Results 51 to 60 of about 851 (145)

Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications

MedComm, Volume 4, Issue 3, June 2023., 2023
The reversible and irreversible protein posttranslational modifications, such as acetylation, methylation, phosphorylation, ubiquitination, glycosylation, SUMOylation, and redox modifications, are essential regulators in organisms and cells. This work systematically summarizes the features, regulatory mechanisms, substrates, functions, and related ...
Qian Zhong, Xina Xiao, Yijie Qiu, Zhiqiang Xu, Chunyu Chen, Baochen Chong, Xinjun Zhao, Shan Hai, Shuangqing Li, Zhenmei An, Lunzhi Dai   +10 more
wiley   +1 more source

Temporal Integrative Omics Reveals an Increase in Nondegradative Ubiquitylation during Primary Hepatocyte Dedifferentiation

Engineering, 2020
Primary hepatocytes (PHCs) are widely used in various fields, but the progressive deterioration of liver-specific features in vitro significantly limits their application.
Zhengyi Jiang, Zeyu Sun, Xiaoxi Ouyang, Yalei Zhao, Menghao Zhou, Baohong Wang, Qirui Li, Linxiao Fan, Sainan Zhang, Lanjuan Li   +9 more
doaj   +1 more source

Comprehensive analysis of the ubiquitinome during oncogene-induced senescence in human fibroblasts [PDF]

Cell Cycle, 2015
Oncogene-induced senescence (OIS) is an important tumor suppression mechanism preventing uncontrolled proliferation in response to aberrant oncogenic signaling. The profound functional and morphological remodelling of the senescent cell involves extensive changes.
Fee Bengsch, Zhigang Tu, Hsin-Yao Tang, Hengrui Zhu, David W Speicher, Rugang Zhang   +5 more
openaire   +2 more sources

Global Analysis of Host and Bacterial Ubiquitinome in Response to Salmonella Typhimurium Infection [PDF]

Molecular Cell, 2016
Ubiquitination serves as a critical signal in the host immune response to infection. Many pathogens have evolved strategies to exploit the ubiquitin (Ub) system to promote their own survival through a complex interplay between host defense machinery and bacterial virulence factors.
Evgenij Fiskin, Tihana Bionda, Ivan Dikic, Christian Behrends   +3 more
openaire   +2 more sources

How ubiquitination regulates the TGF-β signalling pathway: New insights and new players [PDF]

, 2011
Ubiquitination of protein species in regulating signal transduction pathways is universally accepted as of fundamental importance for normal development, and defects in this process have been implicated in the progression of many human diseases.
Bai, Bengoechea-Alonso, Bernassola, Chen, Chen, Chen, Chiu, Ciechanover, Ciehanover, Coccetti, Cook, Cook, Corcoran, Dunn, Ebisawa, Fang, Finley, Flasza, Foot, Foster, Fukuchi, Fukuchi, Fuxe, Gao, Gao, Gazdoiu, Grenfell, Groettrup, Guedat, Haldeman, Handley-Gearhart, Hayashi, He, Hjerpe, Ho, Huang, Huang, Huang, Inoue, Jin, Kang, Kasanov, Kavsak, Kerscher, Koinuma, Komuro, Kuratomi, Li, Liao, Lin, Liu, Liu, Lu, Maddika, Miyazawa, Moren, Mukhopadhyay, Mund, Murata, Nakamura, Nakao, Ogunjimi, Orban, Pelzer, Petroski, Pickart, Pirozzi, Putters, Raikwar, Sadowski, Schmierer, Seo, Shook, Soond, Soond, Stephen, Summers, Sun, Sun, Suzuki, Tajima, Tatematsu, Thrower, Walden, Wan, Wan, Wan, Wendt, Wiesner, Xie, Xu, Xu, Zhang, Zhang, Zhu, Zou   +95 more
core   +1 more source

Identification of substrates for human deubiquitinating enzymes (DUBs): An up-to-date review and a case study for neurodevelopmental disorders [PDF]

, 2022
Similar to the reversal of kinase-mediated protein phosphorylation by phosphatases, deubiquitinating enzymes (DUBs) oppose the action of E3 ubiquitin ligases and reverse the ubiquitination of proteins.
Elu Arantzamendi, Nagore, Mayor Martínez, Ugo, Osinalde Moraleja, Nerea, Presa Torre, Natalia, Prieto Agujeta, Gorka, Ramírez Sánchez, Juan Manuel, Rodríguez Pérez, José Antonio   +6 more
core   +1 more source

Proteomic analysis of ubiquitination substrates reveals a CTLH E3 ligase complex‐dependent regulation of glycolysis

The FASEB Journal, Volume 35, Issue 9, September 2021., 2021
Abstract Ubiquitination is an essential post‐translational modification that regulates protein stability or function. Its substrate specificity is dictated by various E3 ligases. The human C‐terminal to LisH (CTLH) complex is a newly discovered multi‐subunit really interesting new gene (RING) E3 ligase with only a few known ubiquitination targets. Here,
Matthew E. R. Maitland, Miljan Kuljanin, Xu Wang, Gilles A. Lajoie, Caroline Schild‐Poulter   +4 more
wiley   +1 more source

Functional Diversity and Structural Disorder in the Human Ubiquitination Pathway [PDF]

, 2013
The ubiquitin-proteasome system plays a central role in cellular regulation and protein quality control (PQC). The system is built as a pyramid of increasing complexity, with two E1 (ubiquitin activating), few dozen E2 (ubiquitin conjugating) and several
A Arrigoni, A Hershko, A Mohan, AE Deffenbaugh, B Bothner, B Hao, B Hess, C Guda, C Haynes, CJ Cox, CM Pickart, D Ekman, D Szklarczyk, D Van Der Spoel, D Vuzman, DM Duda, DM Duda, DW Leung, ES Zimmerman, ET Powers, F Bernassola, F Tama, F. Gisou van der Goot, FU Hartl, G Bussi, G Moncalian, G Swaminathan, G Wu, H Daub, H Dinkel, H Dou, H Shimizu, H Zhu, HC van Leeuwen, HE Niessen, HJ Dyson, HM Berman, I Szymkiewicz, I von Ossowski, J Liu, J Ma, J Prilusky, JC Rosenbaum, JH Fong, JM Huibregtse, K Peng, K Suhre, L Aravind, L Yang, LM Iakoucheva, M Christen, M Cormont, M Fuxreiter, M Fuxreiter, M Guharoy, M Hochstrasser, M Kanehisa, M Kanehisa, M Kanehisa, M Vidal, M Zhao, MA McCoy, Mainak Guharoy, MD Petroski, MD Petroski, ME Sowa, N Foray, N Mathias, N Zheng, P Tompa, P Tompa, P Tompa, P Tompa, P Tompa, Pallab Bhowmick, PE Ryan, PE Wright, Peter Tompa, PW Hildebrand, R Kiss, RG Smock, Rita Pancsa, RJ Deshaies, S Fishbain, S Vucetic, S Wiesner, SC Kales, SJ Demarest, SJ van Wijk, T Hagai, T Inobe, T Mittag, T Ravid, U Emekli, VN Uversky, W Humphrey, W Li, WY Mark, X Zhong, Y Haupt, Y Sheng, Y Xie, Z Dosztanyi, Z Dosztanyi, Z Dosztanyi   +104 more
core   +3 more sources

ALS-linked loss of Cyclin-F function affects HSP90 [PDF]

, 2022
The founding member of the F-box protein family, Cyclin-F, serves as a substrate adaptor for the E3 ligase Skp1-Cul1-F-box (SCF)Cyclin-F which is responsible for ubiquitination of proteins involved in cell cycle progression, DNA damage and mitotic ...
Behrends, Christian, Gattringer, Vanessa, Siebert, Alexander, Weishaupt, Jochen H.   +3 more
core   +1 more source

The platelet proteasome and immunoproteasome are stable in buffy‐coat derived platelet concentrates for up to 7 days

Transfusion, Volume 61, Issue 9, Page 2746-2755, September 2021., 2021
Abstract Objectives Characterization of the proteasome and its stability in buffy‐coat derived platelet concentrates (PCs) during storage. Background The proteasome plays a key role in cell homeostasis by processing misfolded or abnormal proteins and regulating the levels and activities of a high number of proteins contributing to cell cycle, survival,
Lisa Colberg, Clemens Cammann, Jan Wesche, Eylin Topfstedt, Ulrike Seifert, Andreas Greinacher   +5 more
wiley   +1 more source