27679932-B5E11F48-A290-41C2-A338-D9E02165C7B8Q27680008-8F984C11-768B-4241-B061-14038941214BQ27680992-EF5DCE92-A9AF-49B8-85B8-7BC8E8BE523DQ27681274-BC6B2437-CFDD-4C8D-95B1-C207E5214997Q27681713-5513A8DD-36D4-46EF-9A08-11EFC0EA00E5Q27682517-A88A4B7C-21BD-4FD8-942E-0F54D034C911Q27683598-FFF2B560-3E99-408C-8859-F78A27E16362Q27684635-324E3DA8-97AB-4066-94B1-DC43E102284FQ27765727-55AB853B-2F89-4D84-8519-912BBAA70440Q28254935-A3203834-1EC7-4830-9785-9585BD7043A7Q28274664-0C0C4B00-1F22-4C38-AFA7-083C15324D16Q28572982-A3AE4F77-7815-4E9E-9659-AB378330C97DQ30157675-8F63F28A-BA2A-4E82-9D51-AEB9193A9CAD
P50
description
hulumtues
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Raymond C Stevens
@en
Raymond C Stevens
@es
Raymond C Stevens
@nl
Raymond C Stevens
@sl
Raymond Stevens
@fr
type
label
Raymond C Stevens
@en
Raymond C Stevens
@es
Raymond C Stevens
@nl
Raymond C Stevens
@sl
Raymond Stevens
@fr
prefLabel
Raymond C Stevens
@en
Raymond C Stevens
@es
Raymond C Stevens
@nl
Raymond C Stevens
@sl
Raymond Stevens
@fr
P1053
K-7272-2015
P106
P21
P31
P3829
P496
0000-0002-4522-8725