Moonlighting by Different Stressors: Crystal Structure of the Chaperone Species of a 2-Cys Peroxiredoxin - Wikidata - awgldk - TriplyDB

Moonlighting by Different Stressors: Crystal Structure of the Chaperone Species of a 2-Cys Peroxiredoxin

Moonlighting by Different Stressors: Crystal Structure of the Chaperone Species of a 2-Cys Peroxiredoxin

http://www.wikidata.org/entity/Q27677957

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Microbial 2-Cys Peroxiredoxins: Insights into Their Complex Physiological Roles Peroxiredoxins: guardians against oxidative stress and modulators of peroxide signaling A primer on peroxiredoxin biochemistry The Crystal Structures of the Tryparedoxin-Tryparedoxin Peroxidase Couple Unveil the Structural Determinants of Leishmania Detoxification Pathway Peroxiredoxin-1 from the Human Hookworm Ancylostoma ceylanicum Forms a Stable Oxidized Decamer and Is Covalently Inhibited by Conoidin A The crystal structure of archaeal serine hydroxymethyltransferase reveals idiosyncratic features likely required to withstand high temperatures Structure of TSA2 reveals novel features of the active-site loop of peroxiredoxins An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone Thiol-based redox switches Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum.Redox-dependent chaperone/peroxidase function of 2-Cys-Prx from the cyanobacterium Anabaena PCC7120: role in oxidative stress tolerance.A 1-Cys Peroxiredoxin from a Thermophilic Archaeon Moonlights as a Molecular Chaperone to Protect Protein and DNA against Stress-Induced Damage.Kinetic analysis of structural influences on the susceptibility of peroxiredoxins 2 and 3 to hyperoxidation Enhancement of the Chaperone Activity of Alkyl Hydroperoxide Reductase C from Pseudomonas aeruginosa PAO1 Resulting from a Point-Specific Mutation Confers Heat Tolerance in Escherichia coli.An anaerobic bacterium, Bacteroides thetaiotaomicron, uses a consortium of enzymes to scavenge hydrogen peroxide.Peroxiredoxins, gerontogenes linking aging to genome instability and cancer.Linking Peroxiredoxin and Vacuolar-ATPase Functions in Calorie Restriction-Mediated Life Span Extension.Thioredoxin reductase and its inhibitors.Selenocysteine robustness versus cysteine versatility: a hypothesis on the evolution of the moonlighting behaviour of peroxiredoxins.One ring (or two) to hold them all – on the structure and function of protein nanotubes.Neuroprotective effects of PrxI over-expression in an in vitro human Alzheimer's disease model.Catalytic Thr or Ser Residue Modulates Structural Switches in 2-Cys Peroxiredoxin by Distinct Mechanisms.In vivo parameters influencing 2-Cys Prx oligomerization: The role of enzyme sulfinylation.Natural products triptolide, celastrol, and withaferin A inhibit the chaperone activity of peroxiredoxin I.Evidence that glutathione and the glutathione system efficiently recycle 1-cys sulfiredoxin in vivo.Hyperoxidized peroxiredoxin 2 interacts with the protein disulfide- isomerase ERp46.Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7210.Stress-Activated Chaperones: A First Line of Defense.Maintaining a Healthy Proteome during Oxidative Stress.Supramolecular self-assembly of graphene oxide and metal nanoparticles into stacked multilayers by means of a multitasking protein ring.The Peroxiredoxin Family: An Unfolding Story.Reduction of oxalate levels in tomato fruit and consequent metabolic remodeling following overexpression of a fungal oxalate decarboxylase.Metal-induced self-assembly of peroxiredoxin as a tool for sorting ultrasmall gold nanoparticles into one-dimensional clusters A peroxiredoxin-based proteinaceous scaffold for the growth and differentiation of neuronal cells and tumour stem cells in the absence of prodifferentiation agents Molecular mechanism of the Escherichia coli AhpC in the function of a chaperone under heat-shock conditions

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Moonlighting by Different Stressors: Crystal Structure of the Chaperone Species of a 2-Cys Peroxiredoxin

http://www.wikidata.org/entity/Q27677957

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2012 nî lūn-bûn

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2012 թուականի Մարտին հրատարակուած գիտական յօդուած

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2012 թվականի մարտին հրատարակված գիտական հոդված

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2012年の論文

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Moonlighting by Different Stre ...... ecies of a 2-Cys Peroxiredoxin

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Moonlighting by different stre ...... ecies of a 2-Cys peroxiredoxin

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Andrea Bellelli

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David L Williams

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Francesco Angelucci

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Giovanna Boumis

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Ilias Koutris

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Palita Sriratana

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PREX: PeroxiRedoxin classification indEX, a database of subfamily assignments across the diverse peroxiredoxin family

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Crystal structure of a multifunctional 2-Cys peroxiredoxin heme-binding protein 23 kDa/proliferation-associated gene product

Structure of the sulphiredoxin–peroxiredoxin complex reveals an essential repair embrace

Protein Engineering of the Quaternary Sulfiredoxin{middle dot}Peroxiredoxin Enzyme{middle dot}Substrate Complex Reveals the Molecular Basis for Cysteine Sulfinic Acid Phosphorylation

Molecular replacement with MOLREP

Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

Developments in the CCP4 molecular-graphics project

Overview of the CCP4 suite and current developments

MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes

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10.1016/J.STR.2012.01.004

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3

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Maurizio Brunori

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Fulvio Saccoccia

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molecular chaperones

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structural biology

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