Results 31 to 40 of about 38,177 (201)

C-iSUMO: A sumoylation site predictor that incorporates intrinsic characteristics of amino acid sequences

, 2020
Post-translational modifications are considered important molecular interactions in protein science. One of these modifications is “sumoylation” whose computational detection has recently become a challenge.
Reddy, Hamendra Manhar, Sharma, Alok, Dehzangi, Abdollah, Lopez, Yosvany   +3 more
core   +1 more source

SUMOylation and de-SUMOylation in response to DNA damage [PDF]

, 2011
To maintain genomic integrity, a cell must utilize multiple mechanisms to protect its DNA from the damage generated by environmental agents or DNA metabolism. SUMO (small ubiquitin-like modifier) can regulate protein stability, protein cellular location,
Yeh, Edward T.H., Hong Dou, Chao Huang, Lu, Long-Sheng, Long-Sheng Lu, Huang, Chao, Thang Van Nguyen, Van Nguyen, Thang, Edward T.H. Yeh, Dou, Hong   +9 more
core   +1 more source

mRNA expression analysis of the SUMO pathway genes in the adult mouse retina

Biology Open, 2015
Sumoylation is a reversible post-translational modification that regulates different cellular processes by conjugation/deconjugation of SUMO moieties to target proteins.
Víctor Abad-Morales, Elena B. Domènech, Alejandro Garanto, Gemma Marfany   +3 more
doaj   +1 more source

Sumoylation of transcription factor Tec1 regulates signaling of mitogen-activated protein kinase pathways in yeast. [PDF]

PLoS ONE, 2009
Tec1 is a transcription factor in the yeast mitogen-activated protein kinase (MAPK) pathway that controls invasive growth. Previously we reported that a fraction of Tec1 protein is sumoylated on residue lysine 54 in normally growing cells.
Yuqi Wang, Ameair Abu Irqeba, Mihretu Ayalew, Kristina Suntay   +3 more
doaj   +1 more source

An Atypical Mechanism of SUMOylation of Neurofibromin SecPH Domain Provides New Insights into SUMOylation Site Selection

International audienceNeurofibromin (Nf1) is a giant multidomain protein encoded by the tumour-suppressor gene NF1. NF1 is mutated in a common genetic disease, neurofibromatosis type I (NF1), and in various cancers.
Mosrin-Huaman, Christine, Goffinont, Stéphane, Vallée, Béatrice, Dundović, Iva, Normand, Thierry, Suskiewicz, Marcin, J, Sosic, Iva, Godin, Fabienne, Mosrin, Christine, Suskiewicz, Marcin, J., Serrano, Amandine, Bergoug, Mohammed, Bénédetti, Hélène, Doudeau, Michel   +13 more
core   +6 more sources

Host SUMOylation in bacterial infections and immune defense mechanisms

Frontiers in Microbiology
SUMOylation, the covalent attachment of small ubiquitin-like modifier proteins (SUMO) to lysine residues of target substrates, has emerged as a crucial post-translational modification regulating various cellular processes.
Yuhua Xu, Xi Ma, Zhifeng Wu, Ruitong Huang, Chenhua Liao, Di Huang, Yujun Tang, Chengbin Zhu, Yaqi Wang, Siyuan Zhang, Peng Liu, Jiaofeng Peng   +11 more
doaj   +1 more source

Extranuclear SUMOylation in Neurons [PDF]

, 2018
Post-translational modification of substrate proteins by SUMO conjugation regulates a diverse array of cellular processes. While predominantly a nuclear protein modification, there is a growing appreciation that SUMOylation of proteins outside the ...
Wilkinson, Kevin, Kevin A. Wilkinson, Jeremy M. Henley, Henley, Jeremy, Carmichael, Ruth, Ruth E. Carmichael   +5 more
core   +1 more source

Correlation between serum SUMO1 level and hypertriglyceridemia in type 2 diabetes mellitus patients

Shanghai Jiaotong Daxue xuebao. Yixue ban
Objective·To explore the correlation between serum small ubiquitin-like modifier 1 (SUMO1) levels and hypertriglyceridemia in patients with type 2 diabetes mellitus (T2DM).Methods·A total of 239 newly diagnosed T2DM patients were recruited from the ...
ZHANG Xinyan, LI Han, RAN Hui, SU Qing, ZHANG Hongmei   +4 more
doaj   +1 more source

Dynamic sumoylation of promoter-bound general transcription factors facilitates transcription by RNA polymerase II.

PLoS Genetics, 2021
Transcription-related proteins are frequently identified as targets of sumoylation, including multiple subunits of the RNA polymerase II (RNAPII) general transcription factors (GTFs).
Mohammad S Baig, Yimo Dou, Benjamin G Bergey, Russell Bahar, Justin M Burgener, Marjan Moallem, James B McNeil, Akhi Akhter, Giovanni L Burke, Veroni S Sri Theivakadadcham, Patricia Richard, Damien D'Amours, Emanuel Rosonina   +12 more
doaj   +1 more source

Threonine 348 regulates the subcellular localization of PTEN

FEBS Open Bio, EarlyView.
Thr348 in the C2 domain is a key contributor to PTEN subcellular localization. The PTEN350 fragment and PTENA4 accumulated in the nucleus, whereas PTENK13R,A4 predominantly localized to the plasma membrane. In contrast, substitution of Thr348 with Asp (T348D) disrupted these characteristic localization patterns, resulting in predominant cytoplasmic ...
Takashi Kato, Suzu Tanaka, Miyu Ohashi
wiley   +1 more source