Targeting the von Hippel–Lindau E3 Ubiquitin Ligase Using Small Molecules To Disrupt the VHL/HIF-1α Interaction
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Targeting Protein-Protein Interactions in the HIF SystemCyclic and Macrocyclic Peptides as Chemical Tools To Recognise Protein Surfaces and Probe Protein-Protein InteractionsFocusing on shared subpockets - new developments in fragment-based drug discoveryTargeting the androgen receptor with steroid conjugatesStructure-Guided Design and Optimization of Small Molecules Targeting the Protein–Protein Interaction between the von Hippel–Lindau (VHL) E3 Ubiquitin Ligase and the Hypoxia Inducible Factor (HIF) Alpha Subunit with in Vitro Nanomolar AffinitiesSmall-Molecule Inhibitors of the Interaction between the E3 Ligase VHL and HIF1αDissecting Fragment-Based Lead Discovery at the von Hippel-Lindau Protein:Hypoxia Inducible Factor 1α Protein-Protein InterfaceMultimeric Complexes among Ankyrin-Repeat and SOCS-box Protein 9 (ASB9), ElonginBC, and Cullin 5: Insights into the Structure and Assembly of ECS-type Cullin-RING E3 Ubiquitin LigasesIs NMR Fragment Screening Fine-Tuned to Assess Druggability of Protein–Protein Interactions?Discovery of novel inhibitors disrupting HIF-1α/von Hippel-Lindau interaction through shape-based screening and cascade dockingPotent and selective chemical probe of hypoxic signalling downstream of HIF-α hydroxylation via VHL inhibitionNMR approaches in structure-based lead discovery: recent developments and new frontiers for targeting multi-protein complexesTargeting Cullin-RING E3 ubiquitin ligases for drug discovery: structure, assembly and small-molecule modulation.Small-molecule inhibitors of protein-protein interactions: progressing toward the reality.HaloPROTACS: Use of Small Molecule PROTACs to Induce Degradation of HaloTag Fusion Proteins.Catalytic in vivo protein knockdown by small-molecule PROTACs.Induced protein degradation: an emerging drug discovery paradigm.Biophysical screening for the discovery of small-molecule ligands.Insights into Cullin-RING E3 ubiquitin ligase recruitment: structure of the VHL-EloBC-Cul2 complexLigand deconstruction: Why some fragment binding positions are conserved and others are notState-of-the-art strategies for targeting protein-protein interactions by small-molecule inhibitors.E3 Ubiquitin Ligase VHL Regulates Hypoxia-Inducible Factor-1α to Maintain Regulatory T Cell Stability and Suppressive Capacity.Chemical approaches to targeted protein degradation through modulation of the ubiquitin-proteasome pathwayFocused grid-based resampling for protein docking and mapping.Hypoxia as a therapy for mitochondrial disease.Characterization of biaryl torsional energetics and its treatment in OPLS all-atom force fieldsPROTAC-induced BET protein degradation as a therapy for castration-resistant prostate cancer.Role of ubiquitin ligases and the proteasome in oncogenesis: novel targets for anticancer therapies.Emerging therapies targeting the ubiquitin proteasome system in cancerBinding of small molecules at interface of protein-protein complex - A newer approach to rational drug design.Small-molecule control of intracellular protein levels through modulation of the ubiquitin proteasome systemNMR-based approaches for the identification and optimization of inhibitors of protein-protein interactions.Screening for E3-ubiquitin ligase inhibitors: challenges and opportunities.Impact of Target Warhead and Linkage Vector on Inducing Protein Degradation: Comparison of Bromodomain and Extra-Terminal (BET) Degraders Derived from Triazolodiazepine (JQ1) and Tetrahydroquinoline (I-BET726) BET Inhibitor Scaffolds.Hypoxia-inducible factor (HIF) inhibitors: a patent survey (2011-2015).Chemical Methods to Knock Down the Amyloid Proteins.Drugging the undruggable: targeting challenging E3 ligases for personalized medicine.Modular PROTAC Design for the Degradation of Oncogenic BCR-ABL.Targeted Protein Degradation by Small Molecules.Targeted protein knockdown using small molecule degraders.
P2860
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P2860
Targeting the von Hippel–Lindau E3 Ubiquitin Ligase Using Small Molecules To Disrupt the VHL/HIF-1α Interaction
description
2012 nî lūn-bûn
@nan
2012 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մարտին 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
Targeting the von Hippel–Linda ...... upt the VHL/HIF-1α Interaction
@ast
Targeting the von Hippel–Linda ...... upt the VHL/HIF-1α Interaction
@en
Targeting the von Hippel–Linda ...... upt the VHL/HIF-1α Interaction
@nl
type
label
Targeting the von Hippel–Linda ...... upt the VHL/HIF-1α Interaction
@ast
Targeting the von Hippel–Linda ...... upt the VHL/HIF-1α Interaction
@en
Targeting the von Hippel–Linda ...... upt the VHL/HIF-1α Interaction
@nl
prefLabel
Targeting the von Hippel–Linda ...... upt the VHL/HIF-1α Interaction
@ast
Targeting the von Hippel–Linda ...... upt the VHL/HIF-1α Interaction
@en
Targeting the von Hippel–Linda ...... upt the VHL/HIF-1α Interaction
@nl
P2093
P2860
P50
P3181
P356
P1476
Targeting the von Hippel–Linda ...... upt the VHL/HIF-1α Interaction
@en
P2093
Craig M Crews
Dennis L Buckley
Devin J Noblin
Hyun Seop Tae
Julien Michel
Peter C Gareiss
P2860
P304
P3181
P356
10.1021/JA209924V
P407
P577
2012-03-14T00:00:00Z