Results 21 to 30 of about 80,587 (292)

Assembly of the Drosophila 26 S proteasome is accompanied by extensive subunit rearrangements [PDF]

, 2002
The subunit contacts in the regulatory complex of the Drosophila 26 S proteasome were studied through the cross-linking of closely spaced subunits of the complex, and analysis of the cross-linking pattern in an immunoblot assay with the use of subunit ...
Kapelari, Barbara, Barbara KAPELARI, Sümegi, Máté, Baumeister, Wolfgang, Hölzl, Harald, Éva KURUCZ, Máté SÜMEGI, István ANDÓ, Harald HÖLZL, Andó, István, Kurucz, Éva, Udvardy, Andor, Andor UDVARDY, Wolfgang BAUMEISTER   +13 more
core   +2 more sources

Changes in proteasome structure and function caused by HAMLET in tumor cells. [PDF]

PLoS ONE, 2009
Proteasomes control the level of endogenous unfolded proteins by degrading them in the proteolytic core. Insufficient degradation due to altered protein structure or proteasome inhibition may trigger cell death.
Lotta Gustafsson, Sonja Aits, Patrik Onnerfjord, Maria Trulsson, Petter Storm, Catharina Svanborg   +5 more
doaj   +1 more source

Circulating 20S proteasome is independently associated with abdominal muscle mass in hemodialysis patients. [PDF]

PLoS ONE, 2015
Protein-energy wasting is highly prevalent in hemodialysis patients, and it contributes to patient morbidity and mortality. The ubiquitin-proteasome system is the major pathway for intracellular protein degradation and it is involved in the regulation of
Hirotaka Fukasawa, Mai Kaneko, Hiroki Niwa, Takashi Matsuyama, Hideo Yasuda, Hiromichi Kumagai, Ryuichi Furuya   +6 more
doaj   +1 more source

Assembly of the 20S proteasome

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2014
The proteasome is a cellular protease responsible for the selective degradation of the majority of the intracellular proteome. It recognizes, unfolds, and cleaves proteins that are destined for removal, usually by prior attachment to polymers of ubiquitin. This macromolecular machine is composed of two subcomplexes, the 19S regulatory particle (RP) and
Kunjappu, Mary J., Hochstrasser, Mark
openaire   +2 more sources

Fluorescence-based proteasome activity profiling [PDF]

, 2011
With the proteasome emerging as a therapeutic target for cancer treatment, accurate tools for monitoring proteasome (inhibitor) activity are in demand.
Jong, A., Rodenko, B., Berkers, C.R., Schuurman, K.G., Ovaa, H., Boris Rodenko, Annemieke de Jong, Celia R. Berkers, Karianne G. Schuurman, Huib Ovaa   +9 more
core   +1 more source

Tissue- and developmental stage-specific changes in the subcellular localization of the 26S proteasome in the ovary of Drosophila melanogaster [PDF]

, 2004
The intracellular localization of the 26S proteasome in the different ovarian cell types of Drosophila melanogaster was studied by means of immunofluorescence staining and laser scanning microscopy, with the use of antibodies specific for regulatory ...
Andó, István, Kurucz, Éva, Udvardy, Andor, Gausz, János, Ádám, Géza, Noselli, Stéphane   +5 more
core   +1 more source

Redox regulation of the proteasome via S-glutathionylation

Redox Biology, 2014
The proteasome is a multimeric and multicatalytic intracellular protease responsible for the degradation of proteins involved in cell cycle control, various signaling processes, antigen presentation, and control of protein synthesis.
Marilene Demasi, Luis E.S. Netto, Gustavo M. Silva, Adrian Hand, Cristiano L.P. de Oliveira, Renata N. Bicev, Fabio Gozzo, Mario H. Barros, Janaina M.M. Leme, Erina Ohara   +9 more
doaj   +1 more source

Insulin-Degrading Enzyme Is a Non Proteasomal Target of Carfilzomib and Affects the 20S Proteasome Inhibition by the Drug

Biomolecules, 2022
Carfilzomib is a last generation proteasome inhibitor (PI) with proven clinical efficacy in the treatment of relapsed/refractory multiple myeloma. This drug is considered to be extremely specific in inhibiting the chymotrypsin-like activity of the 20S ...
Grazia Raffaella Tundo, Diego Sbardella, Francesco Oddone, Giuseppe Grasso, Stefano Marini, Maria Grazia Atzori, Anna Maria Santoro, Danilo Milardi, Francesco Bellia, Gabriele Macari, Grazia Graziani, Fabio Polticelli, Paolo Cascio, Mariacristina Parravano, Massimo Coletta   +14 more
doaj   +1 more source

Dss1 Is a 26S Proteasome Ubiquitin Receptor [PDF]

, 2014
The ubiquitin-proteasome system is the major pathway for protein degradation in eukaryotic cells. Proteins to be degraded are conjugated to ubiquitin chains that act as recognition signals for the 26S proteasome.
Hardwick, Kevin G., Hay, Ronald T., Larsen, Ida B., Kragelund, Birthe B., Tatham, Michael H, Rösner, Heike I, Kragelund, Birthe Brandt, Hay, Ronald T, Kragelund, Birthe B, Kriegenburg, Franziska, Tatham, Michael H., Rösner, Heike Ilona, Paraskevopoulos, Konstantinos, Brandstrup, Rikke, Larsen, Ida B, Medina, Bethan; id_orcid, Hartmann-Petersen, Rasmus, Gordon, Colin, Rösner, Heike I., Hardwick, Kevin G, Medina, Bethan   +20 more
core   +1 more source

Elevated plasma 20S proteasome chymotrypsin-like activity is correlated with IL-8 levels and associated with an increased risk of death in glial brain tumor patients.

PLoS ONE, 2020
IntroductionIn cancer treatment an attempt has been made to pharmacologically regulate the proteasome functions, thus the aim was to test whether 20S proteasome chymotrypsin-like (ChT-L) activity has a role in glial brain tumors. Furthermore, we analyzed
Olga Martyna Koper-Lenkiewicz, Joanna Kamińska, Joanna Reszeć, Violetta Dymicka-Piekarska, Halina Ostrowska, Maria Karpińska, Joanna Matowicka-Karna, Marzena Tylicka   +7 more
doaj   +1 more source