Results 21 to 30 of about 12,608 (191)

Antibody RING-Mediated Destruction of Endogenous Proteins [PDF]

open access: yes, 2020
International ...
Abidi, Naima   +7 more
core   +4 more sources

Regulation of Wnt Singaling Pathway by Poly (ADP-Ribose) Glycohydrolase (PARG) Silencing Suppresses Lung Cancer in Mice Induced by Benzo(a)pyrene Inhalation Exposure

open access: yesFrontiers in Pharmacology, 2019
Benzo(a)pyrene (BaP) is a polycyclic aromatic hydrocarbon that specifically causes cancer and is widely distributed in the environment. Poly (ADP-ribosylation), as a key post-translational modification in BaP-induced carcinogenesis, is mainly catalyzed ...
Wenjuan Dai   +16 more
doaj   +1 more source

PARG suppresses tumorigenesis and downregulates genes controlling angiogenesis, inflammatory response, and immune cell recruitment

open access: yesBMC Cancer, 2022
Chemokines are highly expressed in tumor microenvironment and play a critical role in all aspects of tumorigenesis, including the recruitment of tumor-promoting immune cells, activation of cancer-associated fibroblasts, angiogenesis, metastasis, and ...
Sarah Johnson   +5 more
doaj   +1 more source

PARP and PARG inhibitors in cancer treatment [PDF]

open access: yesGenes & Development, 2020
Oxidative and replication stress underlie genomic instability of cancer cells. Amplifying genomic instability through radiotherapy and chemotherapy has been a powerful but nonselective means of killing cancer cells. Precision medicine has revolutionized cancer therapy by putting forth the concept of selective targeting of cancer cells. Poly(ADP-ribose)
openaire   +2 more sources

O-GlcNAc has crosstalk with ADP-ribosylation via PARG

open access: yesJournal of Biological Chemistry, 2023
O-linked N-acetylglucosamine (O-GlcNAc) glycosylation, a prevalent protein post-translational modification (PTM) that occurs intracellularly, has been shown to crosstalk with phosphorylation and ubiquitination. However, it is unclear whether it interplays with other PTMs. Here we studied its relationship with ADP-ribosylation, which involves decorating
Jie Li   +13 more
openaire   +2 more sources

Poly(ADP-Ribose) Glycohydrolase (PARG) Silencing Suppresses Benzo(a)pyrene Induced Cell Transformation.

open access: yesPLoS ONE, 2016
Benzo(a)pyrene (BaP) is a ubiquitously distributed environmental pollutant and known carcinogen, which can induce malignant transformation in rodent and human cells.
Xuan Li   +8 more
doaj   +1 more source

Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal

open access: yesNature Communications, 2021
PARG and ARH3 are the main hydrolases to reverse serine poly(ADP-ribosylation) yet their activities in the process differ. Here, the authors synthesise linear and branched poly(ADP-ribose) molecules, perform structure-function analysis and elucidate the ...
Johannes Gregor Matthias Rack   +13 more
doaj   +1 more source

Radiosensitization with an inhibitor of poly(ADP-ribose) glycohydrolase: A comparison with the PARP1/2/3 inhibitor olaparib [PDF]

open access: yes, 2018
Upon DNA binding the poly(ADP-ribose) polymerase family of enzymes (PARPs) add multiple ADP-ribose subunits to themselves and other acceptor proteins.
Albert   +94 more
core   +2 more sources

Radiation-induced mitotic catastrophe in PARG-deficient cells [PDF]

open access: yesJournal of Cell Science, 2009
Poly(ADP-ribosyl)ation is a post-translational modification of proteins involved in the regulation of chromatin structure, DNA metabolism, cell division and cell death. Through the hydrolysis of poly(ADP-ribose) (PAR), Poly(ADP-ribose) glycohydrolase (PARG) has a crucial role in the control of life-and-death balance following DNA insult.
Amé, Jean-Christophe   +7 more
openaire   +3 more sources

Helicoverpa armigera nucleopolyhedrovirus occlusion-derived virus-associated protein, HA100, affects oral infectivity in vivo but not virus replication in vitro [PDF]

open access: yes, 2011
ORF100 (ha100) of Helicoverpa armigera nucleopolyhedrovirus (HearNPV) has been reported as one of the unique genes of group II alphabaculoviruses encoding a protein located in the occlusion-derived virus (ODV) envelope and nucleocapsid.
Deng, F.   +7 more
core   +3 more sources

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