Results 61 to 70 of about 13,776 (215)

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

open access: yesBiomolecules, 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   +4 more
doaj   +1 more source

Alternative splicing of the SUMO1/2/3 transcripts affects cellular SUMOylation and produces functionally distinct SUMO protein isoforms

open access: yesScientific Reports, 2023
Substantial increases in the conjugation of the main human SUMO paralogs, SUMO1, SUMO2, and SUMO3, are observed upon exposure to different cellular stressors, and such increases are considered important to facilitate cell survival to stress.
Myriah L. Acuña   +11 more
doaj   +1 more source

Crosstalk Between SUMO and Ubiquitin-Like Proteins: Implication for Antiviral Defense

open access: yesFrontiers in Cell and Developmental Biology, 2021
Interferon (IFN) is a crucial first line of defense against viral infection. This cytokine induces the expression of several IFN-Stimulated Genes (ISGs), some of which act as restriction factors.
Mounira K. Chelbi-Alix   +2 more
doaj   +1 more source

SUMO modulation of protein aggregation and degradation

open access: yesAIMS Molecular Science, 2015
Small ubiquitin-like modifier (SUMO) conjugation and binding to target proteins regulate a wide variety of cellular pathways. The functional aspects of SUMOylation include changes in protein-protein interactions, intracellular trafficking as well as protein aggregation and degradation.
Feligioni M   +5 more
openaire   +3 more sources

The E3 Ubiquitin Ligase ARIH1 Facilitates Colorectal Cancer Progression by Promoting Oxidative Phosphorylation via the Mitochondrial Translocation of K63‐Linked Ubiquitinated PHB1

open access: yesAdvanced Science, EarlyView.
The RBR E3 ubiquitin ligase ARIH1, which is upregulated in colorectal cancer cells, promotes cell growth and metastasis and correlates with an unfavorable CRC prognosis. Mechanistically, ARIH1 catalyzes K63‐linked ubiquitination of PHB1, enhancing the interaction between PHB1 and Akt.
Ying Tong   +13 more
wiley   +1 more source

SuMo: A Mutation Testing Strategy for Solidity Smart Contracts [PDF]

open access: yesarXiv, 2021
Smart Contracts are software programs that are deployed and executed within a blockchain infrastructure. Due to their immutable nature, directly resulting from the specific characteristics of the deploying infrastructure, smart contracts must be thoroughly tested before their release.
arxiv  

Kindlin Regulates Mechanosensitive Activation and Adhesion Assembly of Integrin beta6

open access: yesAdvanced Science, EarlyView.
Extracellular matrix compliance plays a critical role in the regulation of integrin‐mediated adhesion and cell motility. Here, it is reported that strengthening the kindlin2‐integrin β6 interaction overcomes the dependence on extracellular substrate stiffness and promotes integrin β6‐mediated cell migration.
Wan Ning Lee   +3 more
wiley   +1 more source

SUMO chain formation is required for response to replication arrest in S. pombe.

open access: yesPLoS ONE, 2009
SUMO is a ubiquitin-like protein that is post-translationally attached to one or more lysine residues on target proteins. Despite having only 18% sequence identity with ubiquitin, SUMO contains the conserved betabetaalphabetabetaalphabeta fold present in
Andrew Skilton   +4 more
doaj   +1 more source

SUMO Chains Rule on Chromatin Occupancy

open access: yesFrontiers in Cell and Developmental Biology, 2020
The dynamic and reversible post-translational modification of proteins and protein complexes with the ubiquitin-related SUMO modifier regulates a wide variety of nuclear functions, such as transcription, replication and DNA repair.
Jan Keiten-Schmitz   +2 more
doaj   +1 more source

The MdHB7L–MdICE1L–MdHOS1 Module Fine‐Tunes Apple Cold Response via CBF‐Dependent and CBF‐Independent Pathways

open access: yesAdvanced Science, EarlyView.
In early cold response, MdICE1L utilizes MdHB7L as a cofactor to facilitate the transcriptional activation of MdCBFs, thereby activating cold signaling rapidly and strongly. Subsequently, MdICE1L is degraded by MdHOS1. Meanwhile, MdHB7L is released and accumulates.
Jie Yang   +8 more
wiley   +1 more source

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