ArticleThe Journal of biological chemistry2018
Thiosulfate sulfurtransferase-like domain-containing 1 protein interacts with thioredoxin.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
41 citing papers in PubMed, 66 citations in OpenAlex.
- Knockouts of Sulfur Metabolism Genes Induce Chronic Inflammation and Immune Dysregulation inAntioxidants (Basel, Switzerland) · 2026Article
- Proteomic Insights into Heroin Use: Links to Neurodegeneration.Molecular neurobiology · 2026Article
- Proteomic Changes in the Cytoplasmatic Fraction of Weaned Piglets' Liver and Kidney Under Antioxidant and Mycotoxin Diets.Antioxidants (Basel, Switzerland) · 2025Article
- Construction of molecular subtypes and prognostic model for breast cancer based on sulfur metabolism-related genes.Translational cancer research · 2025Article
- The Biological Consequences of the Knockout of Genes Involved in the Synthesis and Metabolism of HAntioxidants (Basel, Switzerland) · 2025Article
- Thiosulphate sulfurtransferase: Biological roles and therapeutic potential.Redox biology · 2025Review
- Dual Roles of Reducing Systems in Protein Persulfidation and Depersulfidation.Antioxidants (Basel, Switzerland) · 2025Review
- Structural and biochemical characterization of an encapsulin-associated rhodanese from Acinetobacter baumannii.Protein science : a publication of the Protein Society · 2024Article
- Structural and biochemical characterization of an encapsulin-associated rhodanese frombioRxiv : the preprint server for biology · 2024Article
- Structural and functional characterization of sulfurtransferase from Frondihabitans sp. PAMC28461.PloS one · 2024Article
- Thiosulfate sulfurtransferase deficiency promotes oxidative distress and aberrant NRF2 function in the brain.Redox biology · 2023Article
- Identification and characterization of a small molecule that activates thiosulfate sulfurtransferase and stimulates mitochondrial respiration.Protein science : a publication of the Protein Society · 2023Article
- Sensing and regulation of reactive sulfur species (RSS) in bacteria.Current opinion in chemical biology · 2023Review
- Emerging Chemical Biology of Protein Persulfidation.Antioxidants & redox signaling · 2023Review
- Interactions of reactive sulfur species with metalloproteins.Redox biology · 2023Review
- Rhodanese-Fold Containing Proteins in Humans: Not Just Key Players in Sulfur Trafficking.Antioxidants (Basel, Switzerland) · 2023Review
- A sulfide-sensor and a sulfane sulfur-sensor collectively regulate sulfur-oxidation for feather degradation by Bacillus licheniformis.Communications biology · 2023Article
- Glutathione-Related Enzymes and Proteins: A Review.Molecules (Basel, Switzerland) · 2023Review
- Low Expression of TSTD2 Serves as a Biomarker for Poor Prognosis in Kidney Renal Clear Cell Carcinoma.International journal of general medicine · 2023Article
- High-LevelOphthalmology science · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
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. Mammalian rhodanese and mercaptopyruvate sulfurtransferase are perhaps the best-studied members of this protein superfamily and are involved in hydrogen sulfide metabolism. The relatively unstudied human thiosulfate sulfurtransferase-like domain-containing 1 (TSTD1) protein, a single-domain cytoplasmic sulfurtransferase, was also postulated to play a role in the sulfide oxidation pathway using thiosulfate to form glutathione persulfide, for subsequent processing in the mitochondrial matrix. Prior kinetic analysis of TSTD1 was performed at pH 9.2, raising questions about relevance and the proposed model for TSTD1 function. In this study, we report a 1.04 Å resolution crystal structure of human TSTD1, which displays an exposed active site that is distinct from that of rhodanese and mercaptopyruvate sulfurtransferase. Kinetic studies with a combination of sulfur donors and acceptors reveal that TSTD1 exhibits a low
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.