Results 71 to 80 of about 393,592 (390)

Order of the Proteasomal ATPases and Eukaryotic Proteasome Assembly [PDF]

Cell Biochemistry and Biophysics, 2011
The 26S proteasome is responsible for a large fraction of the regulated protein degradation in eukaryotic cells. The enzyme complex is composed of a 20S proteolytic core particle (CP) capped on one or both ends with a 19S regulatory particle (RP). The RP recognizes and unfolds substrates and translocates them into the CP.
Robert J. Tomko, Mark Hochstrasser
openaire   +3 more sources

Rewriting the dendritic cell code in cancer—from subset identity to immunotherapeutic design

FEBS Letters, EarlyView.
Dendritic cells (DCs) play central roles in cancer immunity but are often subverted by the tumor microenvironment. This review explores the diversity of DC subsets, their functional plasticity, and emerging therapeutic strategies to reprogram DCs for enhanced antitumor responses, including vaccines, in vivo targeting, and DC‐based immunotherapies ...
Estevão Carlos Silva Barcelos, Doriana Ricciuti, Giada Mondanelli, Marco Gargaro   +3 more
wiley   +1 more source

Proteasome inhibition for treatment of leishmaniasis, Chagas disease and sleeping sickness

Nature, 2016
Chagas disease, leishmaniasis and sleeping sickness affect 20 million people worldwide and lead to more than 50,000 deaths annually. The diseases are caused by infection with the kinetoplastid parasites Trypanosoma cruzi, Leishmania spp.
Shilpi Khare, A. Nagle, Agnes Biggart, Yin H. Lai, Fang-Ping Liang, Lauren C. Davis, S. W. Barnes, Casey J. N. Mathison, E. Myburgh, E. Myburgh, Mu-Yun Gao, J. R. Gillespie, Xianzhong Liu, J. L. Tan, Monique Stinson, Ianne Rivera, Jaime Ballard, V. Yeh, T. Groessl, Glenn C. Federe, Hazel X. Y. Koh, John D. Venable, B. Bursulaya, Michael Shapiro, Mishra Pranab, G. Spraggon, Ansgar Brock, J. Mottram, J. Mottram, F. Buckner, Srinivasa P. S. Rao, B. Wen, J. Walker, T. Tuntland, V. Molteni, R. Glynne, F. Supek   +36 more
semanticscholar   +1 more source

Next-generation proteasome inhibitor oprozomib synergizes with modulators of the unfolded protein response to suppress hepatocellular carcinoma [PDF]

, 2016
Hepatocellular carcinoma (HCC) responds poorly to conventional systemic therapies. The first-in-class proteasome inhibitor bortezomib has been approved in clinical use for hematologic malignancies and has shown modest activity in solid tumors, including ...
Bogaerts, Eliene, Coucke, Céline, Devisscher, Lindsey, Geerts, Anja, Laukens, Debby, Libbrecht, Louis, Paridaens, Annelies, Raevens, Sarah, Van Steenkiste, Christophe, Van Vlierberghe, Hans, Vandewynckel, Yves-Paul, Vandierendonck, Aster, Verhelst, Xavier   +12 more
core   +2 more sources

From omics to AI—mapping the pathogenic pathways in type 2 diabetes

FEBS Letters, EarlyView.
Integrating multi‐omics data with AI‐based modelling (unsupervised and supervised machine learning) identify optimal patient clusters, informing AI‐driven accurate risk stratification. Digital twins simulate individual trajectories in real time, guiding precision medicine by matching patients to targeted therapies.
Siobhán O'Sullivan, Lu Qi, Pierre Zalloua   +2 more
wiley   +1 more source

The novel β2-selective proteasome inhibitor LU-102 synergizes with bortezomib and carfilzomib to overcome proteasome inhibitor resistance of myeloma cells

Haematologica, 2015
Proteasome inhibitor resistance is a challenge for myeloma therapy. Bortezomib targets the β5 and β1 activity, but not the β2 activity of the proteasome.
Marianne Kraus, Juergen Bader, Paul P. Geurink, Emily S. Weyburne, Anne C. Mirabella, Tobias Silzle, Tamer B. Shabaneh, Wouter A. van der Linden, Gerjan de Bruin, Sarah R. Haile, Eva van Rooden, Christina Appenzeller, Nan Li, Alexei F. Kisselev, Herman Overkleeft, Christoph Driessen   +15 more
doaj   +1 more source

The proteasome lid triggers COP9 signalosome activity during the transition of Saccharomyces cerevisiae cells into quiescence. [PDF]

, 2019
The class of Cullin–RING E3 ligases (CRLs) selectively ubiquitinate a large portion of proteins targeted for proteolysis by the 26S proteasome. Before degradation, ubiquitin molecules are removed from their conjugated proteins by deubiquitinating enzymes,
Bramasole, Lylan, Cirigliano, Angela, Glickman, Michael H., Gurevich, Sylvia, Harshuk, Dana, Pick, Elah, Rinaldi, Teresa, Sinha, Abhishek, Yu, Zanlin   +8 more
core  

Quality Control System Response to Stochastic Growth of Amyloid Fibrils [PDF]

, 2012
We introduce a stochastic model describing aggregation of misfolded proteins and degradation by the protein quality control system in a single cell. In analogy with existing literature, aggregates can grow, nucleate and fragment stochastically. We assume
Lizana, Ludvig, Otzen, Daniel, Pigolotti, Simone, Sneppen, Kim   +3 more
core   +2 more sources

Proteasome dynamics

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2014
Proteasomes are highly conserved multisubunit protease complexes and occur in the cyto- and nucleoplasm of eukaryotic cells. In dividing cells proteasomes exist as holoenzymes and primarily localize in the nucleus. During quiescence they dissociate into proteolytic core and regulatory complexes and are sequestered into motile cytosolic clusters ...
openaire   +2 more sources

Proteasome plasticity

FEBS Letters, 2005
The 26S proteasome is responsible for regulated proteolysis of most intracellular proteins yet the focus of intense regulatory action itself. Proteasome abundance is responsive to cell needs or stress conditions, and dynamically localized to concentrations of substrates. Proteasomes are continually assembled and disassembled, and their subunits subject
Glickman, Michael H., Raveh, Dina
openaire   +2 more sources