Distinct phosphorylation sites on the β(2)-adrenergic receptor establish a barcode that encodes differential functions of β-arrestin. - Wikidata - awgldk - TriplyDB

Distinct phosphorylation sites on the β(2)-adrenergic receptor establish a barcode that encodes differential functions of β-arrestin.

Distinct phosphorylation sites on the β(2)-adrenergic receptor establish a barcode that encodes differential functions of β-arrestin.

http://www.wikidata.org/entity/Q41883529

about

GRK2: multiple roles beyond G protein-coupled receptor desensitization Regulation of G protein-coupled receptors by allosteric ligands Crystal Structures of a Stabilized β1-Adrenoceptor Bound to the Biased Agonists Bucindolol and Carvedilol A molecular code for endosomal recycling of phosphorylated cargos by the SNX27-retromer complex Novel Structural Approaches to Study GPCR Regulation Molecular mechanisms underlying β-adrenergic receptor-mediated cross-talk between sympathetic neurons and immune cells The catalytic region and PEST domain of PTPN18 distinctly regulate the HER2 phosphorylation and ubiquitination barcodes Copper is required for oncogenic BRAF signalling and tumorigenesis Ligand-specific endocytic dwell times control functional selectivity of the cannabinoid receptor 1 G-Protein/β-Arrestin-Linked Fluctuating Network of G-Protein-Coupled Receptors for Predicting Drug Efficacy and Bias Using Short-Term Molecular Dynamics Simulation The expanding GRK interactome: Implications in cardiovascular disease and potential for therapeutic development.Arrestin-Bound Rhodopsin: A Molecular Structure and its Impact on the Development of Biased GPCR Ligands.Computational analysis of the CB1 carboxyl-terminus in the receptor-G protein complex Structure-function of the G protein-coupled receptor superfamily.Optodynamic simulation of β-adrenergic receptor signalling.A Comprehensive View of the β-Arrestinome.Quantitative phosphoproteomics unravels biased phosphorylation of serotonin 2A receptor at Ser280 by hallucinogenic versus nonhallucinogenic agonists.Probing the stoichiometry of β2-adrenergic receptor phosphorylation by targeted mass spectrometry Divergent transducer-specific molecular efficacies generate biased agonism at a G protein-coupled receptor (GPCR)Minireview: Spatial Programming of G Protein-Coupled Receptor Activity: Decoding Signaling in Health and Disease Prostaglandin receptor EP2 in the crosshairs of anti-inflammation, anti-cancer, and neuroprotection Molecular Signature That Determines the Acute Tolerance of G Protein-Coupled Receptors β2-Adrenoceptor involved in smoking-induced airway mucus hypersecretion through β-arrestin-dependent signaling.Determination of sites of U50,488H-promoted phosphorylation of the mouse κ opioid receptor (KOPR): disconnect between KOPR phosphorylation and internalization Insulin inhibits cardiac contractility by inducing a Gi-biased β2-adrenergic signaling in hearts.Loss of morphine reward and dependence in mice lacking G protein-coupled receptor kinase 5.Overlapping and opposing functions of G protein-coupled receptor kinase 2 (GRK2) and GRK5 during heart development.Overexpression of TNNI3K, a cardiac-specific MAPKKK, promotes cardiac dysfunction.Allosteric modulation of β-arrestin-biased angiotensin II type 1 receptor signaling by membrane stretch.Identification of phosphorylation sites in the COOH-terminal tail of the μ-opioid receptor A Pluridimensional View of Biased Agonism.Identification and functional characterization of the phosphorylation sites of the neuropeptide FF2 receptor.Opioid receptor desensitization: mechanisms and its link to tolerance Development and characterization of pepducins as Gs-biased allosteric agonists.G protein-coupled receptors--recent advances Co-expression of GRK2 reveals a novel conformational state of the µ-opioid receptor The stem cell-expressed receptor Lgr5 possesses canonical and functionally active molecular determinants critical to β-arrestin-2 recruitment.Dodecyl maltopyranoside enabled purification of active human GABA type A receptors for deep and direct proteomic sequencing G protein-coupled receptor (GPCR) signaling via heterotrimeric G proteins from endosomes.A broadly conserved g-protein-coupled receptor kinase phosphorylation mechanism controls Drosophila smoothened activity.

P2860

Q24624571-F121A6BF-343C-4C81-BE8F-B72A1910E1D4 Q26864384-889E58CB-9D71-4B95-9E38-BF4BADD58034 Q27679036-C5FD674B-F097-4E0C-8F05-973DE8EA372C Q27727997-D6CE2D9C-6291-4EE7-800F-0BB7C73ECE98 Q28067568-00D768AD-6EF9-4C6F-B15C-360BDAC0B396 Q28083146-B71C1EC8-2A33-4B80-8534-533C76BDD340 Q28118816-336F5450-F21E-4534-BE3F-D80B48D9DBE0 Q28237892-34EFF20E-9B6A-4CD4-B618-F1C71C3EFE78 Q28245037-4B0223AF-BF16-4A4E-B44C-473AB5B64AD8 Q28552105-B658FD98-3F66-4AB4-B4E2-57E0F81C1DAC Q30250314-2213D088-439E-4424-9558-F37DC477AFFA Q30379083-14431689-18A7-43D6-B017-AA725B9CD512 Q30385837-FFAAE62D-5363-4F44-9202-746BAE3E2731 Q30576993-8C2AD6A5-9B54-4742-B95E-8268788368F5 Q30666240-CAEAB77F-4D06-4626-9AF2-8C1D2A6D061F Q30840655-58645254-732F-4AF8-AF1B-646917A035D3 Q33583171-7E258C49-79CE-4571-BF0A-997B527D74ED Q33616665-BA8329BC-1591-4755-B589-DB4CE981CF36 Q33619504-F19D0D44-2ACB-4898-ACB1-AF235088930B Q33631599-6D83F56E-EF7B-4508-B14F-8C753E6216B3 Q33651797-E6CF96FE-AB95-4C08-9520-0619FF4106F5 Q33655870-CF9B863C-E5FB-4196-AE2C-2CA1CFBFE9E8 Q33721324-5A7160A4-1E1A-405D-8D36-29974D30F6F1 Q33728974-B5F70FA0-D52F-4442-A1DC-E01806C7F6A2 Q33959744-6959F85E-B61C-47FA-B5AE-62849FFFBEC3 Q33993802-1A841EFB-EE5D-45EB-9130-0275AB9F8CEF Q34249070-2689C3A8-2FF6-4C6B-BF9C-93D239453FAB Q34307352-4B53CB71-B61B-4139-A717-477E38AFB66C Q34317331-B668D744-B22C-49DB-ABAB-6EC3E8BD5AE8 Q34482298-65279174-1A15-47A4-AE81-371F06182527 Q34540545-C10BD09E-199C-4267-BC92-13E3E29B40EC Q34634103-15AE33C1-7E58-4613-B07A-E2CB4E814483 Q34729984-5004939F-9573-4889-82EB-83322CBFB3E2 Q34774416-E1BB4F33-26F0-490F-98D4-55AB9BC57C35 Q35065927-EA55BD09-9F23-4831-B180-BB891CCC1469 Q35078148-04FA094C-24CE-4318-A77A-7EE61D94C133 Q35080956-920E3478-E2F2-4648-88A5-0300F9286D59 Q35148408-A4A6C071-E74A-4658-9EC9-A396863ED0F0 Q35172569-E470BA24-6237-4D57-8C58-C0B82F331BA2 Q35204277-04EEB4AA-066B-4EBB-A854-7F1477AF990F

P2860

Distinct phosphorylation sites on the β(2)-adrenergic receptor establish a barcode that encodes differential functions of β-arrestin.

http://www.wikidata.org/entity/Q41883529

description

2011 nî lūn-bûn

@nan

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

2011年论文

@zh

2011年论文

@zh-cn

name

Distinct phosphorylation sites ...... ntial functions of β-arrestin.

@en

type

label

Distinct phosphorylation sites ...... ntial functions of β-arrestin.

@en

prefLabel

Distinct phosphorylation sites ...... ntial functions of β-arrestin.

@en

P1433

Q41883529-E9DD1729-EA56-4A9B-9E55-C75E82C09ABF

P1476

Q41883529-CAA9C554-F0EC-4955-A1C9-2826398A428B

P2093

Q41883529-04835CF3-62F7-44C8-9DD8-8C2209B86120

Q41883529-1E603C15-1210-4730-932A-FCC53EEB1606

Q41883529-7F529901-A3C4-44D9-9A5D-273879B52640

Q41883529-8557A258-9833-4096-9518-EB1B075E619C

Q41883529-8A4E1AB7-607F-424A-A86E-6B6B04132981

Q41883529-BB64B8AC-1758-4FDD-BF68-E73EC40F1932

Q41883529-CB2C716A-67B6-4EE3-84E4-E943A7335839

Q41883529-DCFB4A09-6323-427E-B857-37CC51AE73B9

Q41883529-F88ECCE2-8F57-403D-90A2-75A594579804

Q41883529-FDFCAF84-94E1-4042-A557-3DBFBCF8633D

P2860

Q41883529-0896B9BE-F1EC-4578-8441-4EAEAEAC1CD4

Q41883529-0C7A52F7-B357-4FFA-A32B-14C38080D3E7

Q41883529-138289CB-D04B-4AA7-A2E1-03097CC6D9B4

Q41883529-15081F7B-F2E1-46DA-BE33-EB1062EE14AE

Q41883529-15313E55-86A7-4215-BA7C-9C68B54FF88C

Q41883529-16DBB3E4-8473-4757-8296-8E87B9608906

Q41883529-1D47EAB1-B682-418D-A8BF-DB5082F02A91

Q41883529-249F2140-3A15-4A18-B64A-A9CA39C23DCD

Q41883529-24F30A61-5C9B-4EDF-BBE3-C75F42CD6331

Q41883529-31F17613-F5A7-4BC7-9E49-CC1B91B1E996

P304

Q41883529-7F408D22-BF31-443E-B7E7-FCA02AB37B1D

P31

Q41883529-37692E31-26F5-496E-8BCD-DFD402A778D3

P356

Q41883529-D9F9E96B-EF3B-442F-817C-33369670DD58

P433

Q41883529-12F6835F-A620-4F50-9226-FD124E6B640B

P478

Q41883529-B8B4261E-4661-4782-9502-4EDACA5824FD

P50

Q41883529-2088DFD0-730F-4FC4-B6B4-F228AFE2629E

Q41883529-24446A21-CCF7-4172-8F51-8F2C20011196

Q41883529-84D38E2E-3B9D-4979-9485-82C3D17B7D28

P577

Q41883529-50BBF100-192A-44A6-9E1B-CD318CFC95EE

P5875

Q41883529-2A750B49-6A5B-4742-85D2-814831468922

P698

Q41883529-C7CEBBDE-460D-466D-A95D-07A678BCC471

P921

Q41883529-CFDCA61E-F9FA-415A-87B7-C10A96528055

P932

Q41883529-1FFF6347-8475-49C8-8110-1348B7B34FFF

P356

SCISIGNAL.2001707

P1433

Science Signaling

P1476

Distinct phosphorylation sites ...... ential functions of β-arrestin

@en

P2093

Christopher M Lam

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

Erin A Bressler

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

Kelly N Nobles

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

Kunhong Xiao

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

Makoto R Hara

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

Robert J Lefkowitz

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

Ryan T Strachan

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

Seungkirl Ahn

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

Sudha K Shenoy

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

Teng-Yi Huang

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

P2860

A probability-based approach for high-throughput protein phosphorylation analysis and site localization

Desensitization, internalization, and signaling functions of beta-arrestins demonstrated by RNA interference

ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage

Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2

Functional specialization of beta-arrestin interactions revealed by proteomic analysis

Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics

Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin

Transduction of receptor signals by beta-arrestins

Identification of the G protein-coupled receptor kinase phosphorylation sites in the human beta2-adrenergic receptor

The active conformation of beta-arrestin1: direct evidence for the phosphate sensor in the N-domain and conformational differences in the active states of beta-arrestins1 and -2

P304

ra51

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

P31

scholarly article

P356

10.1126/SCISIGNAL.2001707

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

P433

185

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

P478

4

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

P50

Sudarshan Rajagopal

P577

2011-08-01T00:00:00Z

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

P5875

51596588

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

P698

21868357

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

P921

phosphorylation

P932

3415961

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