Results 31 to 40 of about 107,280 (285)

The Proteasome Activator PA200/PSME4: An Emerging New Player in Health and Disease

Biomolecules, 2022
Proteasomes comprise a family of proteasomal complexes essential for maintaining protein homeostasis. Accordingly, proteasomes represent promising therapeutic targets in multiple human diseases.
Ayse Seda Yazgili, Frédéric Ebstein, Silke Meiners   +2 more
doaj   +1 more source

Clinical Use of Proteasome Inhibitors in the Treatment of Multiple Myeloma

Pharmaceuticals, 2014
Multiple myeloma (MM) is an incurable hematological malignancy characterized by the clonal proliferation of neoplastic plasma cells. The use of proteasome inhibitors in the treatment of MM has led to significant improvements in outcomes.
Noah M. Merin, Kevin R. Kelly
doaj   +1 more source

FoxM1 is a general target for proteasome inhibitors. [PDF]

PLoS ONE, 2009
Proteasome inhibitors are currently in the clinic or in clinical trials, but the mechanism of their anticancer activity is not completely understood. The oncogenic transcription factor FoxM1 is one of the most overexpressed genes in human tumors, while ...
Uppoor G Bhat, Marianna Halasi, Andrei L Gartel   +2 more
doaj   +1 more source

Organoids in pediatric cancer research

FEBS Letters, EarlyView.
Organoid technology has revolutionized cancer research, yet its application in pediatric oncology remains limited. Recent advances have enabled the development of pediatric tumor organoids, offering new insights into disease biology, treatment response, and interactions with the tumor microenvironment.
Carla Ríos Arceo, Jarno Drost
wiley   +1 more source

Immunoproteasome Activity in Chronic Lymphocytic Leukemia as a Target of the Immunoproteasome-Selective Inhibitors

Cells, 2022
Targeting proteasome with proteasome inhibitors (PIs) is an approved treatment strategy in multiple myeloma that has also been explored pre-clinically and clinically in other hematological malignancies.
Andrej Besse, Marianne Kraus, Max Mendez-Lopez, Elmer Maurits, Herman S. Overkleeft, Christoph Driessen, Lenka Besse   +6 more
doaj   +1 more source

Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10

FEBS Letters, EarlyView.
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang, Satoshi Hashimoto, Sota Ito, Chisato Kikuguchi, Miho Hoshi, Kiyoshi Yamaguchi, Yoichi Furukawa, Toru Suzuki, Toshifumi Inada   +8 more
wiley   +1 more source

Small interfering RNA targeting mcl-1 enhances proteasome inhibitor-induced apoptosis in various solid malignant tumors

BMC Cancer, 2011
Background Targeting the ubiquitin-proteasome pathway is a promising approach for anticancer strategies. Recently, we found Bik accumulation in cancer cell lines after they were treated with bortezomib.
Zhou Wei, Hu Jingzi, Tang Haimei, Wang Da, Huang Xuefeng, He Chao, Zhu Hongbo   +6 more
doaj   +1 more source

The role of histone modifications in transcription regulation upon DNA damage

FEBS Letters, EarlyView.
This review discusses the critical role of histone modifications in regulating gene expression during the DNA damage response (DDR). By modulating chromatin structure and recruiting repair factors, these post‐translational modifications fine‐tune transcriptional programmes to maintain genomic stability.
Angelina Job Kolady, Siyao Wang
wiley   +1 more source

New proteasome inhibitors in the treatment of multiple myeloma

Hematology, Transfusion and Cell Therapy, 2019
The treatment of patients with relapsed and/or refractory multiple myeloma has improved considerably in the last 15 years, after the introduction of proteasome inhibitors and immunomodulatory drugs.
Vania Tietsche de Moraes Hungria, Edvan de Queiroz Crusoé, Rosane Isabel Bittencourt, Angelo Maiolino, Roberto José Pessoa Magalhães, Jairo do Nascimento Sobrinho, Jorge Vaz Pinto, Ricardo Coutinho Fortes, Eloisa de Sá Moreira, Paula Yurie Tanaka   +9 more
doaj   +1 more source

Cell density–dependent nuclear‐cytoplasmic shuttling of SETDB1 integrates with Hippo signaling to regulate YAP1‐mediated transcription

FEBS Letters, EarlyView.
At low cell density, SETDB1 and YAP1 accumulate in the nucleus. As cell density increases, the Hippo pathway is gradually activated, and SETDB1 is associated with increased YAP1 phosphorylation. At high cell density, phosphorylated YAP1 is sequestered in the cytoplasm, while SETDB1 becomes polyubiquitinated and degraded by the ubiquitin–proteasome ...
Jaemin Eom, Jaewoong Jang, Jung Sun Park, Yong‐Kook Kang   +3 more
wiley   +1 more source