Results 281 to 290 of about 1,958,325 (325)

Chemical approaches to explore ubiquitin-like proteins. [PDF]

RSC Chem Biol
Mousa R, Shkolnik D, Alalouf Y, Brik A.
europepmc   +1 more source

The role of USP36 in ribosome biogenesis and other pathophysiological processes. [PDF]

Front Mol Biosci
Shao L, Guo M, Kou Q, Guo Y, Li X, Li F.
europepmc   +1 more source

Ubiquitin-like SUMO protease expansion in rice (Oryza sativa)

Sue-ob K, Zhang C, Sharma E, Bhosale R, Sadanandom A, Jones AR.   +5 more
europepmc   +1 more source

Expression of SUMO enzymes is fiber type dependent in skeletal muscles and is dysregulated in muscle disuse [PDF]

The FASEB Journal, 2019
SUMOylation is a dynamic, reversible, enzymatic drug‐targetable post‐translational modification (PTM) reaction where the Small Ubiquitin‐like Modifier (SUMO) moieties are attached to proteins.
Arvind Venkat Namuduri, G. Heras, Volker M. Lauschke, M. Vitadello, Leonardo Traini, N. Cacciani, L. Gorza, Stefano Gastaldello   +7 more
semanticscholar   +4 more sources

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SUMO Chain Formation by Plant Enzymes.

Methods in molecular biology, 2016
SUMO conjugation is a conserved process of eukaryotes, and essential in metazoa. Different isoforms of SUMO are present in eukaryotic genomes. Saccharomyces cerevisiae has only one SUMO protein, humans have four and Arabidopsis thaliana has eight, the main isoforms being SUMO1 and SUMO2 with about 95 % identity.
Konstantin Tomanov, Ionida Ziba, A. Bachmair   +2 more
semanticscholar   +4 more sources

Biochemical characterization of SUMO-conjugating enzymes by in vitro sumoylation assays.

Methods in Enzymology, 2019
The small ubiquitin-related modifier (SUMO) is a protein of ~10kDa that is covalently conjugated to its substrate proteins in an enzymatic process called sumoylation. This posttranslational modification is an essential regulatory mechanism that plays crucial roles in many cellular pathways.
N. Eisenhardt, D. Ilic, E. Nagamalleswari, A. Pichler   +3 more
semanticscholar   +5 more sources

Conformational and Interface Variability in Multivalent SIM-SUMO Interaction.

Journal of Physical Chemistry B, 2023
SUMO targeted ubiqutin ligases (STUbLs) like RNF4 or Arkadia/RNF111 recognize SUMO chains through multiple SUMO interacting motifs (SIMs). Typically, these are contained in disordered regions of these enzymes and also the individual SUMO domains of SUMO ...
Alex Kötter, H. Mootz, A. Heuer
semanticscholar   +1 more source

Aberrant SENP1-SUMO-Sirt3 Signaling Causes the Disturbances of Mitochondrial Deacetylation and Oxidative Phosphorylation in Prion-Infected Animal and Cell Models.

ACS Chemical Neuroscience, 2023
Post-translational modifications of proteins, such as acetylation and SUMOylation, play important roles in regulation of protein functions and pathophysiology of different diseases including neurodegenerative diseases.
Dong-Dong Chen, Qiang Shi, Xin Liu, Donglin Liang, Yuezhang Wu, Qin Fan, K. Xiao, Cao Chen, Xiao-Ping Dong   +8 more
semanticscholar   +1 more source