Results 1 to 10 of about 28,091 (92)

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   +11 more sources

Ubiquitin-protein ligases [PDF]

Journal of Cell Science, 2004
Post-translational covalent tagging of proteins with the 76-residue protein ubiquitin (Ub) serves many functions. Polyubiquitylated proteins are directed to the large multi-component, multi-catalytic protease the 26S proteasome.
P A, Robinson, H C, Ardley
openaire   +2 more sources

Ubiquitylation in immune disorders and cancer: from molecular mechanisms to therapeutic implications [PDF]

, 2012
Conjugation of ubiquitin to proteins (ubiquitylation) has emerged to be one of the most crucial post-translational modifications controlling virtually all cellular processes.
Fulda, Simone, Rajalingam, Krishnaraj, Dikic, Ivan   +2 more
core   +2 more sources

RBR E3 ubiquitin ligases: new structures, new insights, new questions [PDF]

, 2014
The RBR (RING-BetweenRING-RING) or TRIAD [two RING fingers and a DRIL (double RING finger linked)] E3 ubiquitin ligases comprise a group of 12 complex multidomain enzymes.
Shaw, Gary S., Spratt, Donald E., Walden, Helen   +2 more
core   +1 more source

The ubiquitin E3/E4 ligase, UBE4A, fine-tunes protein ubiquitylation and accumulation at sites of DNA damage facilitating double-strand break repair [PDF]

, 2018
Double-strand breaks (DSBs) are critical DNA lesions that robustly activate the elaborate DNA damage response (DDR) network. We identified a critical player in DDR fine-tuning - the E3/E4 ubiquitin ligase, UBE4A.
Baranes Bachar, Keren, Huertas Sánchez, Pablo, Levy Barda, Adva, Oehler, Judith, Soria Bretones, Isabel   +4 more
core   +1 more source

The role of Schizosaccharomyces pombe SUMO ligases in genome stability [PDF]

, 2007
SUMOylation is a post-translational modification that affects a large number of proteins, many of which are nuclear. While the role of SUMOylation is beginning to be elucidated, it is clear that understanding the mechanisms that regulate the process is ...
A. Skilton, al-Khodairy, Allshire, Allshire, Andrews, Apionishev, Branzei, Chakrabarti, Cheng, E.A. Outwin, Ekwall, F.-X. Ogi, F.Z. Watts, Grishchuk, Ho, Ho, Hoege, Hooker, J.C.-Y. Ho, Johnson, Kagey, Kahyo, L. Gardner, L.K. Boyd, M.A.M. Trickey, McDonald, Okubo, Pichler, Potts, Reindle, Sachdev, Schmidt, Sergeant, Shayeghi, Shin, Stelter, Strahl-Bolsinger, Tanaka, Taylor, Thon, Watts, Xhemalce, Xhemalce, Zhao, Zhao   +44 more
core   +2 more sources

Regulation of alphaherpesvirus infections by the ICP0 family of proteins [PDF]

, 2013
Immediate-early protein ICP0 of herpes simplex virus type 1 (HSV-1) is important for the regulation of lytic and latent viral infection. Like the related proteins expressed by other alphaherpesviruses, ICP0 has a zinc-stabilized RING finger domain that ...
Boutell, Chris, Everett, Roger
core   +1 more source

Synergistic recruitment of UbcH7~Ub and phosphorylated Ubl domain triggers parkin activation [PDF]

, 2018
The E3 ligase parkin ubiquitinates outer mitochondrial membrane proteins during oxidative stress and is linked to early-onset Parkinson’s disease. Parkin is autoinhibited but is activated by the kinase PINK1 that phosphorylates ubiquitin leading to ...
Aguirre, Jacob D., Barber, Kathryn R., Chaugule, Viduth K., Condos, Tara E.C., Dunkerley, Karen M., Freeman, E Aisha, Konermann, Lars, Shaw, Gary S., Walden, Helen, Xiao, Yiming   +9 more
core   +1 more source

Rapid degradation of mutant SLC25A46 by the ubiquitin-proteasome system results in MFN1/2-mediated hyperfusion of mitochondria. [PDF]

, 2017
SCL25A46 is a mitochondrial carrier protein that surprisingly localizes to the outer membrane and is distantly related to Ugo1. Here we show that a subset of SLC25A46 interacts with mitochondrial dynamics components and the MICOS complex.
Claypool, Steven M, Jen, Joanna C, Koehler, Carla M, Steffen, Janos, Vashisht, Ajay A, Wan, Jijun, Wohlschlegel, James A   +6 more
core   +1 more source

A Novel Peptide-Based SILAC Method to Identify the Posttranslational Modifications Provides Evidence for Unconventional Ubiquitination in the ER-Associated Degradation Pathway. [PDF]

, 2013
The endoplasmic reticulum-associated degradation (ERAD) pathway is responsible for disposing misfolded proteins from the endoplasmic reticulum by inducing their ubiquitination and degradation.
Anania, Veronica, Bustos, Daisy, COSCOY, Laurent, Kirkpatrick, Donald, Lill, Jennie   +4 more
core   +3 more sources