Results 21 to 30 of about 1,145 (168)
Genome sequence of Desulfurella amilsii strain TR1 and comparative genomics of Desulfurellaceae family [PDF]
, 2017 The acidotolerant sulfur reducer Desulfurella amilsii was isolated from sediments of Tinto river, an extremely acidic environment. Its ability to grow in a broad range of pH and to tolerate certain heavy metals offers potential for metal recovery ...
Ahemad +63 more
core +3 more sources
Parasites & Vectors, 2020 Background Modulation of the host immune response by nematode parasites has been widely reported. Rhodaneses (thiosulfate: cyanide sulfurtransferases) are present in a wide range of organisms, such as archaea, bacteria, fungi, plants and animals ...
Yujian Wang +7 more
doaj +1 more source
Mitochondrial Sulfide Detoxification Requires a Functional Isoform O-Acetylserine(thiol)lyase C in Arabidopsis thaliana [PDF]
, 2012 In non-cyanogenic species, the main source of cyanide derives from ethylene and camalexin biosyntheses. In mitochondria, cyanide is a potent inhibitor of the cytochrome c oxidase and is metabolised by the β-Cyanoalanine synthase CYS-C1, catalysing the ...
García Fernández, Irene +3 more
core +1 more source
Intracellular Localization of Arabidopsis Sulfurtransferases [PDF]
Plant Physiology, 2004 Abstract Sulfurtransferases (Str) comprise a group of enzymes widely distributed in archaea, eubacteria, and eukaryota which catalyze the transfer of a sulfur atom from suitable sulfur donors to nucleophilic sulfur acceptors. In all organisms analyzed to date, small gene families encoding Str proteins have been identified.
Bauer, Michael +4 more
openaire +2 more sources
Past, present and future of cyanide antagonism research: From the early remedies to the current therapies. [PDF]
, 2015 This paper reviews milestones in antidotal therapies for cyanide (CN) spanning early remedies, current antidotal systems and research towards next generation therapies. CN has been a part of plant defense mechanisms for millions of years.
Budai, Marianna +3 more
core +2 more sources
Recent Advances in Our Understanding of the Biosynthesis of Sulfur Modifications in tRNAs
Frontiers in Microbiology, 2018 Sulfur is an essential element in all living organisms. In tRNA molecules, there are many sulfur-containing nucleosides, introduced post-transcriptionally, that function to ensure proper codon recognition or stabilization of tRNA structure, thereby ...
Naoki Shigi
doaj +1 more source
Conformational studies on Arabidopsis sulfurtransferase AtStr1 with spectroscopic methods [PDF]
, 2007 Sulfurtransferases/rhodaneses (Str) are enzymes widely distributed in archaea, prokaryota and eukaryota, and catalyze the transfer of sulfur from a donor molecule to a thiophilic acceptor substrate.
Bartels, Andrea +3 more
core +2 more sources
Plant mercaptopyruvate sulfurtransferases [PDF]
European Journal of Biochemistry, 2000 Mercaptopyruvate sulfurtransferase (MST, EC 2.8.1.2) and thiosulfate sulfurtransferase (TST, rhodanese, EC 2.8.1.1) are evolutionarily related enzymes that catalyze the transfer of sulfur ions from mercaptopyruvate and thiosulfate, respectively, to cyanide ions.
T, Nakamura, Y, Yamaguchi, H, Sano
openaire +2 more sources
Unraveling the role of thiosulfate sulfurtransferase in metabolic diseases [PDF]
, 2020 Thiosulfate sulfurtransferase (TST, EC 2.8.1.1), also known as Rhodanese, is a mitochondrial enzyme which catalyzes the transfer of sulfur in several molecular pathways.
Aguilar Lozano, Sheila P +8 more
core +2 more sources
Molecules, 2015 Plants and animals have evolved various potential mechanisms to surmount the adverse effects of heavy metal toxicity. Plants possess low molecular weight compounds containing sulfhydryl groups (-SH) that actively react with toxic metals.
Parvin Most, Jutta Papenbrock
doaj +1 more source