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Targeted protein degradation

Current Opinion in Chemical Biology, 2005
The ubiquitin-proteasome pathway plays a major role in cellular protein destruction and regulates fundamental cellular processes such as the cell cycle, cell signaling, and development. By altering the substrate recognition of ubiquitin-protein ligases, their robust proteolytic activity can be re-directed to recruit and accelerate the degradation of ...
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Drugs Targeting Protein—Protein Interactions

ChemInform, 2006
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF.
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Targeted protein degradation mechanisms

Drug Discovery Today: Technologies, 2019
Targeted protein degradation mediated by small molecule degraders represents an exciting new therapeutic opportunity to eliminate disease-causing proteins. These molecules recruit E3 ubiquitin ligases to the protein of interest and mediate its ubiquitination and subsequent proteolysis by the proteasome.
Yi, Zhang   +3 more
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Targeting of lysosomal proteins

Seminars in Cell & Developmental Biology, 2000
Proper cell homeostasis requires the efficient transport of a large variety of soluble acid hydrolases and transmembrane proteins from the trans-Golgi network (TGN) to lysosomes. While most of these molecules reach this degradative compartment, some transmembrane proteins, in particular, the acid hydrolase receptors are retrieved to the TGN.
Y, Rouillé, W, Rohn, B, Hoflack
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Protein targeting to peroxisomes

Biochemical Society Transactions, 1990
Peroxisomes are single-membrane-bound organelles that have important functions in cell metabolism. They are almost ubiquitous in eukaryotic cells and biochemical findings over the past 10 years have shown that they are involved in cell respiration, and also play a significant role in lipid metabolism (for reviews, see [ l , 21).
G M, Small, A S, Lewin
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Monomeric Targeted Protein Degraders

Journal of Medicinal Chemistry, 2020
The discovery and development of targeted protein degraders have become important areas of research in the field of medicinal chemistry. Inducing degradation of a target protein presents several advantages relative to simple inhibition including a potential for extended duration of action and more profound pharmacology.
Emily J. Hanan   +5 more
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Targeting of Motor Proteins

Science, 1996
Microtubules are responsible for chromosome segregation and the movement and reorganization of membranous organelles. Many aspects of microtubule-based motility can be attributed to the action of motor proteins, producing force directed toward either end of microtubules.
R B, Vallee, M P, Sheetz
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Protein–Protein Interactions as Drug Targets

Future Medicinal Chemistry, 2015
Modulation of protein-protein interactions (PPIs) is becoming increasingly important in drug discovery and chemical biology. While a few years ago this 'target class' was deemed to be largely undruggable an impressing number of publications and success stories now show that targeting PPIs with small, drug-like molecules indeed is a feasible approach ...
Skwarczynska, Malgorzata   +1 more
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Proteolysis-targeting Chimeras for Targeting Protein for Degradation

Future Medicinal Chemistry, 2019
Proteolysis-targeting chimeras (PROTACs) are an emerging tool for therapeutic intervention by reducing or eliminating disease-causing proteins. PROTACs are bifunctional molecules that consist of a target protein ligand, a linker and an E3 ligase ligand, which mediate the polyubiquitination of the target protein, ultimately leading to the target protein
Jianguo, Qi, Gang, Zhang
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SnapShot: Targeted protein degradation

Cell
Targeted protein degradation strategies leverage endogenous cellular degradation machinery to selectively eliminate a protein of interest. Emerging technologies are opening avenues in drug discovery and functional characterization of intracellular, membrane, and extracellular proteins. To view this SnapShot, open or download the PDF.
Yu, Ding, Boxun, Lu
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