Results 11 to 20 of about 917,448 (310)

Bacterial Cysteine-Inducible Cysteine Resistance Systems [PDF]

open access: yesJournal of Bacteriology, 2016
ABSTRACT Cysteine donates sulfur to macromolecules and occurs naturally in many proteins. Because low concentrations of cysteine are cytotoxic, its intracellular concentration is stringently controlled. In bacteria, cysteine biosynthesis is regulated by feedback inhibition of the activities of serine acetyltransferase (SAT) and 3-
Kazuhiro, Takumi, Gen, Nonaka
openaire   +2 more sources

Up-Converting Nanocrystals Modified With Fluorescent Markers for the Detection of Amino Acids: Preparation, Characterization, and Sensing Performance

open access: yesFrontiers in Chemistry, 2022
The present work was devoted to developing rhodamine-like chemosensing systems for cysteine (Cys) optical recognition. Aiming at low background light and minimal photobleaching effect, up-converting nanocrystals were firstly synthesized and latterly ...
YuLang Fei, Kun Wu, Liang Liu, Liang Liu
doaj   +1 more source

In vitro and in vivo anthelmintic efficacy of plant cysteine proteinases against the rodent gastrointestinal nematode, Trichuris muris [PDF]

open access: yes, 2006
We examined the mechanism of action and compared the anthelmintic efficacy of cysteine proteinases from papaya, pineapple, fig, kiwi fruit and Egyptian milkweed in vitro using the rodent gastrointestinal nematode Heligmosomoides polygyrus.
Behnke, J.M.   +4 more
core   +3 more sources

Multiple Disulfide-Bonded States of Native Proteins: Estimate of Number Using Probabilities of Disulfide Bond Formation

open access: yesMolecules, 2020
The polypeptide backbone of proteins is held together by two main types of covalent bonds: the peptide bonds that link the amino acid residues and the disulfide bonds that link pairs of cysteine amino acids. Disulfide bonds form as a protein folds in the
Philip J. Hogg
doaj   +1 more source

The Potential of a Protein Model Synthesized Absent of Methionine

open access: yesMolecules, 2022
Methionine is an amino acid long thought to be essential, but only in the case of protein synthesis initiation. In more recent years, methionine has been found to play an important role in antioxidant defense, stability, and modulation of cell and ...
Ronald J. Savino   +2 more
doaj   +1 more source

Proteome-wide analysis of cysteine oxidation reveals metabolic sensitivity to redox stress [PDF]

open access: yes, 2018
Reactive oxygen species (ROS) are increasingly recognised as important signalling molecules through oxidation of protein cysteine residues. Comprehensive identification of redox-regulated proteins and pathways is crucial to understand ROS-mediated events.
Gottlieb, Eyal   +4 more
core   +2 more sources

Methods and procedures for the processing of feather from poultry slaughterhouses and the application of feather meal as antioxidant

open access: yesActa Universitatis Sapientiae: Alimentaria, 2018
The research subject is the elaboration of a method and procedure for processing feather from poultry slaughterhouses and using it as antioxidant as well as for satisfying the sulphurous amino acid needs of ruminants.
Csapó J., Albert Cs.
doaj   +1 more source

Evaluation of Rhenium and Technetium-99m Complexes Bearing Quinazoline Derivatives as Potential EGFR Agents

open access: yesMolecules, 2023
Τhe Epidermal Growth Factor Receptor tyrosine kinase inhibitor (EGFR-TKI) 6-amino-4-[(3-bromophenyl) amino]quinazoline was derivatized with 6-bromohexanoyl-chloride and coupled with the tridentate chelating agents N-(2-pyridylmethyl) aminoethyl acetic ...
Konstantina Makrypidi   +9 more
doaj   +1 more source

Thiol-reactive analogues of galanthamine, codeine and morphine as potential probes to interrogate allosteric binding within nAChRs [PDF]

open access: yes, 2016
Alkaloids including galanthamine (1) and codeine (2) are reported to be positive allosteric modulators of nicotinic acetylcholine receptors (nAChRs) but the binding sites responsible for this activity are not known with certainty.
Balle, Thomas   +3 more
core   +1 more source

The cysteine proteome

open access: yesFree 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

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