Results 31 to 40 of about 27,758 (248)

Characterization of the brain 26S proteasome and its interacting proteins

Frontiers in Molecular Neuroscience, 2010
Proteasome-mediated proteolysis is important for synaptic plasticity, neuronal development, protein quality control, and many other processes in neurons.
Hwan-Ching Tai, Henrike Besche, Alfred L Goldberg, Erin M Schuman, Erin M Schuman   +4 more
doaj   +1 more source

Ubiquitin-Like protein 5 interacts with the silencing suppressor p3 of rice stripe virus and mediates its degradation through the 26S proteasome pathway.

PLoS Pathogens, 2020
Ubiquitin like protein 5 (UBL5) interacts with other proteins to regulate their function but differs from ubiquitin and other UBLs because it does not form covalent conjugates.
Binghua Chen, Lin Lin, Yuwen Lu, Jiejun Peng, Hongying Zheng, Qiankun Yang, Shaofei Rao, Guanwei Wu, Junmin Li, Zhuo Chen, Baoan Song, Jianping Chen, Fei Yan   +12 more
doaj   +1 more source

Phosphatase UBLCP1 controls proteasome assembly [PDF]

Open Biology, 2017
Ubiquitin-like domain-containing C-terminal domain phosphatase 1 (UBLCP1), an FCP/SCP phosphatase family member, was identified as the first proteasome phosphatase.
Shuangwu Sun, Sisi Liu, Zhengmao Zhang, Wang Zeng, Chuang Sun, Tao Tao, Xia Lin, Xin-Hua Feng   +7 more
doaj   +1 more source

Depleting the 19S proteasome regulatory PSMD1 subunit as a cancer therapy strategy

Cancer Medicine, 2023
Background Proteasome inhibitors are in use in treating certain types of cancers. These drugs inhibit the catalytic activity of the 20S proteasome, shared by all the different proteasome complexes.
Julia Adler, Roni Oren, Yosef Shaul
doaj   +1 more source

Assembly, structure, and function of the 26S proteasome [PDF]

Trends in Cell Biology, 2010
The 26S proteasome is a large multiprotein complex involved in the regulated degradation of ubiquitinated proteins in the cell. The 26S proteasome has been shown to control an increasing number of essential biochemical mechanisms of the cellular lifecycle including DNA synthesis, repair, transcription, translation, and cell signal transduction ...
Lynn, Bedford, Simon, Paine, Paul W, Sheppard, R John, Mayer, Jeroen, Roelofs   +4 more
openaire   +2 more sources

Regulation of the 26S proteasome by adenovirus E1A [PDF]

The EMBO Journal, 2000
We have identified the N-terminus of adenovirus early region 1A (AdE1A) as a region that can regulate the 26S proteasome. Specifically, in vitro and in vivo co-precipitation studies have revealed that the 19S regulatory components of the proteasome, Sug1 (S8) and S4, bind through amino acids (aa) 4-25 of Ad5 E1A.
A S, Turnell, R J, Grand, C, Gorbea, X, Zhang, W, Wang, J S, Mymryk, P H, Gallimore   +6 more
openaire   +2 more sources

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

Microbiome−host proteostasis crosstalk—An emerging perspective on mechanisms and interventions toward healthy longevity

FEBS Letters, EarlyView.
Proteostasis and the gut microbiota play a key role in shaping host physiology. Microbiota‐derived metabolites, vitamins, and RNA modulate host proteostasis. Findings from model systems, including C. elegans, indicate microbes can either stabilize or disrupt host proteostasis.
Abhishek Anil Dubey, Maria Ermolaeva
wiley   +1 more source

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

FEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source

Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome

Nature Communications, 2018
The 26S proteasome consists of a core particle that is capped at each side by a regulatory particle. Here the authors present cryo-EM structures of the activated human 26S proteasome holoenzyme in three alternative open-gate states, which provides ...
Yanan Zhu, Wei Li Wang, Daqi Yu, Qi Ouyang, Ying Lu, Youdong Mao   +5 more
doaj   +1 more source