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Engineering a thermo-stable superoxide dismutase functional at sub-zero to >50°C, which also tolerates autoclaving

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What this work says

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

inferredcites →https://doi.org/10.1006/abbi.2000.1786openalex-snapshot
A Free Cysteine Residue at the Dimer Interface Decreases Conformational Stability of Xenopus laevis Copper,Zinc Superoxide Dismutase
inferredcites →https://doi.org/10.1006/abio.1976.9999openalex-snapshot
A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
inferredcites →https://doi.org/10.1007/978-90-481-9501-5_24openalex-snapshot
An Industrial Perspective
inferredcites →https://doi.org/10.1007/bf00020249openalex-snapshot
Subunit interaction enhances enzyme activity and stability of sweet potato cytosolic Cu/Zn-superoxide dismutase purified by a His-tagged recombinant protein method
inferredcites →https://doi.org/10.1007/bf00173326openalex-snapshot
Role of cysteine residues in esterase from Bacillus stearothermophilus and increasing its thermostability by the replacement of cysteines
inferredcites →https://doi.org/10.1007/bf01007608openalex-snapshot
A spectroscopic characterization of a monomeric analog of copper, zinc superoxide dismutase
inferredcites →https://doi.org/10.1007/pl00000935openalex-snapshot
How do thermophilic proteins deal with heat?
inferredcites →https://doi.org/10.1007/s10126-006-0143-yopenalex-snapshot
Replacement of Buried Cysteine from Zebrafish Cu/Zn Superoxide Dismutase and Enhancement of Its Stability via Site-Directed Mutagenesis
inferredcites →https://doi.org/10.1016/0003-2697(71)90370-8openalex-snapshot
Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
inferredcites →https://doi.org/10.1016/0014-5793(82)80939-3openalex-snapshot
Reversibility of the thermal denaturation of yeast superoxide dismutase
inferredcites →https://doi.org/10.1016/0022-2836(92)90734-2openalex-snapshot
Evolutionary conservativeness of electric field in the Cu,Zn superoxide dismutase active site
inferredcites →https://doi.org/10.1016/0076-6879(86)30013-2openalex-snapshot
[11] Calculation of protein conformation from circular dichroism
inferredcites →https://doi.org/10.1016/0076-6879(90)86093-bopenalex-snapshot
[1] Role of free radicals and catalytic metal ions in human disease: An overview
inferredcites →https://doi.org/10.1016/j.jmb.2003.09.069openalex-snapshot
Folding of Cu, Zn Superoxide Dismutase and Familial Amyotrophic Lateral Sclerosis
inferredcites →https://doi.org/10.1016/j.jmb.2004.08.085openalex-snapshot
Probing the High Energy States in Proteins by Proteolysis
inferredcites →https://doi.org/10.1016/j.jmb.2006.09.048openalex-snapshot
The Coupling between Disulphide Status, Metallation and Dimer Interface Strength in Cu/Zn Superoxide Dismutase
inferredcites →https://doi.org/10.1016/j.molcatb.2010.11.007openalex-snapshot
The basic and applied aspects of superoxide dismutase
inferredcites →https://doi.org/10.1016/s0021-9258(18)37859-1openalex-snapshot
Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds.
inferredcites →https://doi.org/10.1016/s0021-9258(18)66701-8openalex-snapshot
Crystallographic characterization of recombinant human CuZn superoxide dismutase.
inferredcites →https://doi.org/10.1016/s0021-9258(18)77291-8openalex-snapshot
Changes in crystallographic structure and thermostability of a Cu,Zn superoxide dismutase mutant resulting from the removal of a buried cysteine.
inferredcites →https://doi.org/10.1016/s0021-9258(18)83275-6openalex-snapshot
The structural stability of a protein is an important determinant of its proteolytic susceptibility in Escherichia coli
inferredcites →https://doi.org/10.1016/s0021-9258(19)44055-6openalex-snapshot
On the Stability of Bovine Superoxide Dismutase
inferredcites →https://doi.org/10.1021/bi00590a005openalex-snapshot
Subunit association and side-chain reactivities of bovine erythrocyte superoxide dismutase in denaturing solvents
inferredcites →https://doi.org/10.1021/bi0491898openalex-snapshot
Structural Basis of Protein Kinetic Stability: Resistance to Sodium Dodecyl Sulfate Suggests a Central Role for Rigidity and a Bias Toward β-Sheet Structure
inferredcites →https://doi.org/10.1021/bi9803473openalex-snapshot
Solution Structure of Reduced Monomeric Q133M2 Copper, Zinc Superoxide Dismutase (SOD). Why Is SOD a Dimeric Enzyme?,
inferredcites →https://doi.org/10.1021/jf0111559openalex-snapshot
Characterization of Copper/Zinc-Superoxide Dismutase fromPagrus majorcDNA and Enzyme Stability
inferredcites →https://doi.org/10.1021/jf0207070openalex-snapshot
Copper/Zinc-Superoxide Dismutase from Lemon cDNA and Enzyme Stability
inferredcites →https://doi.org/10.1021/jf981355topenalex-snapshot
Characterization of the Dimer−Monomer Equilibrium of the Papaya Copper/Zinc Superoxide Dismutase and Its Equilibrium Shift by a Single Amino Acid Mutation
inferredcites →https://doi.org/10.1038/227680a0openalex-snapshot
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
inferredcites →https://doi.org/10.1038/358347a0openalex-snapshot
Faster superoxide dismutase mutants designed by enhancing electrostatic guidance
inferredcites →https://doi.org/10.1042/bj2070641openalex-snapshot
A correlation between protein thermostability and resistance to proteolysis
inferredcites →https://doi.org/10.1042/bj3200713openalex-snapshot
The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins
inferredcites →https://doi.org/10.1042/bj3340219openalex-snapshot
Thermal inactivation and chaperonin-mediated renaturation of mitochondrial aspartate aminotransferase
inferredcites →https://doi.org/10.1073/pnas.0813167106openalex-snapshot
Detergent binding explains anomalous SDS-PAGE migration of membrane proteins
inferredcites →https://doi.org/10.1073/pnas.212527999openalex-snapshot
Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases
inferredcites →https://doi.org/10.1073/pnas.2436143100openalex-snapshot
The dual nature of human extracellular superoxide dismutase: One sequence and two structures
inferredcites →https://doi.org/10.1073/pnas.84.19.6663openalex-snapshot
Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding.
inferredcites →https://doi.org/10.1073/pnas.90.4.1629openalex-snapshot
Increased resistance to oxidative stress in transgenic plants that overexpress chloroplastic Cu/Zn superoxide dismutase.
inferredcites →https://doi.org/10.1073/pnas.93.23.12774openalex-snapshot
Novel dimeric interface and electrostatic recognition in bacterial Cu,Zn superoxide dismutase
inferredcites →https://doi.org/10.1073/pnas.95.21.12300openalex-snapshot
Protein thermostability above 100°C: A key role for ionic interactions
inferredcites →https://doi.org/10.1074/jbc.273.10.5655openalex-snapshot
Role of the Dimeric Structure in Cu,Zn Superoxide Dismutase
inferredcites →https://doi.org/10.1074/jbc.m007891200openalex-snapshot
Copper- and Zinc-containing Superoxide Dismutase Can Act as a Superoxide Reductase and a Superoxide Oxidase
inferredcites →https://doi.org/10.1093/bioinformatics/bth248openalex-snapshot
POLYVIEW: a flexible visualization tool for structural and functional annotations of proteins
inferredcites →https://doi.org/10.1093/nar/25.2.447openalex-snapshot
Alanine-stretch scanning mutagenesis: a simple and efficient method to probe protein structure and function
inferredcites →https://doi.org/10.1093/treephys/27.9.1253openalex-snapshot
Tea (Camellia sinensis) clones with shorter periods of winter dormancy exhibit lower accumulation of reactive oxygen species
inferredcites →https://doi.org/10.1107/s0907444908019069openalex-snapshot
Structure of a superoxide dismutase and implications for copper-ion chelation
inferredcites →https://doi.org/10.1111/j.1365-3040.1994.tb00146.xopenalex-snapshot
Protection against oxygen radicals: an important defence mechanism studied in transgenic plants
inferredcites →https://doi.org/10.1126/science.8351519openalex-snapshot
Amyotrophic Lateral Ssclerosis and Structural Defects in Cu,Zn Superoxide Dismutase
inferredcites →https://doi.org/10.1128/aem.71.10.5728-5734.2005openalex-snapshot
Directed Evolution of a Thermostable Phosphite Dehydrogenase for NAD(P)H Regeneration
inferredcites →https://doi.org/10.1146/annurev.arplant.53.100201.160729openalex-snapshot
A CCLIMATIVE R ESPONSE TO T EMPERATURE S TRESS IN H IGHER P LANTS : Approaches of Gene Engineering for Temperature Tolerance
inferredcites →https://doi.org/10.2210/pdb3sod/pdbopenalex-snapshot
CHANGES IN CRYSTALLOGRAPHIC STRUCTURE AND THERMOSTABILITY OF A CU,ZN SUPEROXIDE DISMUTASE MUTANT RESULTING FROM THE REMOVAL OF BURIED CYSTEINE
inferredcites →https://doi.org/10.3109/07388551.2010.490937openalex-snapshot
Superoxide dismutase: an industrial perspective

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

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A comparative study of fatty acid profile and formation of biofilm in Geobacillus gargensis exposed to variable abiotic stress
inferred← citeshttps://doi.org/10.1155/2013/782450openalex-snapshot
Superoxide-Dismutase Deficient Mutants in Common Beans (Phaseolus vulgarisL.): Genetic Control, Differential Expressions of Isozymes, and Sensitivity to Arsenic
inferred← citeshttps://doi.org/10.1186/s11671-026-04489-7openalex-snapshot
Biosynthesis of selenium nanoparticles by Aloe vera leaf extract and its biomedical applications
inferred← citeshttps://doi.org/10.1186/s12870-024-05292-1openalex-snapshot
Seed priming with potassium nitrate alleviates the high temperature stress by modulating growth and antioxidant potential in carrot seeds and seedlings
inferred← citeshttps://doi.org/10.1186/s12870-026-08899-8openalex-snapshot
Biofortifying sunflower with Zinc (Zn) aminochelates: a promising strategy for calcareous soil conditions
inferred← citeshttps://doi.org/10.1186/s40064-016-1854-9openalex-snapshot
Improving the thermostability and stress tolerance of an archaeon hyperthermophilic superoxide dismutase by fusion with a unique N-terminal domain
inferred← citeshttps://doi.org/10.1186/s43094-023-00527-8openalex-snapshot
Phytocompounds, antioxidant potential, and inhibitory actions of ethanolic leaf fraction of Sida linifolia Linn. (Malvaceae) on enzymes linked to inflammation, diabetes, and neurological disorders
inferred← citeshttps://doi.org/10.1371/journal.pone.0110302openalex-snapshot
Simultaneous Over-Expression of PaSOD and RaAPX in Transgenic Arabidopsis thaliana Confers Cold Stress Tolerance through Increase in Vascular Lignifications
inferred← citeshttps://doi.org/10.1371/journal.pone.0247864openalex-snapshot
Genome-wide identification and expression profiling of basic leucine zipper transcription factors following abiotic stresses in potato (Solanum tuberosum L.)
inferred← citeshttps://doi.org/10.1371/journal.pone.0260047openalex-snapshot
Construction and potential application of bacterial superoxide dismutase expressed in Bacillus subtilis against mycotoxins
inferred← citeshttps://doi.org/10.14719/pst.2020.7.3.797openalex-snapshot
COMPARISON BETWEEN TUBELESS AND TUBE PERCUTANEOUS NEPHROLITHOTOMIES IN PEDIATRIC POPULATION: A RANDOMIZED CONTROLLED TRIAL
inferred← citeshttps://doi.org/10.14720/aas.2019.114.2.6openalex-snapshot
Cadmium toxicity in African yam bean (Sphenostylis stenocarpa (HOCHST. EX A.RICH.) HARMS genotypes
inferred← citeshttps://doi.org/10.1515/jbcpp-2018-0070openalex-snapshot
Dynamics of inflammatory reaction and oxidative stress across maternal serum, placenta and amniotic fluid in laboratory rats and the role played by genistein aglycone
inferred← citeshttps://doi.org/10.21203/rs.3.rs-2771658/v1openalex-snapshot
Leaf litter contributes to the obstacles of Cynanchum auriculatum Royle ex Wight continuous cropping
inferred← citeshttps://doi.org/10.21448/ijsm.1799514openalex-snapshot
Enzymatic and non-enzymatic antioxidant activities of Lepiota procera and Lactarius deterrimus species from Anatolia
inferred← citeshttps://doi.org/10.2174/0929866530666230519122612openalex-snapshot
Protein Engineering, a Robust Tool to Engineer Novel Functions in Protein
inferred← citeshttps://doi.org/10.26656/fr.2017.6(6).642openalex-snapshot
Effect of pH and temperature on antioxidant enzymes activities in Morinda citrifolia L. (Mengkudu) leaves extract
inferred← citeshttps://doi.org/10.33472/afjbs.2.2.2020.25-39openalex-snapshot
Statistical augmentation of thermostable Superoxide dismutase (SOD) production from Bacillus licheniformis SPB-13 of Himalayan ranges
inferred← citeshttps://doi.org/10.3389/fbioe.2020.614498openalex-snapshot
A SH3_5 Cell Anchoring Domain for Non-recombinant Surface Display on Lactic Acid Bacteria
inferred← citeshttps://doi.org/10.3389/fnut.2022.850824openalex-snapshot
Production of a Novel Superoxide Dismutase by Escherichia coli and Pichia pastoris and Analysis of the Thermal Stability of the Enzyme
inferred← citeshttps://doi.org/10.3389/fpls.2022.864330openalex-snapshot
Molecular and Biochemical Analysis of Duplicated Cytosolic CuZn Superoxide Dismutases of Rice and in silico Analysis in Plants
inferred← citeshttps://doi.org/10.3389/fpls.2025.1541498openalex-snapshot
Antibacterial potential of silver–selenium nanocomposites in mitigating fire blight disease in Pyrus communis L
inferred← citeshttps://doi.org/10.3390/agriculture13081543openalex-snapshot
The Influence of Phytohormones on Antioxidative and Antibacterial Activities in Callus Cultures of Hypericum perforatum L.
inferred← citeshttps://doi.org/10.3390/cimb47050351openalex-snapshot
The Superoxide Dismutase Family in Balloon Flower (Platycodon grandiflorus): Phylogenetic Relationships, Structural Characteristics, and Expression Patterns
inferred← citeshttps://doi.org/10.3390/horticulturae10020170openalex-snapshot
Boosting Resilience and Efficiency of Tomato Fields to Heat Stress Tolerance Using Cytokinin (6-Benzylaminopurine)
inferred← citeshttps://doi.org/10.3390/horticulturae8040301openalex-snapshot
Foliar Applications of Bacillus subtilis HA1 Culture Filtrate Enhance Tomato Growth and Induce Systemic Resistance against Tobacco mosaic virus Infection
inferred← citeshttps://doi.org/10.3390/ijms14011232openalex-snapshot
From Protein Engineering to Immobilization: Promising Strategies for the Upgrade of Industrial Enzymes
inferred← citeshttps://doi.org/10.3390/jof9020167openalex-snapshot
Trichoderma pubescens Elicit Induced Systemic Resistance in Tomato Challenged by Rhizoctonia solani
inferred← citeshttps://doi.org/10.3390/toxics13090805openalex-snapshot
Single Super Phosphate Improves Lolium perenne Quality and Rhizosphere Microorganism Structure Under Combined Cadmium and Arsenic Stress
inferred← citeshttps://doi.org/10.3390/v14081830openalex-snapshot
Induction of Systemic Resistance to Tobacco mosaic virus in Tomato through Foliar Application of Bacillus amyloliquefaciens Strain TBorg1 Culture Filtrate
inferred← citeshttps://doi.org/10.4172/2157-7439.1000522openalex-snapshot
Biosynthesis and Characterization, Antioxidant and Antimicrobial Activities of Selenium Nanoparticles from Ethanol Extract of Bee Propolis
inferred← citeshttps://doi.org/10.51372/bioagro331.2openalex-snapshot
Role of salicylic acid in heat stress tolerance in tri-genomic Brassica napus L.
inferred← citeshttps://doi.org/10.56093/ijas.v95i1.146067openalex-snapshot
A comparative study on tomato (Solanum lycopersicum) quality under different soil and nutrient management
inferred← citeshttps://doi.org/10.6084/m9.figshare.26739264openalex-snapshot
Additional file 1 of Seed priming with potassium nitrate alleviates the high temperature stress by modulating growth and antioxidant potential in carrot seeds and seedlings
inferred← citeshttps://doi.org/10.70675/3a76f159z03e3z4559zb2e3z3fa5d90698c0openalex-snapshot
Mise au point d'un nouveau modèle animal pour l'évaluation de la toxicité et de la perturbation du développement : application aux neurotoxiques organophosphorés
inferred← citeshttps://doi.org/10.70675/6b5ffa12z6b3ez4d89zb8ddz571a4a21450fopenalex-snapshot
Développement d'une nouvelle génération de pansements antimicrobiens à base d'enzyme à activité lactonase
inferred← citeshttps://doi.org/10.7287/peerj.14845v0.1/reviews/1openalex-snapshot
Peer Review #1 of "Cloning and comparative modeling identifies a highly stress tolerant Cu/Zn cytosolic super oxide dismutase 2 from a drought tolerant maize inbred line (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.14845v0.1/reviews/2openalex-snapshot
Peer Review #2 of "Cloning and comparative modeling identifies a highly stress tolerant Cu/Zn cytosolic super oxide dismutase 2 from a drought tolerant maize inbred line (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.14845v0.1/reviews/3openalex-snapshot
Peer Review #3 of "Cloning and comparative modeling identifies a highly stress tolerant Cu/Zn cytosolic super oxide dismutase 2 from a drought tolerant maize inbred line (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.14845v0.2/reviews/1openalex-snapshot
Peer Review #1 of "Cloning and comparative modeling identifies a highly stress tolerant Cu/Zn cytosolic super oxide dismutase 2 from a drought tolerant maize inbred line (v0.2)"
inferred← citeshttps://doi.org/10.7287/peerj.14845v0.2/reviews/2openalex-snapshot
Peer Review #2 of "Cloning and comparative modeling identifies a highly stress tolerant Cu/Zn cytosolic super oxide dismutase 2 from a drought tolerant maize inbred line (v0.2)"
inferred← citeshttps://doi.org/10.7287/peerj.14845v0.2/reviews/3openalex-snapshot
Peer Review #3 of "Cloning and comparative modeling identifies a highly stress tolerant Cu/Zn cytosolic super oxide dismutase 2 from a drought tolerant maize inbred line (v0.2)"
inferred← citeshttps://doi.org/10.7717/peerj.14845openalex-snapshot
Cloning and comparative modeling identifies a highly stress tolerant Cu/Zn cytosolic super oxide dismutase 2 from a drought tolerant maize inbred line
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.