Purification of Large Cytosolic Proteases for In Vitro Assays: 20S and 26S Proteasomes

Hain, Tobias; Berger, Hendrik; Schild, Hansjörg

doi:10.1007/978-1-62703-218-6_1

Cited by 3 publications

(1 citation statement)

References 13 publications

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“…Upon modification by ubiquitin, substrates can be degraded by the 26S proteasome in an ATP-dependent manner (30,31). The executioner of the ubiquitinproteasome pathway is the 26S proteasome, which consists of a proteolytic core particle (20S proteasome) and two regulatory particles (19S regulatory complex) (32,33). The 20S proteasome has a barrel shape characterized by twofold symmetry and contains multiple catalytic centers located within the inner cavity of a molecular cage.…”

Section: Proteasomesmentioning

confidence: 99%

The role of the ubiquitin-proteasome pathway in cancer development and treatment

Ding¹

2014

Front Biosci

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Ubiquitination is a post-translational modification that plays a role in several cellular processes including cell cycle progression, cell proliferation, DNA replication and apoptosis. Ubiquitin-mediated signaling is frequently altered in cancer cells. Several tumor suppressors and oncogenes interact with enzymes of the ubiquitin-proteasome pathway that function in ubiquitin conjugation and deconjugation. Increasing evidence indicates that the ubiquitin-proteasome system (UPS) plays an important role in cancer development. Several small molecule inhibitors of the UPS have been applied to the treatment of cancer. The current review focuses on the role of the UPS in cancer development and the development of UPS inhibitors for cancer treatment.

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Section: Proteasomesmentioning

confidence: 99%

The role of the ubiquitin-proteasome pathway in cancer development and treatment

Ding¹

2014

Front Biosci

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Immunoaffinity purification of the functional 20S proteasome from human cells via transient overexpression of specific proteasome subunits

Livinskaya

Barlev

2014

Protein Expression and Purification

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Crystal structure of a low molecular weight activator Blm-pep with yeast 20S proteasome – insights into the enzyme activation mechanism

Witkowska

Giżyńska

Grudnik

et al. 2017

Sci Rep

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Proteasomes are responsible for protein turnover in eukaryotic cells, degrading short-lived species but also removing improperly folded or oxidatively damaged ones. Dysfunction of a proteasome results in gradual accumulation of misfolded/damaged proteins, leading to their aggregation. It has been postulated that proteasome activators may facilitate removal of such aggregation-prone proteins and thus prevent development of neurodegenerative disorders. However, the discovery of pharmacologically relevant compounds is hindered by insufficient structural understanding of the activation process. In this study we provide a model peptidic activator of human proteasome and analyze the structure-activity relationship within this novel scaffold. The binding mode of the activator at the relevant pocket within the proteasome has been determined by X-ray crystallography. This crystal structure provides an important basis for rational design of pharmacological compounds. Moreover, by providing a novel insight into the proteasome gating mechanism, our results allow the commonly accepted model of proteasome regulation to be revisited.

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Purification of Large Cytosolic Proteases for In Vitro Assays: 20S and 26S Proteasomes

Cited by 3 publications

References 13 publications

The role of the ubiquitin-proteasome pathway in cancer development and treatment

The role of the ubiquitin-proteasome pathway in cancer development and treatment

Immunoaffinity purification of the functional 20S proteasome from human cells via transient overexpression of specific proteasome subunits

Crystal structure of a low molecular weight activator Blm-pep with yeast 20S proteasome – insights into the enzyme activation mechanism

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