about
Structure and function of an irreversible agonist-β(2) adrenoceptor complexStructure of the human M2 muscarinic acetylcholine receptor bound to an antagonistHigh-resolution crystal structure of human protease-activated receptor 1Covalent agonists for studying G protein-coupled receptor activationCrystal structures of human IPP isomerase: new insights into the catalytic mechanismSingle-molecule force spectroscopy of G-protein-coupled receptors.Identifying and quantifying two ligand-binding sites while imaging native human membrane receptors by AFM.Cholesterol increases kinetic, energetic, and mechanical stability of the human β2-adrenergic receptor.Effective application of bicelles for conformational analysis of G protein-coupled receptors by hydrogen/deuterium exchange mass spectrometry.Crystal structure of the C-terminal domain of the ɛ subunit of human translation initiation factor eIF2B.Imaging G protein-coupled receptors while quantifying their ligand-binding free-energy landscape.Membrane binding of the insertion sequence of Proteus vulgaris L-amino acid deaminase stabilizes protein structure and increases catalytic activity.Crystal structure of Human ASB9-2 and substrate-recognition of CKB.Structures of the Human PGD Receptor CRTH2 Reveal Novel Mechanisms for Ligand RecognitionStructural insights into binding specificity, efficacy and bias of a βAR partial agonistOrthosteric and allosteric action of the C5a receptor antagonistsTrypsin inhibitory loop is an excellent lead structure to design serine protease inhibitors and antimicrobial peptidesCryo-EM Structure of the Human Cannabinoid Receptor CB2-Gi Signaling ComplexStructure of formylpeptide receptor 2-Gi complex reveals insights into ligand recognition and signalingPublisher Correction: Structural insights into binding specificity, efficacy and bias of a β2AR partial agonistDevelopment of "Plug and Play" Fiducial Marks for Structural Studies of GPCR Signaling Complexes by Single-Particle Cryo-EMG Protein-Coupled Receptors in Asthma Therapy: Pharmacology and Drug ActionCryo-EM structure of oxysterol-bound human Smoothened coupled to a heterotrimeric GiConformational Plasticity of Human Protease-Activated Receptor 1 upon Antagonist- and Agonist-Binding
P50
Q24620291-CDC077AA-DE4F-4BFB-BA68-496991AF53CCQ24628686-FEB2C846-770C-483E-BAEF-A7A718494D85Q27675402-1B5B9FBB-0659-4FB2-94CA-697F037F226AQ27684620-C6A00D2A-A350-4FDE-814C-4CE01B12DC48Q28276532-0ABAF2F3-64F1-4B46-8E57-F5CD79E6E827Q34782818-A7E3F2FD-E810-4857-B71F-5DCCC4CA308EQ36320429-2EB78552-5852-4BE0-BB33-691E7B1C6C32Q36483829-38814853-2C32-4A29-8EC4-7E1CFE637E5CQ36503945-8794E508-98C7-4540-9899-EBE547057EBFQ36922857-77CEB7DA-43A8-4D70-A565-8B888FCFE426Q37380347-5BAF0EEF-3B00-4945-ABB9-47ACD1CE06D4Q42541922-AA3DF264-DA13-4CD4-8EEB-D9C0E541D22DQ48614807-76BB3A13-D256-4C58-9C8E-4666E5B9F52FQ57029712-3A82108D-B4A6-4B29-A00F-015E9E2F6478Q57452393-58424C1A-ACCE-4722-A6EC-C28D7C3119A1Q58490040-C8ED5DC6-134B-43B1-84CD-3A2F6F1A48DCQ80033141-2794F277-372A-4D77-8202-F402A994C803Q89467834-62685E68-6ADA-4897-BAFC-B2DBD5BAB340Q89722756-3980B725-F18C-43EB-AA3C-826B810AAC28Q90033553-F315ADDB-E541-4D4B-9DA5-7E9237C5162DQ91025591-D2FEBA03-0D73-418E-B728-D8B10F54233AQ91450334-9D233F9D-9611-4739-AD5A-4FBC8F094ECCQ92548353-CF7A2F56-FED5-4120-A098-6A9F40754C1AQ92681799-C1772DAE-0980-4909-AA86-0C24B7EDE298
P50
description
researcher
@en
հետազոտող
@hy
name
Cheng Zhang
@ast
Cheng Zhang
@en
Cheng Zhang
@es
Cheng Zhang
@nl
Cheng Zhang
@sl
type
label
Cheng Zhang
@ast
Cheng Zhang
@en
Cheng Zhang
@es
Cheng Zhang
@nl
Cheng Zhang
@sl
prefLabel
Cheng Zhang
@ast
Cheng Zhang
@en
Cheng Zhang
@es
Cheng Zhang
@nl
Cheng Zhang
@sl
P1053
O-4372-2015
P106
P31
P3829
P496
0000-0001-9042-4007
P569
2000-01-01T00:00:00Z