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Lysosomes and protein degradation

Biochemical Society Transactions, 1977
Considerable evidence from studies with group-specific proteinase inhibitors, in particular pepstatin, the aspartic proteinase inhibitor, implicates lysosomes in turnover of endogenous cellular proteins. Recent experiments using a new group-specific inhibitor of thiol (cysteine) proteinases, Z-Phe-Ala-diazomethyl ketone, are described.
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The degradation of proteins

Archives of Biochemistry and Biophysics, 1953
Abstract Rate equations for a degrading system based on a simple step mechanism are considered. The initial attack is assumed to occur at random. It is followed by a further random depolymerization of the intermediate fragments but, in general, at a different rate.
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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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Regulated protein degradation

Trends in Biochemical Sciences, 2005
1 Rheinberger, H-J. (2004) A history of protein biosynthesis andribosome research. In Protein Synthesis and Ribosome Structure(Nierhaus, K.H. and Wilson, D.N., eds), pp. 1–51, Wiley-VCH Verlag2 Green, A.A. et al. (1954) The structure of haemoglobin. IV. Signdetermination by the isomorphous replacement method. Proc. Roy.Soc. A225, 287–3073 Ban, N. et al.
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Ubiquitination and Degradation of Proteins

2011
Modification by ubiquitin (Ub) and ubiquitin-like proteins (UbLs) is involved in the regulation of numerous cellular processes and has therefore become an important subject of research in various areas of biomedicine. The large number of components of the system (∼1,500), most of them being ligases (∼800) that recognize their target substrates ...
Yelena, Kravtsova-Ivantsiv   +1 more
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Linkers for protein degradation

Nature Chemical Biology, 2018
The ability to subvert E3 ubiquitin ligases with small-molecule drugs offers tremendous promise for drug discovery. A new study demonstrates how structural and computational techniques can engineer and exploit unnatural protein–protein interfaces to design selective protein degraders.
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Protein degradation in bacteria

Archives of Biochemistry and Biophysics, 1953
Summary 1. Under aerobic conditions which permit growth of Escherichia coli , the rate of protein degradation, as measured by loss of labeled arginine from the acid-insoluble fraction of the culture, is at least 8 ± 2% per 30 hr. 2. When such cells grown in a synthetic medium are transferred to a secondary medium containing a complete amino ...
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Optochemical Control of Protein Degradation

ChemBioChem, 2020
AbstractOptochemical approach has been successfully utilized to regulate cellular protein degradation with a high resolution of spatiotemporal control. In this highlight, we discuss two recent developments of combining reversible optochemical functionalities with the bifunctional proteolysis targeting chimeras, or PROTACs to achieve light‐controlled ...
Peng Wu, Debasish Manna
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Eukaryotic protein degradation

Current Opinion in Cell Biology, 1990
Early studies of intracellular protein degradation revealed several properties common to all types of eukaryotic cells. Cellular proteins are continuously turning over and measurements of the fate of individual proteins have shown them to have widely differing half-lives (ranging from a few minutes to many days).
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Monitoring protein degradation

2002
Publisher Summary Protein degradation processes can be divided in two categories: bulk degradation and selective degradation of specific proteins. Individual protein species can differ in stability by several orders of magnitude. Constitutive fast turnover of a protein allows the rapid modulation of its concentration in response to changes in its ...
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