Results 31 to 40 of about 54,326 (298)

Non-covalent Interaction With SUMO Enhances the Activity of Human Cytomegalovirus Protein IE1

Frontiers in Cell and Developmental Biology, 2021
Viruses interact with the host cellular pathways to optimize cellular conditions for replication. The Human Cytomegalovirus (HCMV) Immediate-Early protein 1 (IE1) is the first viral protein to express during infection.
Vasvi Tripathi, Kiran Sankar Chatterjee, Ranabir Das   +2 more
doaj   +1 more source

SUMO targeting of a stress-tolerant Ulp1 SUMO protease. [PDF]

PLoS ONE, 2018
SUMO proteases of the SENP/Ulp family are master regulators of both sumoylation and desumoylation and regulate SUMO homeostasis in eukaryotic cells. SUMO conjugates rapidly increase in response to cellular stress, including nutrient starvation, hypoxia ...
Jennifer Peek, Catherine Harvey, Dreux Gray, Danny Rosenberg, Likhitha Kolla, Reuben Levy-Myers, Rui Yin, Jonathan L McMurry, Oliver Kerscher   +8 more
doaj   +1 more source

SUMO Modification of Hepatitis B Virus Core Mediates Nuclear Entry, Promyelocytic Leukemia Nuclear Body Association, and Efficient Formation of Covalently Closed Circular DNA

Microbiology Spectrum, 2023
Persistence of hepatitis B virus (HBV) infection is due to a nuclear covalently closed circular DNA (cccDNA), generated from the virion-borne relaxed circular DNA (rcDNA) genome in a process likely involving numerous cell factors from the host DNA damage
Samuel Hofmann, Verena Plank, Peter Groitl, Nathalie Skvorc, Katharina Hofmann, Julius Luther, Chunkyu Ko, Peter Zimmerman, Volker Bruss, Daniela Stadler, Arnaud Carpentier, Shahinda Rezk, Michael Nassal, Ulrike Protzer, Sabrina Schreiner   +14 more
doaj   +1 more source

How Does SUMO Participate in Spindle Organization?

Cells, 2019
The ubiquitin-like protein SUMO is a regulator involved in most cellular mechanisms. Recent studies have discovered new modes of function for this protein.
Ariane Abrieu, Dimitris Liakopoulos
doaj   +1 more source

SUMOylation Is Required for Glycine-Induced Increases in AMPA Receptor Surface Expression (ChemLTP) in Hippocampal Neurons [PDF]

, 2012
yesMultiple pathways participate in the AMPA receptor trafficking that underlies long-term potentiation (LTP) of synaptic transmission. Here we demonstrate that protein SUMOylation is required for insertion of the GluA1 AMPAR subunit following transient ...
Craig, T.J., Henley, J.M., Jaafari, N., Kantamneni, Sriharsha, Konopacki, F.A., Owen, T.F., Rubin, P., Wilkinson, K.A.   +7 more
core   +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   +3 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

SUMO Modification: Wrestling with Protein Conformation [PDF]

Current Biology, 2005
SUMO modification of human thymine-DNA glycosylase facilitates the processing of base excision repair substrates by an unusual mechanism: while leaving the catalytic center unaffected, it induces product release by eliciting a conformational change in the enzyme.
openaire   +3 more sources

SUMOylation in Giardia lamblia: A Conserved Post-Translational Modification in One of the Earliest Divergent Eukaryotes

Biomolecules, 2012
Post-translational modifications are able to regulate protein function and cellular processes in a rapid and reversible way. SUMOylation, the post-translational modification of proteins by the addition of SUMO, is a highly conserved process that seems to
Andrea S. Rópolo, María C. Touz, Nahuel Zamponi, María C. Merino, Cecilia V. Vranych   +4 more
doaj   +1 more source

Site-specific identification and quantitation of endogenous SUMO modifications under native conditions. [PDF]

, 2017
Small ubiquitin-like modifier (SUMO) modification regulates numerous cellular processes. Unlike ubiquitin, detection of endogenous SUMOylated proteins is limited by the lack of naturally occurring protease sites in the C-terminal tail of SUMO proteins ...
Ahmad, Alla S, Bennett, Eric J, Clauser, Karl R, Gu, Hongbo, Komives, Elizabeth A, Leonard, Marilyn, Lumpkin, Ryan J, Meyer, Jesse G, Zhu, Yiying   +8 more
core   +2 more sources