Results 81 to 90 of about 18,434,088 (294)

Overcoming platinum resistance by the disulfiram metabolite CuET in novel preclinical models of human carcinomas

Molecular Oncology, EarlyView.
Cisplatin‐resistant cancer cells survive DNA‐damaging platinum‐based treatment yet remain sensitive to CuET‐induced proteotoxic stress. The distinct mechanism of action allows CuET to overcome and eliminate cisplatin‐resistant tumour cells, unless highly expressed metallothioneins (MTs) interfere with CuET, thereby highlighting MT levels as candidate ...
Stefanos Arampatzis, Tereza Buchtová, Jirina Bartkova, Marie Lund Bay, Christoffer Lynge Halvorsen, Zuzana Machacova, Zdenek Skrott, Martin Mistrik, Ekaterina Dulina, Miguel Andujar‐Sanchez, Estrid Høgdall, Tine Henrichsen Schnack, Claus Høgdall, Berit Jul Mosgaard, Marie Boennelycke, Jacob Brink Laursen, Allan Jensen, Susanne K. Kjær, Tuula Kallunki, Robert Strauss, Jiri Bartek   +20 more
wiley   +1 more source

Mechanisms of ubiquitin-independent proteasomal degradation and their roles in age-related neurodegenerative disease

Frontiers in Cell and Developmental Biology
Neurodegenerative diseases are characterized by the progressive breakdown of neuronal structure and function and the pathological accumulation of misfolded protein aggregates and toxic protein oligomers.
Taylor R. Church, Seth S. Margolis, Seth S. Margolis   +2 more
doaj   +1 more source

Functional Diversity and Structural Disorder in the Human Ubiquitination Pathway [PDF]

, 2013
The ubiquitin-proteasome system plays a central role in cellular regulation and protein quality control (PQC). The system is built as a pyramid of increasing complexity, with two E1 (ubiquitin activating), few dozen E2 (ubiquitin conjugating) and several
Mainak Guharoy, Rita Pancsa (173029), Pallab Bhowmick, Tompa, Péter, Pallab Bhowmick (416342), Peter Tompa, Bhowmick, Pallab, Pancsa Rita, Guharoy Mainak, Bhowmick Pallab, Tompa Peter, Guharoy, Majnak, Mainak Guharoy (416343), Peter Tompa (38445), Rita Pancsa, Pancsa, Rita   +15 more
core   +1 more source

Effects of IGFBP4 deficiency on human preadipocyte proliferation and differentiation through the IGF1R/AKT pathway

FEBS Open Bio, EarlyView.
IGFBP4 knockdown (KD) impairs preadipocyte proliferation and is associated with IGF1R protein downregulation and attenuated AKT phosphorylation. The mechanisms by which IGFBP4 KD influences the IGF1R/AKT signaling pathway involve newly synthesized proteins and lysosomal degradation pathways. Created in BioRender.
Yujia Guo, Sandy Richter, Christoph Bach, Wieland Kiess, Anna Kirstein, Diana Le Duc, Antje Garten   +6 more
wiley   +1 more source

Bisretinoid Degradation and the Ubiquitin-Proteasome System [PDF]

, 2014
Bisretinoid fluorophores of retinal pigment epithelial (RPE) lipofuscin have been shown to undergo degradation in two ways, the first involving photofragmentation following photooxidation of their polyene structure and the second being enzyme-mediated and limited, thus far, to in vitro models employing horseradish peroxidase (HRP).
Janet R, Sparrow, Jilin, Zhou, Shanti Kaligotla, Ghosh, Zhao, Liu   +3 more
openaire   +2 more sources

Regulation of AMPK by the Ubiquitin Proteasome System [PDF]

The American Journal of Pathology, 2011
The 5′-AMP-activated protein kinase (AMPK) functions as a metabolic fuel gauge that is activated in response to environmental stressors to restore cellular energy balance. In the heart, AMPK coordinates the activation of glucose and fatty acid metabolic pathways to ensure increased production of myocardial ATP when required, such as during cardiac ...
Makhosazane, Zungu, Jonathan C, Schisler, M Faadiel, Essop, Chris, McCudden, Cam, Patterson, Monte S, Willis   +5 more
openaire   +2 more sources

The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity

FEBS Open Bio, EarlyView.
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav, Shweta Shweta, Manisha Malhotra, Vikash Maurya, Akhilesh Kumar   +4 more
wiley   +1 more source

Targeting Ubiquitin-Proteasome Pathway by Natural Products: Novel Therapeutic Strategy for Treatment of Neurodegenerative Diseases

Frontiers in Physiology, 2020
Misfolded proteins are the main common feature of neurodegenerative diseases, thereby, normal proteostasis is an important mechanism to regulate the neural survival and the central nervous system functionality.
Saeideh Momtaz, Saeideh Momtaz, Saeideh Momtaz, Zahra Memariani, Fardous F. El-Senduny, Nima Sanadgol, Nima Sanadgol, Fereshteh Golab, Majid Katebi, Amir Hossein Abdolghaffari, Amir Hossein Abdolghaffari, Amir Hossein Abdolghaffari, Amir Hossein Abdolghaffari, Mohammad Hosein Farzaei, Mohammad Hosein Farzaei, Mohammad Abdollahi, Mohammad Abdollahi   +16 more
doaj   +1 more source

The ubiquitin-proteasome system in colorectal cancer

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 2008
The proteasome is a multiprotein complex that regulates the stability of hundreds of cellular proteins and thus, it is implicated in virtually all cellular functions. Most of the time, to be recognized and processed by the proteasome, a protein has to be linked to a chain of ubiquitin molecules. Cell proliferation, apoptosis, angiogenesis and motility,
openaire   +3 more sources

Microglial Deubiquitinase OTUD7B Stabilizes STAT3 to Promote Neuroinflammation and Cognitive Decline in Alzheimer's Disease

Advanced Science, EarlyView.
. ABSTRACT Neuroinflammation driven by microglial activation is a defining feature of Alzheimer's disease (AD), yet the molecular mechanisms sustaining this proinflammatory state remain unclear. Here, we identify the deubiquitinase OTUD7B as a critical regulator of microglial activation and AD pathology.
Luyao Li, Hao Tang, Qin Yu, Yuyang Zhang, Binglu Shi, Ying Kong, Leiyu Xu, Jingjing Shao, Chenghong Hu, Lingyu She, Zhe Wang, Haiyi Chen, Aleksandr V. Samorodov, Gang Cao, Xia Zhao, Yi Wang   +15 more
wiley   +1 more source