Fine-tuning multiprotein complexes using small molecules - Test2 - elhamkhani - TriplyDB

Fine-tuning multiprotein complexes using small molecules

Fine-tuning multiprotein complexes using small molecules

http://www.wikidata.org/entity/Q26822675

about

Direct and Propagated Effects of Small Molecules on Protein-Protein Interaction Networks Expanding the number of 'druggable' targets: non-enzymes and protein-protein interactions Deconvolution method for specific and nonspecific binding of ligand to multiprotein complex by native mass spectrometry.Ordering a Dynamic Protein Via a Small-Molecule Stabilizer Is NMR Fragment Screening Fine-Tuned to Assess Druggability of Protein–Protein Interactions?Exploration of the HIF-1α/p300 interface using peptide and Adhiron phage display technologies Inhibitors of difficult protein-protein interactions identified by high-throughput screening of multiprotein complexes.In vivo modulation of hypoxia-inducible signaling by topographical helix mimetics.Anatomy of β-strands at protein-protein interfaces.Dissecting allosteric effects of activator-coactivator complexes using a covalent small molecule ligand.Targeting the cis-dimerization of LINGO-1 with low MW compounds affects its downstream signalling Development of a capillary electrophoresis platform for identifying inhibitors of protein-protein interactions Allosteric inhibition of human factor XIa: discovery of monosulfated benzofurans as a class of promising inhibitors Small-molecule proteomimetic inhibitors of the HIF-1α-p300 protein-protein interaction.A new class of orthosteric uPAR·uPA small-molecule antagonists are allosteric inhibitors of the uPAR·vitronectin interaction Targeted inhibition of the Shroom3-Rho kinase protein-protein interaction circumvents Nogo66 to promote axon outgrowth.Probing Protein Surfaces: QSAR Analysis with Helix Mimetics.The Chemical Biology of Molecular Chaperones--Implications for Modulation of Proteostasis Conformational Restriction of Peptides Using Dithiol Bis-Alkylation Host-rabies virus protein-protein interactions as druggable antiviral targets Sekikaic acid and lobaric acid target a dynamic interface of the coactivator CBP/p300.Aptamer-based universal fluorometric sensors based on allosteric modulation of RNA-peptide interactions.Downstream Processing Technologies/Capturing and Final Purification : Opportunities for Innovation, Change, and Improvement. A Review of Downstream Processing Developments in Protein Purification.Targeting Allosteric Control Mechanisms in Heat Shock Protein 70 (Hsp70).Recent progress in the development of Toll-like receptor (TLR) antagonists.Systematic Targeting of Protein-Protein Interactions Peptidyl-Proline Isomerases (PPIases): Targets for Natural Products and Natural Product-Inspired Compounds.Validation of the Hsp70-Bag3 protein-protein interaction as a potential therapeutic target in cancer.Targeting hepatic glucose metabolism in the treatment of type 2 diabetes.3-substituted indazoles as configurationally locked 4EGI-1 mimetics and inhibitors of the eIF4E/eIF4G interaction.Fragment screening and druggability assessment for the CBP/p300 KIX domain through protein-observed 19F NMR spectroscopy.FP Tethering: a screening technique to rapidly identify compounds that disrupt protein-protein interactions.A Bifunctional Amino Acid Enables Both Covalent Chemical Capture and Isolation of in Vivo Protein-Protein Interactions.Discovery of Enzymatic Targets of Transcriptional Activators via in Vivo Covalent Chemical Capture Targeting transcription is no longer a quixotic quest Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation.Sequence context and crosslinking mechanism affect the efficiency of in vivo capture of a protein-protein interaction From Fuzzy to Function: The New Frontier of Protein-Protein Interactions.Modulators of 14-3-3 Protein-Protein Interactions.High Throughput Screen for Inhibitors of Protein-Protein Interactions in a Reconstituted Heat Shock Protein 70 (Hsp70) Complex.

P2860

Q26784027-3101C794-55D8-428A-AD37-5C4E7A5093C3 Q27003966-566F0449-9E87-425F-B2E8-B299376921AB Q27301866-D0007BE8-473E-4211-907F-81A6F6970968 Q27676154-39765BD2-CA7C-401C-BC13-94CB79933F23 Q27681373-63208664-CB86-422E-ADCE-D163A9F06035 Q27701444-E9E68433-8E74-4C01-A069-F254FEB81C80 Q30546915-7F2A62E7-E490-43BC-8660-6190087D9A8E Q33694597-AACBB687-74D8-44E0-A28A-7F42C195129B Q34061140-5B60BB16-DDBA-45E5-AF33-E12C1B87C106 Q34083040-B8DA7981-E9C0-4FD6-8E02-8EBFB947CC8B Q34994532-09E1CF61-5F9B-43E1-B44D-FFCA0D8903BF Q34995711-8E7D4405-8C47-44E6-B23C-DF0A393C9AEF Q35049040-43591803-AE55-467C-9A5B-471344EF9443 Q35159929-61C64002-154B-46C1-BB70-A28281943899 Q35559411-8159B36E-9AEC-402D-9E24-EDD8310F8FBF Q35743266-895933D0-FD56-4DE1-B2F3-3918298A6E10 Q35874377-64F0D37D-0B56-4040-BCBD-E051F30C9A82 Q36059002-9E916207-E004-4E82-BA5B-5EDB400977A4 Q36120663-970C75B0-F7CE-4C53-AC4B-75AC00FFDC32 Q36673276-DD2D388F-91AF-4218-A98A-E3DB0B75C061 Q37011508-34C6A247-DAE7-4910-BD00-9DA14ECA4B7F Q38306028-46F22DA4-C118-4E2D-8F17-E1FCEB6A0E56 Q38631194-271FB83B-8D1F-4C69-B221-9A3DFB523297 Q38806853-7CBCB915-D6BE-4315-965B-82B466201350 Q38823065-B90515D7-2778-4507-800F-D847F74AA2F4 Q38856802-3208363C-57D7-4749-9BBD-4DF516175190 Q38895022-313C9D59-1A4E-4DBD-80A2-D87D6FD6FC9F Q38922557-8EF0DB92-1086-49E8-913F-837A9065DD7A Q38925481-44E2D258-24EE-47EC-8258-C1BC98E5311A Q39031191-342F850A-A099-4250-BA04-FABDE35FE633 Q39043214-E2C60E8F-D9AF-4605-941C-30F98A69C3AD Q39085729-639BE31D-9DF9-4607-A14A-BD9D7B4566C2 Q39102926-3A5363FD-0B8B-4303-94C5-74FC4119C02E Q39406767-F2E93FF7-BFE0-402A-A781-6403583AECF0 Q41552169-2C0C6ABC-8811-4E0C-A004-5B50BA77F7AE Q41884789-94C50334-CCC7-4F62-9679-E280DA0C5EF0 Q42112672-8B452F93-3137-445C-B2D8-D9A93350014A Q46522186-A4EBA7CF-CF8D-4883-96DB-89622B626B5D Q47610334-55D731C6-F060-47A6-AC9F-E50E432D530C Q50134093-204B2237-DBB7-4355-9A8A-AEE55F567547

P2860

Fine-tuning multiprotein complexes using small molecules

http://www.wikidata.org/entity/Q26822675

description

2012 nî lūn-bûn

@nan

2012 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի օգոստոսին 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

Fine-tuning multiprotein complexes using small molecules

@ast

Fine-tuning multiprotein complexes using small molecules

@en

Fine-tuning multiprotein complexes using small molecules

@nl

type

label

Fine-tuning multiprotein complexes using small molecules

@ast

Fine-tuning multiprotein complexes using small molecules

@en

Fine-tuning multiprotein complexes using small molecules

@nl

prefLabel

Fine-tuning multiprotein complexes using small molecules

@ast

Fine-tuning multiprotein complexes using small molecules

@en

Fine-tuning multiprotein complexes using small molecules

@nl

P1433

Q26822675-EF144A4B-1F6D-46B7-B053-24662B5B4EC4

P1476

Q26822675-86D79627-E0B1-4A97-9792-595F31CE3AED

P2093

Q26822675-32C6A6CF-AC2A-4E70-961E-A182F805C54E

Q26822675-9F0C0DAC-736A-434A-9147-ABDAA734426D

Q26822675-E5DA595F-6593-49F1-8270-1A26E8CDA8C7

P2860

Q26822675-0120A97D-C93F-4671-B5AE-34D2BF2A89AC

Q26822675-02D9FF1C-53AC-4FF1-A685-7503C86F0B33

Q26822675-04A5AFE5-78BC-4FDF-A2E0-09E06368F2CF

Q26822675-097A4E97-3C4A-4C86-9439-F35D2D45E7D0

Q26822675-09C718EF-77F4-414D-BFA8-A6CAB0A39889

Q26822675-0BDA5898-9CA7-4E5F-92E7-AB17534358AB

Q26822675-0D971EF8-866A-4195-84CA-90F15366D214

Q26822675-0FFFBCCE-B0E7-4ED4-B46B-0E5A75DBE8E7

Q26822675-17B59CAE-9364-41F4-A512-546F41C7F60D

Q26822675-18F6E24E-C632-4705-BD8E-C705645391F1

P304

Q26822675-05A4D95B-56DC-4235-933B-0A4BDF6F7534

P31

Q26822675-8B3C08EF-7C46-4BDA-AD06-B2FEFE951314

P356

Q26822675-9FBD7B3A-4A4C-4ED9-9407-08B233338E93

P407

Q26822675-2792BB30-C821-43D5-BECB-612D88D75350

P433

Q26822675-E1A2C1EF-09DE-45D1-A202-636055F547BE

P478

Q26822675-4576717B-4EA7-4677-AD07-2A6D89AF5644

P50

Q26822675-5A1E8D17-4AF7-4AFB-8F9A-D8D8DFE3E674

P577

Q26822675-731C4B8E-CEDB-4AC5-A268-9D13549723CE

P698

Q26822675-FDDE980E-4E5B-4BD0-A269-B723C893F356

P932

Q26822675-87CEB82F-8C7C-49CA-A275-CE8EC58BFB85

P356

P1433

ACS Chemical Biology

P1476

Fine-tuning multiprotein complexes using small molecules

@en

P2093

Andrea D Thompson

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

Anna K Mapp

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

Jason E Gestwicki

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

P2860

Towards a proteome-scale map of the human protein–protein interaction network

Structure of an ultraweak protein-protein complex and its crucial role in regulation of cell morphology and motility

Small molecules block the polymerization of Z alpha1-antitrypsin and increase the clearance of intracellular aggregates

Structural basis for p300 Taz2-p53 TAD1 binding and modulation by phosphorylation

Estimating the size of the human interactome

Shape shifting leads to small-molecule allosteric drug discovery

Diversity of protein-protein interactions

Role of PDZ proteins in regulating trafficking, signaling, and function of GPCRs: means, motif, and opportunity

Allosteric inhibitors of inducible nitric oxide synthase dimerization discovered via combinatorial chemistry

Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine

P304

1311-1320

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

P31

scholarly article

P356

10.1021/CB300255P

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

P407

P433

8

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

P478

7

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

P50

P577

2012-07-23T00:00:00Z

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

P698

22725693

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

P932

3517816

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