Results 1 to 10 of about 7,232 (217)

S-nitrosation impairs KLF4 activity and instigates endothelial dysfunction in pulmonary arterial hypertension [PDF]

open access: yesRedox Biology, 2019
Krüppel-like factor 4 (KLF4) is a transcription factor with conserved zinc finger domains. As an essential regulator of vascular homeostasis, KLF4 exerts a protective effect in endothelial cells (ECs), including regulating vasodilation, inflammation ...
Yuying Zhang, Nanping Wang, Lei Xiao
exaly   +4 more sources

ESNOQ, proteomic quantification of endogenous S-nitrosation. [PDF]

open access: yesPLoS ONE, 2010
S-nitrosation is a post-translational protein modification and is one of the most important mechanisms of NO signaling. Endogenous S-nitrosothiol (SNO) quantification is a challenge for detailed functional studies.
Xixi Zhou   +6 more
doaj   +3 more sources

Oxygen-linked S-nitrosation in fish myoglobins: a cysteine-specific tertiary allosteric effect. [PDF]

open access: yesPLoS ONE, 2014
The discovery that cysteine (Cys) S-nitrosation of trout myoglobin (Mb) increases heme O2 affinity has revealed a novel allosteric effect that may promote hypoxia-induced nitric oxide (NO) delivery in the trout heart and improve myocardial efficiency. To
Signe Helbo   +5 more
doaj   +3 more sources

S-nitros(yl)ation of CaMKIIα and its precision redox regulation by SNOTAC plays a critical role in learning and memory [PDF]

open access: yesRedox Biology
Ca2+/calmodulin-dependent protein kinase II α (CaMKIIα) and nitric oxide (NO) both play vital roles in learning and memory; however, the underlying mechanisms connecting them have remained elusive.
Boyu Chu   +13 more
doaj   +2 more sources

S-Nitrosoglutathione Reductase—The Master Regulator of Protein S-Nitrosation in Plant NO Signaling

open access: yesPlants, 2019
S-nitrosation has been recognized as an important mechanism of protein posttranslational regulations, based on the attachment of a nitroso group to cysteine thiols.
Jana Jahnová   +2 more
exaly   +3 more sources

S-Nitrosation of E3 Ubiquitin Ligase Complex Components Regulates Hormonal Signalings in Arabidopsis

open access: yesFrontiers in Plant Science, 2022
E3 ubiquitin ligases mediate the last step of the ubiquitination pathway in the ubiquitin-proteasome system (UPS). By targeting transcriptional regulators for their turnover, E3s play a crucial role in every aspect of plant biology.
Maria Cecilia Terrile   +15 more
doaj   +1 more source

Deciphering the Path of S-nitrosation of Human Thioredoxin: Evidence of an Internal NO Transfer and Implication for the Cellular Responses to NO

open access: yesAntioxidants, 2022
Nitric oxide (NO) is a free radical with a signaling capacity. Its cellular functions are achieved mainly through S-nitrosation where thioredoxin (hTrx) is pivotal in the S-transnitrosation to specific cellular targets.
Vitor S. Almeida   +6 more
doaj   +1 more source

Nitric oxide destabilizes Pias3 and regulates sumoylation. [PDF]

open access: yesPLoS ONE, 2007
Small ubiquitin-related protein modifiers (SUMO) modification is an important mechanism for posttranslational regulation of protein function. However, it is largely unknown how the sumoylation pathway is regulated.
Jing Qu   +7 more
doaj   +1 more source

NO and Heme Proteins: Cross-Talk between Heme and Cysteine Residues

open access: yesAntioxidants, 2023
Heme proteins are a diverse group that includes several unrelated families. Their biological function is mainly associated with the reactivity of the heme group, which—among several other reactions—can bind to and react with nitric oxide (NO) and other ...
Cinzia Verde   +2 more
doaj   +1 more source

Keap1 controls protein S-nitrosation and apoptosis-senescence switch in endothelial cells

open access: yesRedox Biology, 2020
Premature senescence, a death escaping pathway for cells experiencing stress, is conducive to aging and cardiovascular diseases. The molecular switch between senescent and apoptotic fate remains, however, poorly recognized.
Aleksandra Kopacz   +11 more
doaj   +1 more source

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