Results 81 to 90 of about 105,668 (286)

ADP‐ribosylation: An emerging regulator of the epigenome

open access: yesMolecular Oncology, EarlyView.
ADP‐ribosylation has emerged as a dynamic epigenetic signaling mechanism that modifies histones and chromatin‐associated proteins. Through coordinated PARylation and MARylation, it integrates with other histone modifications to regulate chromatin structure, transcription factor activity, and gene expression, influencing genome function and disease ...
Cristel V. Camacho   +2 more
wiley   +1 more source

Image_1_How to Inactivate Human Ubiquitin E3 Ligases by Mutation.jpg

open access: yes, 2020
E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to substrate proteins, a process that determines the fate of the modified protein.
Ugo Mayor (404331)   +3 more
core   +1 more source

Unraveling the epigenetic code in cancer cell–tumor microenvironment crosstalk

open access: yesMolecular Oncology, EarlyView.
Epigenetic regulation is a key driver of cancer development and progression. Diverse epigenetic alterations in cancer cells and components of the tumor microenvironment (TME) orchestrate their communication through multiple mechanisms. We discuss how the epigenetic code coordinates bidirectional cancer cell–TME crosstalk to promote cancer progression ...
Ji Hoon Park, Mi‐Young Kim
wiley   +1 more source

Role of E3 ligases on skeletal muscle plasticity.

open access: yes, 2012
Neste estudo analisamos o envolvimento de E3 ligases sob três aspectos da plasticidade muscular esquelética: a perda de massa decorrente do desuso, a manutenção de fibras tipo I e II e a regeneração do tecido muscular.
Igor Luchini Baptista   +1 more
core   +1 more source

Arginine methylation as a regulatory ratchet in cancer: From substrate selection to malignant‐state stabilization

open access: yesMolecular Oncology, EarlyView.
Arginine methylation can be viewed as a persistence‐prone post‐translational modification regulated by a network of PRMTs. Competitive and compensatory interactions among PRMTs can redistribute methylation across substrate pools shaped by sequence, structural, spatial, and environmental layers, reinforcing RNA‐processing, chromatin, and signaling ...
So Hyun Kwon, Ji Min Lee
wiley   +1 more source

Table_1_How to Inactivate Human Ubiquitin E3 Ligases by Mutation.DOCX

open access: yes, 2020
E3 ubiquitin ligases are the ultimate enzymes involved in the transfer of ubiquitin to substrate proteins, a process that determines the fate of the modified protein.
Ugo Mayor (404331)   +3 more
core   +1 more source

Plant E3 Ligases and Their Role in Abiotic Stress Response

open access: yes, 2022
Plants, as sessile organisms, have limited means to cope with environmental changes. Consequently, they have developed complex regulatory systems to ameliorate abiotic stresses im-posed by environmental changes.
Raed Al-Saharin   +2 more
core   +1 more source

Mechanisms and therapeutic opportunities of the ribotoxic stress response in cancer

open access: yesMolecular Oncology, EarlyView.
Cancer cells' high translational demand creates opportunities to therapeutically target ribosome function. Ribosome stalling and collisions activate ZAKα and the ribotoxic stress response (RSR), which can trigger rapid, p53‐independent apoptosis in cancer.
Anastassiya Kim   +7 more
wiley   +1 more source

IDENTIFICATION AND FUNCTIONAL CHARACTERIZATION OF TWO NOVEL RING-TYPE E3 LIGASES FROM SESUVIUM VERRUCOSUM [PDF]

open access: yes, 2023
Drought and salinity pose significant environmental challenges that impact the growth and productivity of plants. Sesuvium verrucosum is a succulent halophyte species of the Aizoaceae family.
Purayil, Fayas Thayale
core   +2 more sources

E3 Ubiquitin Ligases and Their Therapeutic Applications in Cancers: Narrative Review

open access: yesJournal of Pharmacy and Bioallied Sciences
E3 ubiquitin ligases are a class of enzymes, essential for maintaining the equilibrium of cells by binding ubiquitin molecules to substrates to mark them for destruction.
Azfar Jamal
doaj   +1 more source

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