Results 71 to 80 of about 164,141 (292)

Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems. [PDF]

PLoS Pathogens, 2007
The specific and covalent addition of ubiquitin to proteins, known as ubiquitination, is a eukaryotic-specific modification central to many cellular processes, such as cell cycle progression, transcriptional regulation, and hormone signaling ...
Aurélie Angot, Annette Vergunst, Stéphane Genin, Nemo Peeters   +3 more
doaj   +1 more source

Copper homeostasis and the ubiquitin proteasome system

Metallomics, 2023
Abstract Copper is involved in many physiological pathways and important biological processes as a cofactor of several copper-dependent enzymes. Given the requirement for copper and its potential toxicity, intracellular copper levels are tightly controlled. Disturbances of human copper homeostasis are characterized by disorders of copper
Bichao Zhang, Richard Burke
openaire   +2 more sources

Multi‐omics and low‐input proteomics profiling reveals dynamic regulation driving pluripotency initiation in early mouse embryos

FEBS Open Bio, EarlyView.
Mouse pre‐implantation development involves a transition from totipotency to pluripotency. Integrating transcriptomics, epigenetic profiling, low‐input proteomics and functional assays, we show that eight‐cell embryos retain residual totipotency features, whereas cytoskeletal remodeling regulated by the ubiquitin‐proteasome system drives progression ...
Wanqiong Li, Xi Xiao, Lingbin Qi, Chanyi Li, Sirui Song, Jiaying Qin, Zhigang Xue, Jinfeng Xue, Huaifang Li   +8 more
wiley   +1 more source

Glycogen Synthase Kinase (GSK) 3β phosphorylates and protects nuclear myosin 1c from proteasome-mediated degradation to activate rDNA transcription in early G1 cells [PDF]

, 2014
Nuclear myosin 1c (NM1) mediates RNA polymerase I (pol I) transcription activation and cell cycle progression by facilitating PCAF-mediated H3K9 acetylation, but the molecular mechanism by which NM1 is regulated remains unclear.
A Cole, A Hay-Koren, A Sarshad, A Vintermist, A-S Tseng, AA Sérandour, AC O'Sullivan, Aishe A. Sarshad, AM Al-Khouri, Anne Von Euler, Bader Al-Muzzaini, CJ Fiol, D Drygin, D Wu, Douglas Lamont, DW Young, E Cavellán, E Kinoshita, E Sanij, F Mohn, GE Zentner, I Grummt, J Grisouard, J Russell, J Ye, JR Woodgett, JR Woodgett, JR Woodgett, L Meijer, Laura Borgonovo-Brandter, LC Fuentealba, M Benavides, M Liu, M Rosner, M Welcker, MA Munoz, Martin Corcoran, N Fomproix, N Visa, Neus Visa, NG Kim, P Cohen, P de Lanerolle, P Percipalle, P Percipalle, Piergiorgio Percipalle, Raffaella Santoro, RS Jope, S Boulon, T Moss, T Tasaki, T Vincent, V Stambolic, VA Smits, VF Taelman, VV Philimonenko, VW Ding, WJ Ryves, YC Tsai   +58 more
core   +5 more sources

Meta‐analysis fails to show any correlation between protein abundance and ubiquitination changes

FEBS Open Bio, EarlyView.
We analyzed over 50 published proteomics datasets to explore the relationship between protein levels and ubiquitination changes across multiple experimental conditions and biological systems. Although ubiquitination is often associated with protein degradation, our analysis shows that changes in ubiquitination do not globally correlate with changes in ...
Nerea Osinalde, Unai Alduntzin, Gorka Prieto, Ugo Mayor   +3 more
wiley   +1 more source

The ubiquitin-proteasome system in glioma cell cycle control

Cell Division, 2012
A major determinant of cell fate is regulation of cell cycle. Tight regulation of this process is lost during the course of development and progression of various tumors.
Vlachostergios Panagiotis J, Voutsadakis Ioannis A, Papandreou Christos N   +2 more
doaj   +1 more source

Development of Protacs to Target Cancer-promoting Proteins for Ubiquitination and Degradation [PDF]

, 2003
The proteome contains hundreds of proteins that in theory could be excellent therapeutic targets for the treatment of human diseases. However, many of these proteins are from functional classes that have never been validated as viable candidates for the ...
Crews, Craig M., Deshaies, Raymond J., Kim, Kyung B., Ransick, Andy, Sakamoto, Kathleen M., Stein, Bernd, Verma, Rati   +6 more
core   +1 more source

Proteasomal degradation of intracellularly expressed Amblyomin‐X limits suicide gene therapy potential in melanoma cells

FEBS Open Bio, EarlyView.
This study explores the feasibility of expressing the antitumoral protein Amblyomin‐X through a suicide gene therapy approach and investigates its intracellular fate after gene delivery. Although the gene is efficiently expressed, melanoma cells rapidly degrade the Amblyomin‐X protein via proteasome activity.
Victor Dal Posolo Cinel, Carlos DeOcesano Pereira, Aline Ramos Maia Lobba, Melissa Regina Fessel, Ana Marisa Chudzinski‐Tavassi   +4 more
wiley   +1 more source

Targeting apoptosis in solid tumors: the role of bortezomib from preclinical to clinical evidence. [PDF]

, 2007
The ubiquitin-proteasome pathway is the main proteolytic system present in the nucleus and cytoplasm of all eukaryotic cells. Apoptosis activation induced by ubiquitin-proteasome pathway inhibition makes the proteasome a new target of anticancer therapy.
AA, ADAMS, ADAMS, ADAMS, AGHAJANIAN, ALBANELL, AMIRI, AN, ANDERSEN, Antonio Russo, APPLEMAN, ARLT, BANCROFT, BANCROFT, BERENSON, Bruno Vincenzi, CHAUGHAN, CHEN, CHIARLE, CUSACK, CUSACK, Daniele Santini, DAVIES, DAVIES, DAVIS, DEMARCHI, EDELMAN, FAN, FANUCCHI, FINLEY, FRANKEL, Giuseppe Cicero, Giuseppe Tonini, HIDESHIMA, KABORE, KONDAGUNTA, KORSMEYER, KRESGE, KURLAND, LACOMBE, LAURICELLA, LEBLANC, LING, LLOYD, LUDWIG, MA, MAKI, Maria E Fratto, MARX, MELINO, MYUNG, OCEAN, PRICE, RYAN, SAYER, SCHELMAN, SCHMID, SHINORA, STEVENSON, SUN, SUNWOO, SUNWOO, TEICHER, Valentina Agnese, Valentina Schiró, Viviana Bazan, VOORTMAN, WANG, WANG, WILKINSON, WILLIAMS, YANG   +71 more
core   +1 more source

Large‐scale bidirectional arrayed genetic screens identify OXR1 and EMC4 as modifiers of αSynuclein aggregation

FEBS Open Bio, EarlyView.
Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane, Lea Nikolić, Lorenzo Maraio, Thomas Goiran, Nathan Karpilovsky, Stefano Sellitto, Vangelis Bouris, Jiang‐An Yin, Ronald Melki, Edward A Fon, Adriano Aguzzi, Elena De Cecco   +11 more
wiley   +1 more source