Výsledky vyhledávání - "Ingvild, Gudim"

Akademický článek

Thioredoxin reductase from Bacillus cereus exhibits distinct reduction and NADPH‐binding properties

Autor: Marita Shoor, Ingvild Gudim, Hans‐Petter Hersleth, Marta Hammerstad

Publikováno v: FEBS Open Bio, Vol 11, Iss 11, Pp 3019-3031 (2021)

Low‐molecular‐weight (low Mr) thioredoxin reductases (TrxRs) are homodimeric NADPH‐dependent dithiol flavoenzymes that reduce thioredoxins (Trxs) or Trx‐like proteins involved in the activation networks of enzymes, such as the bacterial class

Externí odkaz: https://doaj.org/article/609f43615c98423b8405c6b3b3a86246

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Thioredoxin reductase from Bacillus cereus exhibits distinct reduction and NADPH‐binding properties

Autor: Hans-Petter Hersleth, Marta Hammerstad, Marita Shoor, Ingvild Gudim

Publikováno v: FEBS Open Bio, Vol 11, Iss 11, Pp 3019-3031 (2021)
'FEBS Open Bio ', vol: 11, pages: 3019-3031 (2021)
FEBS Open Bio

Low‐molecular‐weight (low M r) thioredoxin reductases (TrxRs) are homodimeric NADPH‐dependent dithiol flavoenzymes that reduce thioredoxins (Trxs) or Trx‐like proteins involved in the activation networks of enzymes, such as the bacterial clas

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c265a845744d79d1992b9759ee5f1244
https://doaj.org/article/609f43615c98423b8405c6b3b3a86246

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Akademický článek

Measurement of FNR-NrdI Interaction by Microscale Thermophoresis (MST)

Autor: Ingvild Gudim, Marie Lofstad, Marta Hammerstad, Hans-Petter Hersleth

Publikováno v: Bio-Protocol, Vol 7, Iss 8 (2017)

This protocol describes how to measure protein-protein interactions by microscale thermophoresis (MST) using the MonolithTM NT.115 instrument (NanoTemper). We have used the protocol to determine the binding affinities between three different flavodox

Externí odkaz: https://doaj.org/article/7b133bc28ab2411dbd6a388d053d798c

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The Crystal structures of bacillithiol disulfide reductase Bdr (YpdA) provide structural and functional insight into a new type of FAD-containing NADPH-dependent oxidoreductase

Autor: Ingvild Gudim, Hans-Petter Hersleth, Marta Hammerstad

Publikováno v: 'Biochemistry ', vol: 59, pages: 4793-4798 (2020)
Biochemistry

Low G+C Gram-positive Firmicutes, such as the clinically important pathogens Staphylococcus aureus and Bacillus cereus, use the low-molecular weight thiol bacillithiol (BSH) as a defense mechanism to buffer the intracellular redox environment and cou

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::80c3f08316006ba754341602c5e3996e
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:56950

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The Crystal Structures of Bacillithiol Disulfide Reductase YpdA Reveal Structural and Functional Insight into a New Type of FAD-Containing NADPH-Dependent Oxidoreductases

Autor: Hans-Petter Hersleth, Marta Hammerstad, Ingvild Gudim

Low G+C Gram-positive Firmicutes, such as the clinically important pathogens Staphylococcus aureus and Bacillus cereus, use the low-molecular weight (LMW) thiol bacillithiol (BSH) as a defense mechanism to buffer the intracellular redox environment a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7ca73210d8242d652f25ea7f2fb0d2d1
https://doi.org/10.1101/2020.12.02.408641

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High-resolution crystal structures reveal a mixture of conformers of the Gly61-Asp62 peptide bond in an oxidized flavodoxin from Bacillus cereus

Autor: Marie Lofstad, Ingvild Gudim, Hans-Petter Hersleth, Wouter van Beek

Publikováno v: Protein Science. 27:1439-1449

Flavodoxins (Flds) are small proteins that shuttle electrons in a range of reactions in microorganisms. Flds contain a redox-active cofactor, a flavin mononucleotide (FMN), and it is well established that when Flds are reduced by one electron, a pept

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::050d0caf8eeb0778eb0517e353b90886
https://doi.org/10.1002/pro.3436

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The characterization of different flavodoxin reductase-flavodoxin (FNR-Fld) interactions reveals an efficient FNR-Fld redox pair and identifies a novel FNR subclass

Autor: Marta Hammerstad, Ingvild Gudim, Hans-Petter Hersleth, Marie Lofstad

Publikováno v: 'Biochemistry ', vol: 57, pages: 5427-5436 (2018)

Flavodoxins (Flds) are small, bacterial proteins that transfer electrons to various redox enzymes. Flavodoxins are reduced by ferredoxin/flavodoxin NADP+ oxidoreductases (FNRs), but little is known of the FNR-Fld interaction. Here, we compare the int

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ec9bc45c4ee4da30abe07eccb06055a
https://epn-library.esrf.fr/flora/jsp/index_view_direct_anonymous.jsp?record=doc:PUB_ESRF:50766

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