Results 1 to 10 of about 3,023 (198)

Thiosulfate sulfurtransferase prevents hyperglycemic damage to the zebrafish pronephros in an experimental model for diabetes. [PDF]

Sci Rep, 2022
Thiosulfate sulfurtransferase (TST, EC 2.8.1.1), also known as Rhodanese, was initially discovered as a cyanide detoxification enzyme. However, it was recently also found to be a genetic predictor of resistance to obesity-related type 2 diabetes ...
Al-Dahmani ZM, Li X, Wiggenhauser LM, Ott H, Kruithof PD, Lunev S, A Batista F, Luo Y, Dolga AM, Morton NM, Groves MR, Kroll J, van Goor H.   +12 more
europepmc   +10 more sources

Identification and characterization of a small molecule that activates thiosulfate sulfurtransferase and stimulates mitochondrial respiration. [PDF]

Protein Sci, 2023
The enzyme Thiosulfate sulfurtransferase (TST, EC 2.8.1.1), is a positive genetic predictor of diabetes type 2 and obesity. As increased TST activity protects against the development of diabetic symptoms in mice, an activating compound for TST may ...
Al-Dahmani ZM, Hadian M, Ruiz-Moreno AJ, Maria SA, Batista FA, Zhang R, Luo Y, Sadremomtaz A, van der Straat R, Spoor M, Dolga AM, Dekker FJ, S S AD, van Goor H, Groves MR.   +14 more
europepmc   +8 more sources

Thiosulfate sulfurtransferase deficiency promotes oxidative distress and aberrant NRF2 function in the brain. [PDF]

Redox Biol, 2023
Thiosulfate sulfurtransferase (TST, EC 2.8.1.1) was discovered as an enzyme that detoxifies cyanide by conversion to thiocyanate (rhodanide) using thiosulfate as substrate; this rhodanese activity was subsequently identified to be almost exclusively located in mitochondria.
Luo Y, Chatre L, Melhem S, Al-Dahmani ZM, Homer NZM, Miedema A, Deelman LE, Groves MR, Feelisch M, Morton NM, Dolga A, van Goor H.   +11 more
europepmc   +10 more sources

Genetic identification of thiosulfate sulfurtransferase as an adipocyte-expressed antidiabetic target in mice selected for leanness [PDF]

Nature Medicine, 2016
The discovery of genetic mechanisms for resistance to obesity and diabetes may illuminate new therapeutic strategies for the treatment of this global health challenge. We used the polygenic 'lean' mouse model, which has been selected for low adiposity over 60 generations, to identify mitochondrial thiosulfate sulfurtransferase (Tst; also known as ...
Nicholas M Morton, Roderick N Carter, Zoi Michailidou   +2 more
exaly   +10 more sources

Unraveling the role of thiosulfate sulfurtransferase in metabolic diseases [PDF]

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 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, Al-Dahmani, Zayana M, de Assis Batista, Fernando, Dolga, Amalia M, Groves, Matthew R, Joles, Jaap A, Kruithof, Paul D, Lunev, Sergey, van Goor, Harry   +8 more
core   +8 more sources

Thiosulfate-cyanide sulfurtransferase a mitochondrial essential enzyme: from cell metabolism to the biotechnological applications [PDF]

International Journal of Molecular Sciences, 2022
Thiosulfate: cyanide sulfurtransferase (TST), also named rhodanese, is an enzyme widely distributed in both prokaryotes and eukaryotes, where it plays a relevant role in mitochondrial function. TST enzyme is involved in several biochemical processes such
Arciero I., Buonvino S., Melino S.
core   +7 more sources

Discovery of a small molecule allosteric activator of human thiosulfate sulfurtransferase [PDF]

, 2023
Recent studies showed that thiosulfate sulfurtransferase (TST) is one of the few peripherally expressed genes that has been identified as a genetic risk factor for metabolic health, with clear evidence of a negative correlation with the development of ...
Al Dahmani-Al Zakwani, Zayana
core   +4 more sources

Thiosulfate sulfurtransferase-like domain-containing 1 protein interacts with thioredoxin. [PDF]

J Biol Chem, 2018
Rhodanese domains are structural modules present in the sulfurtransferase superfamily. These domains can exist as single units, in tandem repeats, or fused to domains with other activities. Despite their prevalence across species, the specific physiological roles of most sulfurtransferases are not known.
Libiad M, Motl N, Akey DL, Sakamoto N, Fearon ER, Smith JL, Banerjee R.   +6 more
europepmc   +7 more sources

Transcriptomics of the <i>Anthopleura</i> Sea Anemone Reveals Unique Adaptive Strategies to Shallow-Water Hydrothermal Vent. [PDF]

Ecol Evol
The nonsymbiotic sea anemone Anthopleura nigrescens thrives in the extreme shallow‐water hydrothermal vents off Kueishan Island, Taiwan, where they represent some of the world's most extreme environments. Transcriptomic analyses revealed that genes involved in H2S homeostasis, stress resistance, and DNA repair are enriched in vent populations ...
Lin MF, Liu LL, Chen CA.
europepmc   +3 more sources

Structural and biochemical characterization of an encapsulin-associated rhodanese from Acinetobacter baumannii. [PDF]

Protein Sci
Abstract Rhodanese‐like domains (RLDs) represent a widespread protein family canonically involved in sulfur transfer reactions between diverse donor and acceptor molecules. RLDs mediate these transsulfuration reactions via a transient persulfide intermediate, created by modifying a conserved cysteine residue in their active sites.
Benisch R, Giessen TW.
europepmc   +2 more sources