Results 21 to 30 of about 17,360,329 (255)

Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation [PDF]

, 2012
Endoplasmic Reticulum (ER)-associated degradation (ERAD) discards abnormal proteins synthesized in the ER. Through coordinated actions of ERAD components, misfolded/anomalous proteins are recognized, ubiquitinated, extracted from the ER and ultimately ...
Amanda Denuc, Marfany Gemma, Denuc Isern, Amanda, Todi, S. V., Burr, A. A., Gemma Marfany, Blount Jessica R., Sokol V Todi, Todi Sokol V., Marfany i Nadal, Gemma, Jessica R Blount, Denuc Amanda, Blount, J. R., Aaron A Burr, Burr Aaron A.   +14 more
core   +2 more sources

Niclosamide prevents the formation of large ubiquitin-containing aggregates caused by proteasome inhibition. [PDF]

PLoS ONE, 2010
Protein aggregation is a hallmark of many neurodegenerative diseases and has been linked to the failure to degrade misfolded and damaged proteins. In the cell, aberrant proteins are degraded by the ubiquitin proteasome system that mainly targets short ...
Esther Gies, Inga Wilde, Jason M Winget, Maria Brack, Barak Rotblat, Carolina Arias Novoa, Aruna D Balgi, Poul H Sorensen, Michel Roberge, Thibault Mayor   +9 more
doaj   +1 more source

Proteasome inhibition-enhanced fracture repair is associated with increased mesenchymal progenitor cells in mice.

PLoS ONE, 2022
The ubiquitin/proteasome system controls the stability of Runx2 and JunB, proteins essential for differentiation of mesenchymal progenitor/stem cells (MPCs) to osteoblasts.
Hengwei Zhang, Xing Li, Jiatong Liu, Xi Lin, Lingpeng Pei, Brendan F Boyce, Lianping Xing   +6 more
doaj   +2 more sources

Fission yeast 26S proteasome mutants are multi-drug resistant due to stabilization of the pap1 transcription factor [PDF]

, 2012
Here we report the result of a genetic screen for mutants resistant to the microtubule poison methyl benzimidazol-2-yl carbamate (MBC) that were also temperature sensitive for growth.
Caroline R. Wilkinson (117644), Itaru Samejima, Mathiassen, Søs G, Penney, M., Mary Penney (117638), McInerny Christopher J., Samejima, I., Mairi Wallace (117659), Wallace Mairi, Søs G Mathiassen, Gordon Colin, Gordon, C., Wallace, Mairi, Christopher J. McInerny (117648), Hartmann-Petersen, Rasmus, Christopher J McInerny, McInerny, C.J., McInerny, Christopher J, Mary Penney, Takashi Toda (102488), Rasmus Hartmann-Petersen (117664), Toda, Takashi, Wilkinson, Caroline, Toda, T., Mathiassen Søs G., Penney, Mary, Colin Gordon, Penney Mary, Hartmann-Petersen, R., Itaru Samejima (117642), Wilkinson, C.R., Colin Gordon (117667), Hartmann-Petersen Rasmus, Søs G. Mathiassen (117654), Samejima Itaru, Wilkinson Caroline R., Mathiassen, Søs, Wilkinson, Caroline R, Rasmus Hartmann-Petersen, McInerny, Christopher, Toda Takashi, Wallace, M., Samejima, Itaru, Gordon, Colin, Takashi Toda, Mathiassen, S.G., Caroline R Wilkinson, Mairi Wallace   +47 more
core   +2 more sources

Fluorescence-based proteasome activity profiling [PDF]

, 2011
With the proteasome emerging as a therapeutic target for cancer treatment, accurate tools for monitoring proteasome (inhibitor) activity are in demand.
Jong, A., Rodenko, B., Berkers, C.R., Schuurman, K.G., Ovaa, H., Boris Rodenko, Annemieke de Jong, Celia R. Berkers, Karianne G. Schuurman, Huib Ovaa   +9 more
core   +1 more source

Assembly of the Drosophila 26 S proteasome is accompanied by extensive subunit rearrangements [PDF]

, 2002
The subunit contacts in the regulatory complex of the Drosophila 26 S proteasome were studied through the cross-linking of closely spaced subunits of the complex, and analysis of the cross-linking pattern in an immunoblot assay with the use of subunit ...
Kapelari, Barbara, Barbara KAPELARI, Sümegi, Máté, Baumeister, Wolfgang, Hölzl, Harald, Éva KURUCZ, Máté SÜMEGI, István ANDÓ, Harald HÖLZL, Andó, István, Kurucz, Éva, Udvardy, Andor, Andor UDVARDY, Wolfgang BAUMEISTER   +13 more
core   +2 more sources

Intracellular Dynamics of the Ubiquitin-Proteasome-System [version 2; referees: 3 approved]

F1000Research, 2015
The ubiquitin-proteasome system is the major degradation pathway for short-lived proteins in eukaryotic cells. Targets of the ubiquitin-proteasome-system are proteins regulating a broad range of cellular processes including cell cycle progression, gene ...
Maisha Chowdhury, Cordula Enenkel
doaj   +1 more source

The molecular basis of CRL4 ubiquitin ligase architecture, targeting and regulation [PDF]

, 2013
Members of the CUL4-RBX1-DDB1 (CRL4) E3 ubiquitin ligase family regulate multiple cellular processes including development, transcription, and DNA repair.
Fischer, Eric Sebastian
core   +1 more source

Intracellular Dynamics of the Ubiquitin-Proteasome-System [v1; ref status: indexed, http://f1000r.es/5o5]

F1000Research, 2015
The ubiquitin-proteasome system is the major degradation pathway for short-lived proteins in eukaryotic cells. Targets of the ubiquitin-proteasome-system are proteins regulating a broad range of cellular processes including cell cycle progression, gene ...
Maisha Chowdhury, Cordula Enenkel
doaj   +1 more source

Up-regulation of ubiquitin–proteasome activity upon loss of NatA-dependent N-terminal acetylation

Life Science Alliance, 2022
Inactivation of N-terminal acetyltransferase A is found to alter Rpn4 as well as E3 ligase abundance, causing up-regulation of Ubiquitin–proteasome activity.
Ilia Kats, Christian Reinbold, Marc Kschonsak, Anton Khmelinskii, Laura Armbruster, Thomas Ruppert, Michael Knop   +6 more
doaj   +1 more source