Results 71 to 80 of about 35,698 (247)

ZDHHC18‐Mediated Palmitoylation of ORF3a Promotes SARS‐CoV‐2 Pathogenesis by Antagonizing TRIM16‐Mediated Ubiquitination and Proteasomal Degradation

open access: yesAdvanced Science, EarlyView.
Palmitoylation by ZDHHC18 blocks ORF3a K27‐linked ubiquitination mediated by TRIM16, thereby preventing its proteasomal degradation and strengthening viral pathogenesis. Targeting palmitoylation through a pharmacological inhibitor (2‐BP), a competitive inhibitory peptide (OPIP), or adenovirus‐mediated knockdown of ZDHHC18 expression presents a ...
Sidi Yang   +17 more
wiley   +1 more source

Ubc9 fusion–directed SUMOylation (UFDS): a method to analyze function of protein SUMOylation

open access: yes, 2007
Although small ubiquitin-like modifier (SUMO) is conjugated to proteins involved in diverse cellular processes, the functional analysis of SUMOylated proteins is often hampered by low levels of specific SUMOylated proteins in the cell. Here we describe a
Gaestel, Matthias   +13 more
core   +1 more source

SUMOylation and Major Depressive Disorder

open access: yes, 2022
Since the discovery of the small ubiquitin-like modifier (SUMO) protein in 1995, SUMOylation has been considered a crucial post-translational modification in diverse cellular functions.
Ryoo, Zae Young   +11 more
core   +1 more source

Master Regulator SMC1A, Stabilized by N6‐Methyladenosine Reader IGF2BP1, Promotes HCC Progression Through Facilitating Enhancer–Promoter Interaction of Nestin

open access: yesAdvanced Science, EarlyView.
IGF2BP1‐mediated m6A stabilization sustains SMC1A expression, enabling cohesin‐associated chromatin regulation of Nestin in hepatocellular carcinoma. This work reveals an epitranscriptomic‐chromatin‐cytoskeletal regulatory axis linked to malignant phenotypes and identifies SMC1A as a biologically relevant vulnerability in HCC.
Zhenxiang Peng   +7 more
wiley   +1 more source

Kerriamycin B inhibits protein SUMOylation [PDF]

open access: yes, 2009
http://www.nature.com/ja/journal/v62/n4/abs/ja200910a.html | http://www.nature.com/ja/journal/v62/n4/abs/ja200910a.htmlProtein SUMOylation has recently been shown as one of the major post-translational modifications involved in a variety of signaling ...
吉田, 稔   +15 more
core   +1 more source

SUMOylation in Skeletal Development, Homeostasis, and Disease

open access: yes, 2022
The modification of proteins by small ubiquitin-related modifier (SUMO) molecules, SUMOylation, is a key post-translational modification involved in a variety of biological processes, such as chromosome organization, DNA replication and repair ...
Zhao, Yaguang   +11 more
core   +1 more source

The Function of SUMOylation and Its Role in the Development of Cancer Cells under Stress Conditions: A Systematic Review

open access: yesStem Cells International, 2020
Malignant tumors still pose serious threats to human health due to their high morbidity and mortality. Recurrence and metastasis are the most important factors affecting patient prognosis.
Qi Zhao   +5 more
doaj   +1 more source

SUMOylation in Drosophila Development [PDF]

open access: yesBiomolecules, 2012
Small ubiquitin-related modifier (SUMO), an ~90 amino acid ubiquitin-like protein, is highly conserved throughout the eukaryotic domain. Like ubiquitin, SUMO is covalently attached to lysine side chains in a large number of target proteins. In contrast to ubiquitin, SUMO does not have a direct role in targeting proteins for proteasomal degradation ...
Smith, Matthew   +2 more
openaire   +5 more sources

SIRT6‐Mediated Deacetylation of ATF3 Promotes Silica‐Induced Lung Fibrosis by Enhancing its Nuclear Import via Binding to Importin α

open access: yesAdvanced Science, EarlyView.
SIRT6‐mediated ATF3 acetylation drives MGARP transcription and mitochondrial dysfunction in macrophages, promoting macrophage senescence and pulmonary fibrosis. Mechanistically, HSP70/Importin α competitively binds to ATF3, modulating its nuclear translocation.
Demin Cheng   +18 more
wiley   +1 more source

Pregnane X Receptor SUMOylation and De-SUMOylation [PDF]

open access: yes, 2014
The pregnane x receptor (PXR, NR1I2) is a member of the nuclear receptor (NR) superfamily of ligand-activated transcription factors. PXR is activated by numerous lipophilic compounds, a variety of drugs and drug metabolites in clinical use.
Liu, Chang
core  

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