Results 81 to 90 of about 254,188 (362)

Ubiquitin Ligation without a Ligase [PDF]

Developmental Cell, 2007
Classically, ubiquitination requires three enzymes acting in sequence: E1, E2, and E3. E3 ubiquitin ligases typically provide substrate specificity. An article in Molecular Cell (Hoeller et al., 2007) now describes the E3-independent monoubiquitination of certain proteins. The mechanism has interesting parallels to SUMO ligation.
openaire   +2 more sources

Cis‐regulatory and long noncoding RNA alterations in breast cancer – current insights, biomarker utility, and the critical need for functional validation

Molecular Oncology, EarlyView.
The noncoding region of the genome plays a key role in regulating gene expression, and mutations within these regions are capable of altering it. Researchers have identified multiple functional noncoding mutations associated with increased cancer risk in the genome of breast cancer patients.
Arnau Cuy Saqués, Aracele Martinez‐Mendez, John Crown, Alex Eustace   +3 more
wiley   +1 more source

Attenuation of HOIL-1L ligase activity promotes systemic autoimmune disorders by augmenting linear ubiquitin signaling

JCI Insight
Linear ubiquitin chains, which are generated specifically by the linear ubiquitin assembly complex (LUBAC) ubiquitin ligase, play crucial roles in immune signaling, including NF-κB activation. LUBAC comprises catalytic large isoform of heme-oxidized iron
Yasuhiro Fuseya, Keiichiro Kadoba, Xiaoxi Liu, Hiroyuki Suetsugu, Takeshi Iwasaki, Koichiro Ohmura, Takayuki Sumida, Yuta Kochi, Akio Morinobu, Chikashi Terao, Kazuhiro Iwai   +10 more
doaj   +1 more source

UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins

Nature Communications, 2018
The U-box ubiquitin ligase UFD-2 is one of the most abundant components of the ubiquitin proteasome system in muscle cells. Here the authors perform in vitro and in vivo experiments and show that UFD-2 has E3 ligase activity and that it ubiquitinates ...
Doris Hellerschmied, Max Roessler, Anita Lehner, Linn Gazda, Karel Stejskal, Richard Imre, Karl Mechtler, Alexander Dammermann, Tim Clausen   +8 more
doaj   +1 more source

Synthesis of Isomeric Phosphoubiquitin Chains Reveals that Phosphorylation Controls Deubiquitinase Activity and Specificity

Cell Reports, 2016
Ubiquitin is post-translationally modified by phosphorylation at several sites, but the consequences of these modifications are largely unknown. Here, we synthesize multi-milligram quantities of ubiquitin phosphorylated at serine 20, serine 57, and ...
Nicolas Huguenin-Dezot, Virginia De Cesare, Julien Peltier, Axel Knebel, Yosua Adi Kristaryianto, Daniel T. Rogerson, Yogesh Kulathu, Matthias Trost, Jason W. Chin   +8 more
doaj   +1 more source

Ubiquitin Ligases in Cholesterol Metabolism

Diabetes & Metabolism Journal, 2014
To maintain cholesterol homeostasis, the processes of cholesterol metabolism are regulated at multiple levels including transcription, translation, and enzymatic activity. Recently, the regulation of protein stability of some key players in cholesterol metabolism has been characterized.
Wei Jiang, Bao-Liang Song
openaire   +3 more sources

Tumour–host interactions in Drosophila: mechanisms in the tumour micro‐ and macroenvironment

Molecular Oncology, EarlyView.
This review examines how tumour–host crosstalk takes place at multiple levels of biological organisation, from local cell competition and immune crosstalk to organism‐wide metabolic and physiological collapse. Here, we integrate findings from Drosophila melanogaster studies that reveal conserved mechanisms through which tumours hijack host systems to ...
José Teles‐Reis, Tor Erik Rusten
wiley   +1 more source

Data for positive selection test and co-evolutionary analysis on mammalian cereblon

Data in Brief, 2019
Cereblon (CRBN) is a substrate recognition subunit of the CRL4 E3 ubiquitin ligase complex, directly binding to specific substrates for poly-ubiquitination followed by proteasome-dependent degradation of proteins.
Wataru Onodera, Toru Asahi, Naoya Sawamura   +2 more
doaj   +1 more source

Overexpression of CDT1 inhibits cell cycle progression at S phase by interacting with the mini‐chromosome maintenance complex and causes DNA damage

FEBS Open Bio, EarlyView.
CDT1 is an essential protein for DNA replication licensing that loads the MCM complex, the eukaryotic replicative DNA helicase, onto replication origins. Overexpression of CDT1 induces cell cycle arrest at the S phase. Here we showed CDT1 inhibits the progression of replication forks by interacting with the MCM complex, leading to the stalling and ...
Takashi Tsuyama, Nonoka Takayama, Rina Tanaka, Yuuki Arai, Yohko Yamaguchi, Yuko Nawata, Yutaro Azuma, Shusuke Tada   +7 more
wiley   +1 more source

Multiple ubiquitin E3 ligase genes antagonistically regulate chloroplast-associated protein degradation [PDF]

, 2023
Sabri Mohd. Ali, Na Li, Ziad Soufi, Jinrong Yao, Errin Johnson, Qihua Ling, Paul Jarvis   +6 more
openalex   +1 more source