Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions - Test2 - elhamkhani - TriplyDB

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

http://www.wikidata.org/entity/Q27670746

about

Discovery of positive allosteric modulators and silent allosteric modulators of the μ-opioid receptor Membrane potentials regulating GPCRs: insights from experiments and molecular dynamics simulations The Use of Multiscale Molecular Simulations in Understanding a Relationship between the Structure and Function of Biological Systems of the Brain: The Application to Monoamine Oxidase Enzymes Large-scale production and protein engineering of G protein-coupled receptors for structural studies Principles of allosteric interactions in cell signaling Molecular switches of the κ opioid receptor triggered by 6'-GNTI and 5'-GNTI.Quaternary structure of a G-protein-coupled receptor heterotetramer in complex with Gi and Gs.Endogenous vs Exogenous Allosteric Modulators in GPCRs: A dispute for shuttling CB1 among different membrane microenvironments.Preferred supramolecular organization and dimer interfaces of opioid receptors from simulated self-association Structural basis for bifunctional peptide recognition at human δ-opioid receptor Molecular control of δ-opioid receptor signalling Lipidic cubic phase injector facilitates membrane protein serial femtosecond crystallography The 2.1 Å Resolution Structure of Cyanopindolol-Bound β1-Adrenoceptor Identifies an Intramembrane Na+ Ion that Stabilises the Ligand-Free Receptor Membrane-Mediated Oligomerization of G Protein Coupled Receptors and Its Implications for GPCR Function Structural basis of Smoothened regulation by its extracellular domains Lipid receptor S1P₁ activation scheme concluded from microsecond all-atom molecular dynamics simulations Age-related differences in bitter taste and efficacy of bitter blockers Structural and energetic effects of A2A adenosine receptor mutations on agonist and antagonist binding The Influence of the 1-(3-Trifluoromethyl-Benzyl)-1H-Pyrazole-4-yl Moiety on the Adenosine Receptors Affinity Profile of Pyrazolo[4,3-e][1,2,4]Triazolo[1,5-c]Pyrimidine Derivatives Role of Annular Lipids in the Functional Properties of Leucine Transporter LeuT Proteomicelles How genetic errors in GPCRs affect their function: Possible therapeutic strategies Sequence, structure and ligand binding evolution of rhodopsin-like G protein-coupled receptors: a crystal structure-based phylogenetic analysis In search of novel ligands using a structure-based approach: a case study on the adenosine A2A receptor Cholesterol binding to ion channels Adenosine receptors as drug targets--what are the challenges?A two-state model for the diffusion of the A2A adenosine receptor in hippocampal neurons: agonist-induced switch to slow mobility is modified by synapse-associated protein 102 (SAP102)Structural and biophysical characterization of an epitope-specific engineered Fab fragment and complexation with membrane proteins: implications for co-crystallization.Membrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory.The role of experimental and computational structural approaches in 7TM drug discovery.The power of mass spectrometry in structural characterization of GPCR signaling.Structure and function of serotonin G protein-coupled receptors.NMR of Membrane Proteins: Beyond Crystals.Membrane protein structure determination by SAD, SIR, or SIRAS phasing in serial femtosecond crystallography using an iododetergent Mechanism of allosteric regulation of β2-adrenergic receptor by cholesterol.Fast iodide-SAD phasing for high-throughput membrane protein structure determination Seven perspectives on GPCR H/D-exchange proteomics methods The second extracellular loop of the adenosine A1 receptor mediates activity of allosteric enhancers Compound activity prediction using models of binding pockets or ligand properties in 3D.Structure-function of the G protein-coupled receptor superfamily.Purine (N)-Methanocarba Nucleoside Derivatives Lacking an Exocyclic Amine as Selective A3 Adenosine Receptor Agonists.

P2860

Q24605838-D78903D2-D635-4556-9A40-C5917531DD12 Q26740438-DAF6669A-8BE2-4C01-BFB7-1A6CF37491EF Q26740761-E2E96EB5-B6A0-428F-9B21-69F834220BA1 Q26866010-3CD89647-BF54-4299-A6D7-160A0FA8EE0B Q26996431-ACA0A953-3F22-43E6-BD46-5130C961E210 Q27302413-78DB14E1-FA0B-4A18-AD3B-8E4F444573AD Q27305013-638B639B-366A-40B3-8E7D-90648CB9E683 Q27308091-5426F2CF-5E57-4D80-90E2-5417CCBFDF85 Q27319797-85B9A12C-6E7D-48D1-932B-4B4A817DBF5B Q27644624-412F0FE5-D730-4143-8F64-A3EE980230F7 Q27681274-D442C42D-D6D1-45C3-BE04-7E584842EE5E Q27681713-1B687B95-6560-414E-889F-6A87A52C1754 Q27682443-3DF49965-FBE4-49E9-BD4A-C9A5A4010FE0 Q28072820-461AF1BD-C2AB-4F89-87AA-7809AC48974A Q28277263-DFE7D1D9-1B6B-4681-9B09-3568ACD38DA1 Q28534072-9E1257B8-7239-4C4B-B895-4F7B65C3288C Q28541080-A6B4D79C-6100-4362-BDF2-5FCA05562F37 Q28543560-3DBCD932-97F9-460F-A3CC-FEB4192427F1 Q28551225-DC3EC04C-D51F-4813-9E53-5CAB5F35BAA2 Q28604147-BED2AF1C-77EF-4185-8FFC-4A37E7003220 Q28646207-2E721FDF-B2AC-4A80-AE61-09E3532DFBFF Q28649590-8A2D1AC6-3A72-4D23-94CD-A172E538146C Q28820807-CB2575C6-426C-48CF-BFDA-71C4168E15C6 Q29036398-ADC88980-B8E9-460D-A2A8-94FBADD20D99 Q29346491-BD1E6546-08C3-408D-A229-383558133C03 Q30009464-22BA9203-79CA-4F5A-909B-9F45D935F5C1 Q30152958-21B19682-57CC-4D3F-B2CC-67FDD20DDEF9 Q30375519-1DC55F41-8279-4C66-8DAC-DEF291D0E3C4 Q30377191-8C59CCB9-4B3A-40EB-8D5E-3C38575E7934 Q30380212-D3CB2471-9CDF-424E-9275-190A3DC56E2F Q30382524-1E0B57EB-58D4-4B52-B1F7-591DB6FB69A2 Q30392129-217CC13D-C5CD-448F-A30E-BBFD6F6800BC Q30394721-6CFE12B7-40EF-4508-B88B-4149DC34DE3E Q30395783-95E25C00-4405-49D0-BAD4-26F9CA0673CF Q30401995-DF350866-0AB0-4977-9837-8AAC8556B157 Q30402263-6D7B1DB5-16ED-41F0-9F35-B9DDD680C0AD Q30408394-B51E9772-ED84-486A-BCD5-B56E034C8C95 Q30423071-58834A87-C531-4384-ACD1-A24F49719D59 Q30576993-9FA8C010-1FB0-4783-BF60-591BA1545392 Q30793386-9E688E87-5593-4E54-BAFC-514F6B48E07D

P2860

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

http://www.wikidata.org/entity/Q27670746

description

2012 nî lūn-bûn

@nan

2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

@ast

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

@en

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

@nl

type

label

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

@ast

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

@en

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

@nl

prefLabel

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

@ast

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

@en

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

@nl

P1433

Q27670746-BB9A086E-69D6-457F-9EA4-E7B21EFBE645

P1476

Q27670746-2CF03BD5-0939-4D23-9962-D25951C3DB6A

P2093

Q27670746-01D013D4-6A08-44CA-8D26-394AB5F4DA35

Q27670746-4A61B35A-407E-4FBA-834A-7776FFEA2D29

Q27670746-4D338890-B89A-4D71-852A-CD7827A26639

Q27670746-6E6DD135-1027-43FF-B1E2-B322E5CACE0B

Q27670746-BDCAA7DF-71D2-445C-8A72-88C914793A7E

Q27670746-D8C89C3D-D829-426B-92C8-6399063536BF

Q27670746-ED56954C-5E0C-412D-A52B-208563F15036

Q27670746-EDBE7E39-3D5A-4933-8EF2-9BA2050F0BAC

P2860

Q27670746-03591BAE-EA4F-4F14-8A27-47F75378F6AC

Q27670746-04272E47-3967-44C2-BCC4-601C1780C938

Q27670746-0DC0068E-319C-4697-B1E4-4970E127517A

Q27670746-0F3F2F26-C8FF-4813-BF96-EE7656757CB4

Q27670746-12478F10-6DFB-45D8-8108-FACBDA7EE9B5

Q27670746-1BDDBFAE-4DE6-49AC-930F-9CBB345E8915

Q27670746-22919939-9321-4DCE-9F3A-F34F7F9581F0

Q27670746-25B09DF6-9BE9-4947-A9D2-77335A29F9FC

Q27670746-26E7DACC-03CA-44CB-BED2-21392BC368EC

Q27670746-2821FD76-E804-4F6F-9E56-2CFD4D117F69

P304

Q27670746-EB0E966A-D831-4692-9AD1-61E791B86B20

P31

Q27670746-B53F1842-B23A-4C3E-B9C2-02AB514538F9

P3181

Q27670746-EB0D3905-D39C-4C4F-BE57-6DE87484DDE0

P356

Q27670746-21FCD691-32ED-4C25-A789-ED891FA43A8D

P407

Q27670746-5387ACC6-A044-40F0-AF04-97459FB7E19D

P433

Q27670746-84328B3B-69A4-4C8C-9824-A6FE8D728754

P478

Q27670746-0B1D0177-EC40-428C-B87C-5AD75EE4EC65

P50

Q27670746-258FBF79-DB4E-4E12-A562-133FED0971C9

Q27670746-51DEF026-17AC-4D97-9D6A-284A3A21A8C8

Q27670746-95103E20-B46B-4CAB-8140-168D9E525EFA

Q27670746-9D241E6C-27CB-46E6-A84B-F6C723902B4C

P577

Q27670746-85348303-80C4-46E7-A626-D44F85CACFCE

P5875

Q27670746-EC74BF17-2EC1-4114-8BA9-941E590A7016

P698

Q27670746-CB7B5F75-ADBB-41BA-B8C2-090BA300574F

P921

Q27670746-0C106464-5B60-4D1C-BE00-CA1DDFCF8F95

P932

Q27670746-F62A329B-F599-41C0-82BA-0E234CEAF273

P3181

P356

SCIENCE.1219218

P1433

P1476

Structural Basis for Allosteric Regulation of GPCRs by Sodium Ions

@en

P2093

Aaron A Thompson

http://www.w3.org/2001/XMLSchema#string

Christopher B Roth

http://www.w3.org/2001/XMLSchema#string

Eugene Chun

http://www.w3.org/2001/XMLSchema#string

Fei Xu

http://www.w3.org/2001/XMLSchema#string

Gye Won Han

http://www.w3.org/2001/XMLSchema#string

Pavel Chubukov

http://www.w3.org/2001/XMLSchema#string

Raymond C Stevens

http://www.w3.org/2001/XMLSchema#string

Wei Liu

http://www.w3.org/2001/XMLSchema#string

P2860

Structure of an agonist-bound human A2A adenosine receptor

Agonist-bound adenosine A2A receptor structures reveal common features of GPCR activation

Crystal structure of a lipid G protein-coupled receptor

Structure of the human κ-opioid receptor in complex with JDTic

GPCRDB: information system for G protein-coupled receptors

Structure of the human M2 muscarinic acetylcholine receptor bound to an antagonist

Crystal structure of the β2 adrenergic receptor-Gs protein complex

MolProbity: all-atom structure validation for macromolecular crystallography

The 2.6 angstrom crystal structure of a human A2A adenosine receptor bound to an antagonist

PHENIX: a comprehensive Python-based system for macromolecular structure solution

P304

232-6

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

709823

http://www.w3.org/2001/XMLSchema#string

P356

10.1126/SCIENCE.1219218

http://www.w3.org/2001/XMLSchema#string

P407

P433

6091

http://www.w3.org/2001/XMLSchema#string

P478

337

http://www.w3.org/2001/XMLSchema#string

P50

Vsevolod Katritch

Laura H Heitman

Adriaan P IJzerman

P577

2012-07-13T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

229153789

http://www.w3.org/2001/XMLSchema#string

P698

22798613

http://www.w3.org/2001/XMLSchema#string

P921

G protein-coupled receptor

P932

3399762

http://www.w3.org/2001/XMLSchema#string