Results 81 to 90 of about 223,299 (305)

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

Overexpression of a soybean ariadne-like ubiquitin ligase gene GmARI1 enhances aluminum tolerance in Arabidopsis. [PDF]

open access: yesPLoS ONE, 2014
Ariadne (ARI) subfamily of RBR (Ring Between Ring fingers) proteins have been found as a group of putative E3 ubiquitin ligases containing RING (Really Interesting New Gene) finger domains in fruitfly, mouse, human and Arabidopsis.
Xiaolian Zhang   +8 more
doaj   +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

In vitro Protein Ubiquitination Assays

open access: yesBio-Protocol, 2013
Ubiquitin can be added to substrate protein as a protein tag by the concerted actions of ubiquitin activating enzyme (E1), ubiquitin conjugating enzyme (E2) and ubiquitin protein ligase (E3).
Qingzhen Zhao, Qi Xie
doaj   +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

TRIM5α as an E3 ubiquitin ligase

open access: yesThe FASEB Journal, 2009
Human immunodeficiency virus type1 (HIV‐1) efficiently infects susceptible cells and causes acquired immunodeficiency syndrome (AIDS) in humans. Although HIV can also enter the cells of Old World monkeys, it encounters a block before reverse transcription.
Makoto Tanaka   +2 more
openaire   +1 more source

E3 ubiquitin ligases in B-cell malignancies [PDF]

open access: yesCellular Immunology, 2019
Ubiquitylation is a post-translational modification (PTM) that controls various cellular signaling pathways. It is orchestrated by a three-step enzymatic cascade know as the ubiquitin proteasome system (UPS). E3 ligases dictate the specificity to the substrates, primarily leading to proteasome-dependent degradation.
Jaewoo Choi, Luca Busino
openaire   +2 more sources

Characterisation of the Cullin-3 mutation that causes a severe form of familial hypertension and hyperkalaemia [PDF]

open access: yes, 2015
Deletion of exon 9 from Cullin-3 (CUL3, residues 403-459: CUL3Δ403-459) causes pseudohypoaldosteronism type IIE (PHA2E), a severe form of familial hyperkalaemia and hypertension (FHHt).
Nichola L Figg   +35 more
core   +1 more source

Data for positive selection test and co-evolutionary analysis on mammalian cereblon

open access: yesData in Brief, 2019
Cereblon (CRBN) is a substrate recognition subunit of the CRL4 E3 ubiquitin ligase complex, directly binding to specific substrates for poly-ubiquitination followed by proteasome-dependent degradation of proteins.
Wataru Onodera   +2 more
doaj   +1 more source

The VHL tumor suppressor at the crossroad of protein folding, aggregation, and cancer

open access: yesMolecular Oncology, EarlyView.
Mutations, environmental stress, and chaperone dysfunction can destabilize pVHL, promoting its conversion from the native folded state into amyloid‐like assemblies. This transition may contribute to protein storage, cell dormancy, survival, and drug resistance.
Lara Abad   +2 more
wiley   +1 more source

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