Results 51 to 60 of about 747,792 (297)
, 2015 of essential biomolecules, such as vitamins, cofactors, antioxidants and many defence compounds, that are formed in response to adverse environmental conditions in which the sulfur moiety is the functional group. Sulfate is transported inside the plant, reduced to sulfide and incorporated into O-acetylserine (OAS) to form cysteine.
García, Irene +2 more
openaire +2 more sources
Isolation and expression analysis of transcripts encoding metallothioneins in oil palm
Biologia Plantarum, 2014 Two of the abundant transcripts encoding type 2 metallothionein (MT) proteins designated as MET2a and MET2b were selected in our previous study due to their high abundance (16.05 %) in the suppression subtractive hybridization library and their ...
A. B. Al-Shanfari, S. N. A. Abdullah
doaj +1 more source
Reconstruction of cysteine biosynthesis using engineered cysteine-free enzymes [PDF]
Scientific Reports, 2018 AbstractAmino acid biosynthesis pathways observed in nature typically require enzymes that are made with the amino acids they produce. For example, Escherichia coli produces cysteine from serine via two enzymes that contain cysteine: serine acetyltransferase (CysE) and O-acetylserine sulfhydrylase (CysK/CysM).
Fujishima, Kosuke +6 more
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Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants
Science, 2019 Oxygen sensing across kingdoms The ability to sense and respond to changes in oxygen levels is critical for most forms of life. To date, mechanistic studies of this process in mammals have focused on the oxygen-sensitive stability of a transcription ...
N. Masson +9 more
semanticscholar +1 more source
Fragmentation of protonated ions of peptides containing cysteine, cysteine sulfinic acid, and cysteine sulfonic acid [PDF]
Journal of the American Society for Mass Spectrometry, 2004 The oxidation of the sulfhydryl group in cysteine to sulfenic acid, sulfinic acid, and sulfonic acid in proteins is important in a number of enzymatic processes. In this study we examined the fragmentation of four peptides containing cysteine, cysteine sulfinic acid (Cys-SO(2)H), and cysteine sulfonic acid (Cys-SO(3)H) in an ion-trap mass spectrometer.
Wang, Yinsheng +3 more
openaire +2 more sources
Hydrogen Sulfide Signaling in Plants: Emerging Roles of Protein Persulfidation
Frontiers in Plant Science, 2018 Hydrogen sulfide (H2S) has been largely referred as a toxic gas and environmental hazard, but recent years, it has emerged as an important gas-signaling molecule with effects on multiple physiological processes in both animal and plant systems.
Angeles Aroca +2 more
doaj +1 more source
Mapping the evolution of mitochondrial complex I through structural variation
FEBS Letters, EarlyView.Respiratory complex I (CI) is crucial for bioenergetic metabolism in many prokaryotes and eukaryotes. It is composed of a conserved set of core subunits and additional accessory subunits that vary depending on the organism. Here, we categorize CI subunits from available structures to map the evolution of CI across eukaryotes. Respiratory complex I (CI)
Dong‐Woo Shin +2 more
wiley +1 more source
Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?
FEBS Letters, EarlyView.This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes +3 more
wiley +1 more source
Free Radical Biology and Medicine, 2015 The cysteine (Cys) proteome is a major component of the adaptive interface between the genome and the exposome. The thiol moiety of Cys undergoes a range of biologic modifications enabling biological switching of structure and reactivity. These biological modifications include sulfenylation and disulfide formation, formation of higher oxidation states,
Go, Young-Mi +2 more
openaire +2 more sources
Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation
FEBS Letters, EarlyView.Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe +3 more
wiley +1 more source