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  1. Book ; Thesis: Proteome-wide roGFP2-tagging reveals protein context-specific oxidation and its modulation by nutrient availability

    Bosch, Katharina / Dick, Tobias P.

    2022  

    Institution Universität Heidelberg
    Author's details presented by M.Sc Katharina Bosch ; first referee: Prof. Dr. Tobias Dick, second referee: Prof. Dr. Michael Knop
    Language English
    Size v, 170 Seiten, Illustrationen, Diagramme
    Publishing place Heidelberg
    Publishing country Germany
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Dissertation, Ruperto Carola University Heidelberg, 2022
    Note Text Englisch, Zusammenfassung in englischer und deutscher Sprache
    HBZ-ID HT030008059
    Database Catalogue ZB MED Medicine, Health

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  2. Book ; Thesis: The GAPDH redox switch

    Rechmann, Benedikt / Dick, Tobias P. / Teleman, Aurelio A.

    a guardian of cellular reductive capacity that promotes tumor growth and limits efficiency of pro-oxidative tumor therapies

    2020  

    Institution Universität Heidelberg
    Author's details presented by Benedikt Rechmann, M.Sc. ; first referee: Privatdozent Dr. Tobias P. Dick, second referee: Professor Dr. Aurelio Teleman
    Language English ; German
    Size XIX, 118 Seiten, Diagramme, Illustrationen
    Publishing place Heidelberg
    Publishing country Germany
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Dissertation, Ruperto Carola University Heidelberg, 2020
    Note Text in Englisch, Zusammenfassung in deutscher und englischer Sprache
    HBZ-ID HT021003415
    Database Catalogue ZB MED Medicine, Health

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  3. Article ; Online: Using the heme peroxidase APEX2 to probe intracellular H

    Eid, Mohammad / Barayeu, Uladzimir / Sulková, Kateřina / Aranda-Vallejo, Carla / Dick, Tobias P

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 1239

    Abstract: Currently available genetically encoded ... ...

    Abstract Currently available genetically encoded H
    MeSH term(s) Heme ; Hydrogen Peroxide ; Oxidation-Reduction ; Peroxidases/chemistry ; Peroxidases/metabolism ; Sulfhydryl Compounds
    Chemical Substances Heme (42VZT0U6YR) ; Hydrogen Peroxide (BBX060AN9V) ; Peroxidases (EC 1.11.1.-) ; Sulfhydryl Compounds
    Language English
    Publishing date 2024-02-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-024-45511-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: 3-Mercaptopyruvate sulfurtransferase: an enzyme at the crossroads of sulfane sulfur trafficking.

    Pedre, Brandán / Dick, Tobias P

    Biological chemistry

    2020  Volume 402, Issue 3, Page(s) 223–237

    Abstract: 3-Mercaptopyruvate sulfurtransferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate to generate an enzyme-bound hydropersulfide. Subsequently, MPST transfers the persulfide's outer sulfur atom to proteins or small molecule acceptors. MPST ... ...

    Abstract 3-Mercaptopyruvate sulfurtransferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate to generate an enzyme-bound hydropersulfide. Subsequently, MPST transfers the persulfide's outer sulfur atom to proteins or small molecule acceptors. MPST activity is known to be involved in hydrogen sulfide generation, tRNA thiolation, protein urmylation and cyanide detoxification. Tissue-specific changes in MPST expression correlate with ageing and the development of metabolic disease. Deletion and overexpression experiments suggest that MPST contributes to oxidative stress resistance, mitochondrial respiratory function and the regulation of fatty acid metabolism. However, the role and regulation of MPST in the larger physiological context remain to be understood.
    MeSH term(s) Animals ; Cysteine/analogs & derivatives ; Cysteine/chemistry ; Cysteine/metabolism ; Humans ; Molecular Structure ; Sulfur/chemistry ; Sulfur/metabolism ; Sulfurtransferases/chemistry ; Sulfurtransferases/metabolism
    Chemical Substances 3-mercaptopyruvic acid (5Z1F5OW4YB) ; Sulfur (70FD1KFU70) ; Sulfurtransferases (EC 2.8.1.-) ; 3-mercaptopyruvate sulphurtransferase (EC 2.8.1.2) ; Cysteine (K848JZ4886)
    Language English
    Publishing date 2020-10-21
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1334659-3
    ISSN 1437-4315 ; 1431-6730 ; 1432-0355
    ISSN (online) 1437-4315
    ISSN 1431-6730 ; 1432-0355
    DOI 10.1515/hsz-2020-0249
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: A comparison of Prx- and OxyR-based H

    Kritsiligkou, Paraskevi / Shen, Tzu Keng / Dick, Tobias P

    The Journal of biological chemistry

    2021  Volume 297, Issue 1, Page(s) 100866

    Abstract: Genetically encoded fluorescent ... ...

    Abstract Genetically encoded fluorescent H
    MeSH term(s) Biosensing Techniques/methods ; Biosensing Techniques/standards ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/metabolism ; Genes, Reporter ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; Hydrogen Peroxide/analysis ; Hydrogen Peroxide/metabolism ; Peroxidases/genetics ; Peroxidases/metabolism ; Peroxiredoxins/genetics ; Peroxiredoxins/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Repressor Proteins/genetics ; Repressor Proteins/metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Escherichia coli Proteins ; Recombinant Proteins ; Repressor Proteins ; Saccharomyces cerevisiae Proteins ; oxyR protein, E coli ; Green Fluorescent Proteins (147336-22-9) ; Hydrogen Peroxide (BBX060AN9V) ; Peroxidases (EC 1.11.1.-) ; Tsa2 protein, S cerevisiae (EC 1.11.1.-) ; Peroxiredoxins (EC 1.11.1.15)
    Language English
    Publishing date 2021-06-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2021.100866
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  6. Article ; Online: Dynamics of thiol-based redox switches: redox at its peak!

    Herrmann, Johannes M / Becker, Katja / Dick, Tobias P

    Biological chemistry

    2021  Volume 402, Issue 3, Page(s) 221–222

    MeSH term(s) Oxidation-Reduction ; Protein Processing, Post-Translational ; Proteins/chemistry ; Sulfhydryl Compounds/chemistry
    Chemical Substances Proteins ; Sulfhydryl Compounds
    Language English
    Publishing date 2021-01-19
    Publishing country Germany
    Document type Editorial ; Research Support, Non-U.S. Gov't
    ZDB-ID 1334659-3
    ISSN 1437-4315 ; 1431-6730 ; 1432-0355
    ISSN (online) 1437-4315
    ISSN 1431-6730 ; 1432-0355
    DOI 10.1515/hsz-2020-0387
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  7. Article ; Online: A role for peroxiredoxins in H

    Barata, Ana G / Dick, Tobias P

    Redox biology

    2019  Volume 28, Page(s) 101340

    Abstract: The p38 mitogen-activated protein kinase (MAPK) signaling pathway plays an important role in the cellular response to various stresses and its deregulation accompanies pathological conditions such as cancer and chronic inflammation. Hydrogen peroxide ( ... ...

    Abstract The p38 mitogen-activated protein kinase (MAPK) signaling pathway plays an important role in the cellular response to various stresses and its deregulation accompanies pathological conditions such as cancer and chronic inflammation. Hydrogen peroxide (H
    MeSH term(s) Animals ; Cell Line ; Drosophila ; Humans ; Hydrogen Peroxide/metabolism ; MAP Kinase Kinase Kinases/metabolism ; MAP Kinase Signaling System ; Models, Biological ; Oxidation-Reduction ; Phosphorylation ; Signal Transduction ; p38 Mitogen-Activated Protein Kinases/metabolism
    Chemical Substances Hydrogen Peroxide (BBX060AN9V) ; p38 Mitogen-Activated Protein Kinases (EC 2.7.11.24) ; MAP Kinase Kinase Kinases (EC 2.7.11.25)
    Language English
    Publishing date 2019-10-08
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2701011-9
    ISSN 2213-2317 ; 2213-2317
    ISSN (online) 2213-2317
    ISSN 2213-2317
    DOI 10.1016/j.redox.2019.101340
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  8. Article ; Online: Emergence of (hydro)persulfides as suppressors of lipid peroxidation and ferroptotic cell death.

    Wu, Zijun / Barayeu, Uladzimir / Schilling, Danny / Dick, Tobias P / Pratt, Derek A

    Current opinion in chemical biology

    2023  Volume 76, Page(s) 102353

    Abstract: Recognition of the prevalence of hydropersulfides (RSSH) and characterization of their enhanced two-electron reactivity relative to thiols have led to their implication in maintaining cellular redox homeostasis, in addition to other potential roles. ... ...

    Abstract Recognition of the prevalence of hydropersulfides (RSSH) and characterization of their enhanced two-electron reactivity relative to thiols have led to their implication in maintaining cellular redox homeostasis, in addition to other potential roles. Recent attention on the one-electron reactivity of RSSH has uncovered their potent radical-trapping antioxidant activity, which enables them to inhibit phospholipid peroxidation and associated cell death by ferroptosis. Herein, we briefly review key aspects of the reactivity and underlying physicochemical properties of RSSH. We emphasize their reactivity to radicals-particularly lipid peroxyl radicals that propagate the lipid peroxidation chain reaction-and the recent recognition that this results in ferroptosis suppression. We highlight open questions related to recent developments in this area and, given that all living organisms possess the ability to synthesize persulfides endogenously, suggest they may be primordial radical scavengers that occurred early in evolution and still play a role today.
    MeSH term(s) Lipid Peroxidation ; Sulfides/chemistry ; Antioxidants/chemistry ; Cell Death
    Chemical Substances persulfides ; Sulfides ; Antioxidants
    Language English
    Publishing date 2023-06-24
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1439176-4
    ISSN 1879-0402 ; 1367-5931
    ISSN (online) 1879-0402
    ISSN 1367-5931
    DOI 10.1016/j.cbpa.2023.102353
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  9. Article ; Online: Proteome-wide tagging with an H

    Kritsiligkou, Paraskevi / Bosch, Katharina / Shen, Tzu Keng / Meurer, Matthias / Knop, Michael / Dick, Tobias P

    Proceedings of the National Academy of Sciences of the United States of America

    2023  Volume 120, Issue 48, Page(s) e2314043120

    Abstract: Hydrogen peroxide ( ... ...

    Abstract Hydrogen peroxide (H
    MeSH term(s) Hydrogen Peroxide/metabolism ; Proteome/metabolism ; Green Fluorescent Proteins/metabolism ; Oxidation-Reduction ; Biosensing Techniques
    Chemical Substances Hydrogen Peroxide (BBX060AN9V) ; Proteome ; Green Fluorescent Proteins (147336-22-9)
    Language English
    Publishing date 2023-11-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2314043120
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  10. Article ; Online: The influence of alkylating agents on sulfur-sulfur bonds in per- and polysulfides.

    Schilling, Danny / Ditrói, Tamás / Barayeu, Uladzimir / Jurányi, Eszter Petra / Nagy, Peter / Dick, Tobias P

    Current opinion in chemical biology

    2023  Volume 76, Page(s) 102368

    Abstract: Per- and polysulfides are sulfane sulfur species produced inside living cells, in organisms as diverse as bacteria, plants and humans, but their biological roles remain to be fully understood. Unfortunately, due to their reactivity, per- and polysulfides ...

    Abstract Per- and polysulfides are sulfane sulfur species produced inside living cells, in organisms as diverse as bacteria, plants and humans, but their biological roles remain to be fully understood. Unfortunately, due to their reactivity, per- and polysulfides are easily altered, interconverted or lost during the processing and analysis of biological material. Thus, all current analytical methods make use of alkylating agents, to quench reactivity of hydropersulfides and hydropolysulfides and also to prevent free thiols from attacking sulfur chains in hydropolysulfides and dialkyl polysulfides. However, recent findings reveal that alkylating agents can also destroy per- and polysulfides, to varying degrees, depending on the choice of alkylating agent. Here, we discuss the challenges associated with the alkylation of per- and polysulfides, the single most important step for their preservation and detection in biological samples.
    MeSH term(s) Humans ; Alkylating Agents ; Sulfides/chemistry ; Sulfur/chemistry ; Sulfhydryl Compounds
    Chemical Substances polysulfide (9080-49-3) ; Alkylating Agents ; Sulfides ; Sulfur (70FD1KFU70) ; Sulfhydryl Compounds
    Language English
    Publishing date 2023-07-18
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 1439176-4
    ISSN 1879-0402 ; 1367-5931
    ISSN (online) 1879-0402
    ISSN 1367-5931
    DOI 10.1016/j.cbpa.2023.102368
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