Results 101 to 110 of about 574,104 (383)
Detection of sequential polyubiquitylation on a millisecond timescale [PDF]
The pathway by which ubiquitin chains are generated on substrate through a cascade of enzymes consisting of an E1, E2 and E3 remains unclear. Multiple distinct models involving chain assembly on E2 or substrate have been proposed.
Deshaies, Raymond J.+3 more
core +2 more sources
Ubiquitination of transcription factors in cancer: unveiling therapeutic potential
In cancer, dysregulated ubiquitination of transcription factors contributes to the uncontrolled growth and survival characteristics of tumors. Tumor suppressors are degraded by aberrant ubiquitination, or oncogenic transcription factors gain stability through ubiquitination, thereby promoting tumorigenesis.
Dongha Kim, Hye Jin Nam, Sung Hee Baek
wiley +1 more source
Uncovering Ubiquitin and Ubiquitin-like Signaling Networks
Proteomes are significantly more complex than genomes and transcriptomes due to protein processing and extensive post-translational modification (PTM) of proteins. Hundreds of different modifications exist. Release 66 of the RESID database(1) (http://www.ebi.ac.uk/RESID/) contains 559 different modifications, including small chemical modifications such
openaire +4 more sources
HECT E3 ubiquitin ligases – emerging insights into their biological roles and disease relevance
Homologous to E6AP C-terminus (HECT) E3 ubiquitin ligases play a critical role in various cellular pathways, including but not limited to protein trafficking, subcellular localization, innate immune response, viral infections, DNA damage responses and ...
Yaya Wang+4 more
semanticscholar +1 more source
Targeted protein degradation in oncology: novel therapeutic opportunity for solid tumours?
Current anticancer therapies are limited by the occurrence of resistance and undruggability of most proteins. Targeted protein degraders are novel, promising agents that trigger the selective degradation of previously undruggable proteins through the recruitment of the ubiquitin–proteasome machinery. Their mechanism of action raises exciting challenges,
Noé Herbel, Sophie Postel‐Vinay
wiley +1 more source
Triad3a induces the degradation of early necrosome to limit RipK1-dependent cytokine production and necroptosis. [PDF]
Understanding the molecular signaling in programmed cell death is vital to a practical understanding of inflammation and immune cell function. Here we identify a previously unrecognized mechanism that functions to downregulate the necrosome, a central ...
A Degterev+67 more
core +2 more sources
Nuclear prothymosin α inhibits epithelial‐mesenchymal transition (EMT) in lung cancer by increasing Smad7 acetylation and competing with Smad2 for binding to SNAI1, TWIST1, and ZEB1 promoters. In early‐stage cancer, ProT suppresses TGF‐β‐induced EMT, while its loss in the nucleus in late‐stage cancer leads to enhanced EMT and poor prognosis.
Liyun Chen+12 more
wiley +1 more source
Recognition and processing of ubiquitin-protein conjugates by the proteasome.
The proteasome is an intricate molecular machine, which serves to degrade proteins following their conjugation to ubiquitin. Substrates dock onto the proteasome at its 19-subunit regulatory particle via a diverse set of ubiquitin receptors and are then ...
D. Finley
semanticscholar +1 more source
Determination of ADP/ATP translocase isoform ratios in malignancy and cellular senescence
The individual functions of three isoforms exchanging ADP and ATP (ADP/ATP translocases; ANTs) on the mitochondrial membrane remain unclear. We developed a method for quantitatively differentiating highly similar human ANT1, ANT2, and ANT3 using parallel reaction monitoring. This method allowed us to assess changes in translocase levels during cellular
Zuzana Liblova+18 more
wiley +1 more source
The ULK1-FBXW5-SEC23B nexus controls autophagy
In response to nutrient deprivation, the cell mobilizes an extensive amount of membrane to form and grow the autophagosome, allowing the progression of autophagy.
Yeon-Tae Jeong+12 more
doaj +1 more source