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Crystal structure of the human thioredoxin reductase–thioredoxin complex

https://doi.org/10.1038/ncomms1382
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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Refined structure of glutathione reductase at 1.54 Å resolution
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[21] Thioredoxin and thioredoxin reductase
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Focus on mammalian thioredoxin reductases — Important selenoproteins with versatile functions
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Truncated mutants of human thioredoxin reductase 1 do not exhibit glutathione reductase activity
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The Structure of Human Thioredoxin Reductase 1 Provides Insights into C-terminal Rearrangements During Catalysis
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Catalytic Cycle of Human Glutathione Reductase Near 1 Å Resolution
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On the potential of thioredoxin reductase inhibitors for cancer therapy
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Oxidative inactivation of thioredoxin as a cellular growth factor and protection by a Cys73 → Ser mutation
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Preparation and assay of mammalian thioredoxin and thioredoxin reductase
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Site-Directed Mutagenesis of Lys36 in Human Thioredoxin: The Highly Conserved Residue Affects Reduction Rates and Growth Stimulation but Is Not Essential for the Redox Protein's Biochemical or Biological Properties
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Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathione
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Buried S-Nitrosocysteine Revealed in Crystal Structures of Human Thioredoxin,
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A Conservedcis-Proline Precludes Metal Binding by the Active Site Thiolates in Members of the Thioredoxin Family of Proteins
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Human Thioredoxin Homodimers: Regulation by pH, Role of Aspartate 60, and Crystal Structure of the Aspartate 60 → Asparagine Mutant,
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Mammalian thioredoxin reductase 1: roles in redox homoeostasis and characterization of cellular targets
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A hypothesis on the catalytic mechanism of the selenoenzyme thioredoxin reductase
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Thiol redox control via thioredoxin and glutaredoxin systems
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Crystal structures of oxidized and reduced mitochondrial thioredoxin reductase provide molecular details of the reaction mechanism
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Mammalian thioredoxin reductase: Oxidation of the C-terminal cysteine/selenocysteine active site forms a thioselenide, and replacement of selenium with sulfur markedly reduces catalytic activity
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Dissection of complex protein dynamics in human thioredoxin
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Thioredoxin is required for S-nitrosation of procaspase-3 and the inhibition of apoptosis in Jurkat cells
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Three-dimensional structure of a mammalian thioredoxin reductase: Implications for mechanism and evolution of a selenocysteine-dependent enzyme
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The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli
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Molecular Cloning and Characterization of a Mitochondrial Selenocysteine-containing Thioredoxin Reductase from Rat Liver
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The Selenium-independent Inherent Pro-oxidant NADPH Oxidase Activity of Mammalian Thioredoxin Reductase and Its Selenium-dependent Direct Peroxidase Activities
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Mapping the Catalytic Cycle of Schistosoma mansoni Thioredoxin Glutathione Reductase by X-ray Crystallography
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Characterization of Alternative Cytosolic Forms and Cellular Targets of Mouse Mitochondrial Thioredoxin Reductase
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Regulation of the Catalytic Activity and Structure of Human Thioredoxin 1 via Oxidation and S-Nitrosylation of Cysteine Residues
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Crystal Structure and Catalysis of the Selenoprotein Thioredoxin Reductase 1
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Thioredoxin and Related Molecules–From Biology to Health and Disease
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Selenium and the Selenoprotein Thioredoxin Reductase in the Prevention, Treatment and Diagnostics of Cancer
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Improved methods for building protein models in electron density maps and the location of errors in these models
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PHENIX : building new software for automated crystallographic structure determination
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XDS
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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
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Regulated Protein Denitrosylation by Cytosolic and Mitochondrial Thioredoxins
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Cell Death by SecTRAPs: Thioredoxin Reductase as a Prooxidant Killer of Cells

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Exploring the Anticancer Activity of Tamoxifen-Based Metal Complexes Targeting Mitochondria
inferred← citeshttps://doi.org/10.1021/acsinfecdis.0c00909openalex-snapshot
Probing the Surface of a Parasite Drug Target Thioredoxin Glutathione Reductase Using Small Molecule Fragments
inferred← citeshttps://doi.org/10.1021/acsnano.3c08485openalex-snapshot
Reversing Ferroptosis Resistance in Breast Cancer via Tailored Lipid and Iron Presentation
inferred← citeshttps://doi.org/10.1021/acsomega.4c01382openalex-snapshot
Simulating the Motion Underlying the Mechanism of Thioredoxin Reductase
inferred← citeshttps://doi.org/10.1021/bi3005076openalex-snapshot
Discovery and Biochemical Characterization of Plasmodium Thioredoxin Reductase Inhibitors from an Antimalarial Set
inferred← citeshttps://doi.org/10.1021/bi301051bopenalex-snapshot
Dissecting Molecular Interactions Involved in Recognition of Target Disulfides by the Barley Thioredoxin System
inferred← citeshttps://doi.org/10.1021/bi400651xopenalex-snapshot
Why Is Mammalian Thioredoxin Reductase 1 So Dependent upon the Use of Selenium?
inferred← citeshttps://doi.org/10.1021/bi400658gopenalex-snapshot
Selenium as an Electron Acceptor during the Catalytic Mechanism of Thioredoxin Reductase
inferred← citeshttps://doi.org/10.1021/bi400931kopenalex-snapshot
A Mechanistic Investigation of the C-Terminal Redox Motif of Thioredoxin Reductase from Plasmodium falciparum
inferred← citeshttps://doi.org/10.1021/bi5013639openalex-snapshot
Lactococcus lactis Thioredoxin Reductase Is Sensitive to Light Inactivation
inferred← citeshttps://doi.org/10.1021/jacs.1c03234openalex-snapshot
Selective, Modular Probes for Thioredoxins Enabled by Rational Tuning of a Unique Disulfide Structure Motif
inferred← citeshttps://doi.org/10.1021/jacs.5b00888openalex-snapshot
A Peptide-Coated Gold Nanocluster Exhibits Unique Behavior in Protein Activity Inhibition
inferred← citeshttps://doi.org/10.1021/jm201359dopenalex-snapshot
Studies toward Novel Peptidomimetic Inhibitors of Thioredoxin–Thioredoxin Reductase System
inferred← citeshttps://doi.org/10.1021/np300118copenalex-snapshot
Gambogic Acid Deactivates Cytosolic and Mitochondrial Thioredoxins by Covalent Binding to the Functional Domain
inferred← citeshttps://doi.org/10.1038/cddis.2014.574openalex-snapshot
The conserved Trp114 residue of thioredoxin reductase 1 has a redox sensor-like function triggering oligomerization and crosslinking upon oxidative stress related to cell death
inferred← citeshttps://doi.org/10.1038/s41388-021-01924-0openalex-snapshot
Thioredoxin reductase is a major regulator of metabolism in leukemia cells
inferred← citeshttps://doi.org/10.1038/s41586-023-06532-4openalex-snapshot
Structural basis for thioredoxin-mediated suppression of NLRP1 inflammasome
inferred← citeshttps://doi.org/10.1038/s41598-026-62673-2openalex-snapshot
Integrated experimental and computational characterization of bioactive metabolites from Streptomyces paradoxus GH53 with antimicrobial, antioxidant, and antitumor activities
inferred← citeshttps://doi.org/10.1038/srep18339openalex-snapshot
Principles of using Cold Atmospheric Plasma Stimulated Media for Cancer Treatment
inferred← citeshttps://doi.org/10.1038/srep46282openalex-snapshot
The structure of Lactococcus lactis thioredoxin reductase reveals molecular features of photo-oxidative damage
inferred← citeshttps://doi.org/10.1039/c4mt00044gopenalex-snapshot
Ruthenium polypyridyl complexes as inducer of ROS-mediated apoptosis in cancer cells by targeting thioredoxin reductase
inferred← citeshttps://doi.org/10.1039/c9mt00304eopenalex-snapshot
Conjugation of a gold( iii ) complex with vitamin B1 and chlorambucil derivatives: anticancer evaluation and mechanistic insights
inferred← citeshttps://doi.org/10.1039/d2nj06196aopenalex-snapshot
Mechanochemistry of dynamic chalcogen-containing polymers: a minireview
inferred← citeshttps://doi.org/10.1039/d3ob01522jopenalex-snapshot
Exploration of 3,4-unsubstituted coumarins as thioredoxin reductase 1 inhibitors for cancer therapy
inferred← citeshttps://doi.org/10.1055/a-2022-1398openalex-snapshot
Efficient and Scalable Syntheses of 1,2-Thiaselenane-4-amine and 1,2-Thiaselenane-5-amine
inferred← citeshttps://doi.org/10.1073/pnas.1323873111openalex-snapshot
Crystal structure of mammalian selenocysteine-dependent iodothyronine deiodinase suggests a peroxiredoxin-like catalytic mechanism
inferred← citeshttps://doi.org/10.1073/pnas.2417269122openalex-snapshot
Modulating the microbiome as an approach to anticancer drug development
inferred← citeshttps://doi.org/10.1080/13543776.2017.1272576openalex-snapshot
Thioredoxin reductase inhibitors: a patent review
inferred← citeshttps://doi.org/10.1080/17460441.2021.1854220openalex-snapshot
How can we improve the design of small molecules to target thioredoxin reductase for treating cancer?
inferred← citeshttps://doi.org/10.1089/ars.2012.4650openalex-snapshot
Thioredoxin System in Cell Death Progression
inferred← citeshttps://doi.org/10.1089/ars.2012.4909openalex-snapshot
Identification of Michael Acceptor-Centric Pharmacophores with Substituents That Yield Strong Thioredoxin Reductase Inhibitory Character Correlated to Antiproliferative Activity
inferred← citeshttps://doi.org/10.1089/ars.2012.5013openalex-snapshot
Selenocysteine in Thiol/Disulfide-Like Exchange Reactions
inferred← citeshttps://doi.org/10.1089/ars.2015.6378openalex-snapshot
TrxR1 as a Potent Regulator of the Nrf2-Keap1 Response System
inferred← citeshttps://doi.org/10.1089/ars.2016.6816openalex-snapshot
The Enzymatic and Structural Basis for Inhibition of Echinococcus granulosus Thioredoxin Glutathione Reductase by Gold(I)
inferred← citeshttps://doi.org/10.1101/2021.06.28.450088openalex-snapshot
A novel small molecule that induces cytotoxicity in lung cancer cells inhibits disulfide reductases GSR and TXNRD1
inferred← citeshttps://doi.org/10.1107/s2059798317002066openalex-snapshot
Is dimerization a common feature in thioredoxins? The case of thioredoxin fromLitopenaeus vannamei
inferred← citeshttps://doi.org/10.1111/febs.14357openalex-snapshot
Kinetic characterization of wild‐type and mutant human thioredoxin glutathione reductase defines its reaction and regulatory mechanisms
inferred← citeshttps://doi.org/10.1111/febs.17301openalex-snapshot
Thioredoxin reductase inhibition and glutathione depletion mediated by glaucocalyxin A promote intracellular disulfide stress in gastric cancer cells
inferred← citeshttps://doi.org/10.1155/2017/8475125openalex-snapshot
Cell Signaling with Extracellular Thioredoxin and Thioredoxin‐Like Proteins: Insight into Their Mechanisms of Action
inferred← citeshttps://doi.org/10.1155/2021/6621292openalex-snapshot
Molecular Basis for the Interactions of Human Thioredoxins with Their Respective Reductases
inferred← citeshttps://doi.org/10.1186/1752-153x-7-175openalex-snapshot
Characterization of PfTrxR inhibitors using antimalarial assays and in silicotechniques
inferred← citeshttps://doi.org/10.1186/s12935-024-03523-xopenalex-snapshot
Reactive oxygen species from non-thermal gas plasma (CAP): implication for targeting cancer stem cells
inferred← citeshttps://doi.org/10.1186/s13020-024-00982-2openalex-snapshot
Natural products for enhancing the sensitivity or decreasing the adverse effects of anticancer drugs through regulating the redox balance
inferred← citeshttps://doi.org/10.1201/b19087-12openalex-snapshot
Regulation of Cellular Signalling by Thioredoxin
inferred← citeshttps://doi.org/10.1371/journal.pgen.1007272openalex-snapshot
Long-lived rodents reveal signatures of positive selection in genes associated with lifespan
inferred← citeshttps://doi.org/10.1371/journal.pone.0291272openalex-snapshot
Breakdown of Arabidopsis thaliana thioredoxins and glutaredoxins based on electrostatic similarity–Leads to common and unique interaction partners and functions
inferred← citeshttps://doi.org/10.1371/journal.ppat.1014125openalex-snapshot
Structural basis for substrate recognition and inhibition of thioredoxin glutathione reductase from Schistosoma japonicum: Implications for antiparasitic development
inferred← citeshttps://doi.org/10.15252/embj.201695021openalex-snapshot
Complex structure of cytochrome c–cytochrome c oxidase reveals a novel protein–protein interaction mode
inferred← citeshttps://doi.org/10.18632/oncotarget.13304openalex-snapshot
Cold atmospheric plasma, a novel promising anti-cancer treatment modality
inferred← citeshttps://doi.org/10.2174/2212796816666220422135204openalex-snapshot
Biological Activity of Synthetic Organoselenium Compounds: What do we Know about the Mechanism?
inferred← citeshttps://doi.org/10.2210/pdb4pol/pdbopenalex-snapshot
BNP7787 Forms Novel Covalent Adducts on Human Thioredoxin and Modulates Thioredoxin Activity
inferred← citeshttps://doi.org/10.25148/etd.fidc001236openalex-snapshot
Characterization of Interaction Between Brevetoxin and Its Native Receptor and Identification of the Role of Brevetoxin in Karenia brevis
inferred← citeshttps://doi.org/10.26434/chemrxiv-2023-plbdropenalex-snapshot
Selective Arylation of Selenocysteine of Thioredoxin Reductase 1 by an Organogold Compound: Expanding the Tool-Box of Metal-Templated Reactions in Cancer Cells
inferred← citeshttps://doi.org/10.31390/gradschool_dissertations.398openalex-snapshot
Biogenesis and Redox Transition of Iron-sulfur Clusters in Proteins
inferred← citeshttps://doi.org/10.3389/fcimb.2025.1533154openalex-snapshot
ChPDIA3 targeted by miR-126-x and miR-21-y responds to Vibrio harveyi infection in Crassostrea hongkongensis
inferred← citeshttps://doi.org/10.3389/fimmu.2013.00514openalex-snapshot
Thioredoxin/Txnip: Redoxisome, as a Redox Switch for the Pathogenesis of Diseases
inferred← citeshttps://doi.org/10.3389/fmolb.2022.883297openalex-snapshot
The Role of the Thioredoxin Detoxification System in Cancer Progression and Resistance
inferred← citeshttps://doi.org/10.3389/fmolb.2024.1274850openalex-snapshot
The C-terminal selenenylsulfide of extracellular/non-reduced thioredoxin reductase endows this protein with selectivity to small-molecule electrophilic reagents under oxidative conditions
inferred← citeshttps://doi.org/10.3389/fmolb.2025.1713876openalex-snapshot
Isolation, characterization, and biological evaluation of endophytic fungi from Phragmites australis: experimental and computational insights
inferred← citeshttps://doi.org/10.3390/antiox13010015openalex-snapshot
Distinct or Overlapping Areas of Mitochondrial Thioredoxin 2 May Be Used for Its Covalent and Strong Non-Covalent Interactions with Protein Ligands
inferred← citeshttps://doi.org/10.3390/antiox7110166openalex-snapshot
Crystal Structure of the Apo-Form of NADPH-Dependent Thioredoxin Reductase from a Methane-Producing Archaeon
inferred← citeshttps://doi.org/10.3390/antiox9050383openalex-snapshot
Role of Selenoproteins in Redox Regulation of Signaling and the Antioxidant System: A Review
inferred← citeshttps://doi.org/10.3390/bios13080811openalex-snapshot
Fluorescent Probes for Mammalian Thioredoxin Reductase: Mechanistic Analysis, Construction Strategies, and Future Perspectives
inferred← citeshttps://doi.org/10.3390/ijms25147827openalex-snapshot
The Interplay between Endogenous and Foodborne Pro-Oxidants and Antioxidants in Shaping Redox Homeostasis
inferred← citeshttps://doi.org/10.3390/molecules22020259openalex-snapshot
The Architecture of Thiol Antioxidant Systems among Invertebrate Parasites
inferred← citeshttps://doi.org/10.3390/molecules28196842openalex-snapshot
Benzophenanthridine Alkaloid Chelerythrine Elicits Necroptosis of Gastric Cancer Cells via Selective Conjugation at the Redox Hyperreactive C-Terminal Sec498 Residue of Cytosolic Selenoprotein Thioredoxin Reductase
inferred← citeshttps://doi.org/10.3390/molecules29010120openalex-snapshot
Selenium—More than Just a Fortuitous Sulfur Substitute in Redox Biology
inferred← citeshttps://doi.org/10.3390/pharmaceutics13040461openalex-snapshot
Alteration of Anticancer and Protein-Binding Properties of Gold(I) Alkynyl by Phenolic Schiff Bases Moieties
inferred← citeshttps://doi.org/10.70675/e4be5f5ezcb5az4395zb8eez6574b4f56ebcopenalex-snapshot
Molecular and structural bases of selenoprotein N dysfunction in diverse forms of congenital muscular dystrophies
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