Results 51 to 60 of about 574,104 (383)

Ubiquitination of GPCRs [PDF]

, 2011
In this chapter, we describe a method for detecting the ubiquitination status of G protein-coupled receptors (GPCRs). This involves co-expression of a GPCR with an epitope-tagged ubiquitin construct in a -heterologous mammalian expression system. Stimulus-dependent modification of the GPCR by -ubiquitin is detected by immunoprecipitation and subsequent
Adriano Marchese, Adriana Caballero
openaire   +3 more sources

Ubiquitin signaling in cell cycle control and tumorigenesis

Cell Death and Differentiation, 2020
Cell cycle progression is a tightly regulated process by which DNA replicates and cell reproduces. The major driving force underlying cell cycle progression is the sequential activation of cyclin-dependent kinases (CDKs), which is achieved in part by the
Fabin Dang, Li Nie, Wenyi Wei
semanticscholar   +1 more source

SUMO chain-induced dimerization activates RNF4 [PDF]

, 2014
Dimeric RING E3 ligases interact with protein substrates and conformationally restrain the ubiquitin-E2-conjugating enzyme thioester complex such that it is primed for catalysis.
Alejandro Rojas-Fernandez, Anna Plechanovová, Brzovic, Buchwald, Budhidarmo, Calderon-Villalobos, de Bie, Deshaies, Desterro, Desterro, Dou, Dou, Dueber, Ellis Jaffray, Feltham, Galanty, Geiss-Friedlander, Geoffroy, Geoffroy, Goddard, Goddard, Golebiowski, Guzzo, Haas, Hattersley, Hay, Hecker, Hickey, Johnson, Kang, Kravtsova-Ivantsiv, Lallemand-Breitenbach, Liew, Linke, Mace, Martin, Melchior, Michael H. Tatham, Mu, Mukhopadhyay, Mukhopadhyay, Neil Hattersley, Perry, Plechanovová, Plechanovová, Pruneda, Rodriguez, Ronald T. Hay, Saitoh, Sampson, Scheffner, Schermelleh, Shen, Song, Spencer, Sun, Tatham, Tatham, Tatham, Tatham, Vyas, Wenzel, Yin, Yin, Zhang   +64 more
core   +2 more sources

Analysis of polyubiquitin conjugates reveals that the Rpn10 substrate receptor contributes to the turnover of multiple proteasome targets [PDF]

, 2005
The polyubiquitin receptor Rpn10 targets ubiquitylated Sic1 to the 26S proteasome for degradation. In contrast, turnover of at least one ubiquitin-proteasome system (UPS) substrate, CPY*, is impervious to deletion of RPN10.
Deshaies, Raymond J., Graumann, Johannes, Lipford, J. Russell, Mayor, Thibault, Smith, Geoffrey T.   +4 more
core   +1 more source

A Ubiquitin-like Protein Unleashes Ubiquitin Ligases [PDF]

Cell, 2008
Modification of cullin-RING ubiquitin ligases by the ubiquitin-like molecule Nedd8 promotes substrate ubiquitination. A crystal structure of a cullin modified by Nedd8 recently reported in Cell (Duda et al., 2008) and a biochemical study in Molecular Cell (Saha and Deshaies, 2008) reveal the dramatic impact on the ligase machinery by conjugation of ...
Ning Zheng, Ning Zheng, Nabiha Huq Saifee   +2 more
openaire   +3 more sources

RNF4-Dependent Oncogene Activation by Protein Stabilization

Cell Reports, 2016
Ubiquitylation regulates signaling pathways critical for cancer development and, in many cases, targets proteins for degradation. Here, we report that ubiquitylation by RNF4 stabilizes otherwise short-lived oncogenic transcription factors, including β ...
Jane J. Thomas, Mona Abed, Julian Heuberger, Rostislav Novak, Yaniv Zohar, Angela P. Beltran Lopez, Julie S. Trausch-Azar, Ma. Xenia G. Ilagan, David Benhamou, Gunnar Dittmar, Raphael Kopan, Walter Birchmeier, Alan L. Schwartz, Amir Orian   +13 more
doaj   +1 more source

Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4 [PDF]

, 2014
The small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and stress response.
A Hershko, A Plechanovova, A Plechanovova, A Rojas-Fernandez, AM Weissman, AT Brunger, AT Namanja, CC Chang, CH Cheng, CM Hecker, CM Pickart, CW Liew, D Reverter, E Escobar-Cabrera, ES Johnson, F Ikeda, FM Lin, GNB Yip, H Sun, HD Ulrich, HY Sun, I Matic, J Marchant, J Prudden, J Song, J Song, J Xia, JD Schnell, JH Hurley, JL Battiste, JS Thrower, K Keusekotten, L Deng, M Ottiger, M Zweckstetter, MH Tatham, MH Tatham, MJ Eddins, MJ Eddins, MR Hansen, MS Rodriguez, N Sekiyama, N Zhang, O Kerscher, O Kerscher, Q Wang, R Bruderer, R Lescasse, R Mahajan, R Varadan, RT Hay, S-R Tzeng, SC Panchal, W Rieping, W-C Huang, XD Zhang, Y Shen, Y Xie   +57 more
core   +3 more sources

Ubiquitination accomplished: E1 and E2 enzymes were not necessary [PDF]

, 2016
Qiu et al. (2016) show that a mono-ADP-ribosyltransferase, SdeA, from Legionella pneumophila catalyzes ADP-ribosylation of ubiquitin, allowing SdeA to modify substrate with ubiquitin in the absence of E1 and E2 ...
Huang, Danny T., Nakasone, Mark
core   +1 more source

Targeting E3 ubiquitin ligases to sensitize cancer radiation therapy

Precision Radiation Oncology, 2019
Radiotherapy is an effective treatment for many cancer patients to eliminate malignant cells and increase survival rate. However, cancer cells can develop resistance in response to radiation through activation of signaling pathways that promote cell ...
Zan Chen, Wei Xu
doaj   +1 more source

Ubiquitin Pathway in VHL Cancer Syndrome

Neoplasia: An International Journal for Oncology Research, 2006
The physiologic response to changes in cellular oxygen tension is ultimately governed by a heterodimeric transcription factor called hypoxia-inducible factor (HIF), which, in adaptation to compromised oxygen availability, transactivates a myriad of genes,
Michael Ohh
doaj   +1 more source