Results 51 to 60 of about 53,578 (248)

NF-κB repression by PIAS3 mediated RelA SUMOylation. [PDF]

open access: yesPLoS ONE, 2012
Negative regulation of the NF-κB transcription factor is essential for tissue homeostasis in response to stress and inflammation. NF-κB activity is regulated by a variety of biochemical mechanisms including phosphorylation, acetylation, and ...
Yuangang Liu   +3 more
doaj   +1 more source

Is PCNA unloading the central function of the Elg1/ATAD5 replication factor C-like complex? [PDF]

open access: yes, 2013
This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.Peer ...
Donaldson, Anne D   +2 more
core   +1 more source

SUMOylation regulates AKT1 activity [PDF]

open access: yesOncogene, 2014
Serine threonine kinase AKT has a central role in the cell, controlling survival, proliferation, metabolism and angiogenesis. Deregulation of its activity underlies a wide range of pathological situations, including cancer. Here we show that AKT is post-translationally modified by the small ubiquitin-like modifier (SUMO) protein. Interestingly, neither
Cruz-Herrera, C.F.   +8 more
openaire   +3 more sources

Importin-beta and CRM1 control a RANBP2 spatiotemporal switch essential for mitotic kinetochore function [PDF]

open access: yes, 2017
Protein conjugation with small ubiquitin-related modifier (SUMO) is a post-translational modification that modulates protein interactions and localisation.
Damizia, Michela   +7 more
core   +1 more source

SUMOylation of claudin‐2 [PDF]

open access: yesAnnals of the New York Academy of Sciences, 2012
The C‐terminal cytoplasmic tails of claudins are likely sites for interaction with proteins that regulate their function. We performed a yeast two‐hybrid screen with the tail of human claudin‐2 against a human kidney cDNA library and identified interactions with the PDZ3 domain of ZO‐2 as well as ubiquitin‐conjugating enzyme E2I (SUMO ligase‐1) and E3 ...
Christina M, Van Itallie   +2 more
openaire   +2 more sources

Proteasomal degradation of intracellularly expressed Amblyomin‐X limits suicide gene therapy potential in melanoma cells

open access: yesFEBS Open Bio, EarlyView.
This study explores the feasibility of expressing the antitumoral protein Amblyomin‐X through a suicide gene therapy approach and investigates its intracellular fate after gene delivery. Although the gene is efficiently expressed, melanoma cells rapidly degrade the Amblyomin‐X protein via proteasome activity.
Victor Dal Posolo Cinel   +4 more
wiley   +1 more source

Forkhead box protein A2 (FOXA2) protein stability and activity are regulated by sumoylation. [PDF]

open access: yesPLoS ONE, 2012
The forkhead box protein A2 (FOXA2) is an important regulator of glucose and lipid metabolism and organismal energy balance. Little is known about how FOXA2 protein expression and activity are regulated by post-translational modifications.
Narasimhaswamy S Belaguli   +3 more
doaj   +1 more source

Androgen receptor acetylation governs trans activation and MEKK1-induced apoptosis without affecting in vitro sumoylation and trans-repression function [PDF]

open access: yes, 2002
This work was supported by grants from the NIH (R01CA86072 to R.G.P. and R01CA72038-01 to S.A.W.F.) and The Susan Komen Breast Cancer Foundation (to R.G.P.). R.T.H. and E.J. were supported by the Medical Research Council. Y.-G.Y.
Chang, Chawnshang   +13 more
core   +1 more source

Mutant NPM1 in Acute Myeloid Leukemia Initiation and Maintenance

open access: yesAging and Cancer, EarlyView.
NPM1 mutations drive acute myeloid leukemia by acting as neomorphic transcriptional regulators that cooperate with Menin–MLL and XPO1 to sustain HOX/MEIS1 expression and block differentiation. Targeting these mutant‐specific transcriptional dependencies provides a rational therapeutic strategy for NPM1‐mutated AML.
Yanan Jiang   +3 more
wiley   +1 more source

Sumoylation in Physiology, Pathology and Therapy

open access: yesCells, 2022
Sumoylation is an essential post-translational modification that has evolved to regulate intricate networks within emerging complexities of eukaryotic cells.
Umut Sahin   +2 more
doaj   +1 more source

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