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The biosynthesis of thymol, carvacrol, and thymohydroquinone in Lamiaceae proceeds via cytochrome P450s and a short-chain dehydrogenase
The biosynthesis of thymol, carvacrol, and thymohydroquinone in Lamiaceae proceeds via cytochrome P450s and a short-chain dehydrogenase
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The biosynthesis of thymol, carvacrol, and thymohydroquinone in Lamiaceae proceeds via cytochrome P450s and a short-chain dehydrogenase

Krause, Sandra T ; Liao, Pan ; Crocoll, Christoph ; Boachon, Benoît ; Förster, Christiane ; Leidecker, Franziska ; Wiese, Natalie ; Zhao, Dongyan ; Wood, Joshua C ; Buell, C Robin ; Gershenzon, Jonathan ; Dudareva, Natalia ; Degenhardt, Jörg

Proceedings of the National Academy of Sciences - PNAS, 2021-12, Vol.118 (52), p.1 [Periódico revisado por pares]

United States: National Academy of Sciences

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2
Dehydrogenase reductase 9 (SDR9C4) and related homologs recognize a broad spectrum of lipid mediator oxylipins as substrates
Dehydrogenase reductase 9 (SDR9C4) and related homologs recognize a broad spectrum of lipid mediator oxylipins as substrates
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Dehydrogenase reductase 9 (SDR9C4) and related homologs recognize a broad spectrum of lipid mediator oxylipins as substrates

Belyaeva, Olga V. ; Wirth, Samuel E. ; Boeglin, William E. ; Karki, Suman ; Goggans, Kelli R. ; Wendell, Stacy G. ; Popov, Kirill M. ; Brash, Alan R. ; Kedishvili, Natalia Y.

The Journal of biological chemistry, 2022-01, Vol.298 (1), p.101527-101527, Article 101527 [Periódico revisado por pares]

United States: Elsevier Inc

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3
Exploiting the Catalytic Diversity of Short‐Chain Dehydrogenases/Reductases: Versatile Enzymes from Plants with Extended Imine Substrate Scope
Exploiting the Catalytic Diversity of Short‐Chain Dehydrogenases/Reductases: Versatile Enzymes from Plants with Extended Imine Substrate Scope
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Exploiting the Catalytic Diversity of Short‐Chain Dehydrogenases/Reductases: Versatile Enzymes from Plants with Extended Imine Substrate Scope

Roth, Sebastian ; Kilgore, Matthew B. ; Kutchan, Toni M. ; Müller, Michael

Chembiochem : a European journal of chemical biology, 2018-09, Vol.19 (17), p.1849-1852 [Periódico revisado por pares]

Germany: Wiley Subscription Services, Inc

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4
Cautionary Tale of Using Tris(alkyl)phosphine Reducing Agents with NAD+‑Dependent Enzymes
Cautionary Tale of Using Tris(alkyl)phosphine Reducing Agents with NAD+‑Dependent Enzymes
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Cautionary Tale of Using Tris(alkyl)phosphine Reducing Agents with NAD+‑Dependent Enzymes

Patel, Sagar M ; Smith, Thomas G ; Morton, Martha ; Stiers, Kyle M ; Seravalli, Javier ; Mayclin, Stephen J ; Edwards, Thomas E ; Tanner, John J ; Becker, Donald F

Biochemistry (Easton), 2020-09, Vol.59 (36), p.3285-3289 [Periódico revisado por pares]

United States: American Chemical Society

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5
A poplar short-chain dehydrogenase reductase plays a potential key role in biphenyl detoxification
A poplar short-chain dehydrogenase reductase plays a potential key role in biphenyl detoxification
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A poplar short-chain dehydrogenase reductase plays a potential key role in biphenyl detoxification

Contreras, Ángela ; Merino, Irene ; Álvarez, Enrique ; Bolonio, David ; Ortiz, José-Eugenio ; Oñate-Sánchez, Luis ; Gómez, Luis

Proceedings of the National Academy of Sciences - PNAS, 2021-08, Vol.118 (35), p.1 [Periódico revisado por pares]

United States: National Academy of Sciences

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6
Sex hormones reduce NNK detoxification through inhibition of short-chain dehydrogenases/reductases and aldo-keto reductases in vitro
Sex hormones reduce NNK detoxification through inhibition of short-chain dehydrogenases/reductases and aldo-keto reductases in vitro
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Sex hormones reduce NNK detoxification through inhibition of short-chain dehydrogenases/reductases and aldo-keto reductases in vitro

Stapelfeld, Claudia ; Maser, Edmund

Chemico-biological interactions, 2017-10, Vol.276, p.167-173 [Periódico revisado por pares]

Ireland: Elsevier B.V

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7
Crossing the Border: From Keto‐ to Imine Reduction in Short‐Chain Dehydrogenases/Reductases
Crossing the Border: From Keto‐ to Imine Reduction in Short‐Chain Dehydrogenases/Reductases
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Crossing the Border: From Keto‐ to Imine Reduction in Short‐Chain Dehydrogenases/Reductases

Roth, Sebastian ; Stockinger, Peter ; Steff, Jakob ; Steimle, Simon ; Sautner, Viktor ; Tittmann, Kai ; Pleiss, Jürgen ; Müller, Michael

Chembiochem : a European journal of chemical biology, 2020-09, Vol.21 (18), p.2615-2619 [Periódico revisado por pares]

Germany: Wiley Subscription Services, Inc

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8
Characterization of human short chain dehydrogenase/reductase SDR16C family members related to retinol dehydrogenase 10
Characterization of human short chain dehydrogenase/reductase SDR16C family members related to retinol dehydrogenase 10
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Characterization of human short chain dehydrogenase/reductase SDR16C family members related to retinol dehydrogenase 10

Adams, Mark K. ; Lee, Seung-Ah ; Belyaeva, Olga V. ; Wu, Lizhi ; Kedishvili, Natalia Y.

Chemico-biological interactions, 2017-10, Vol.276, p.88-94 [Periódico revisado por pares]

Ireland: Elsevier B.V

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9
Unexpected Role of a Short‐Chain Dehydrogenase/Reductase Family Protein in Type II Polyketide Biosynthesis
Unexpected Role of a Short‐Chain Dehydrogenase/Reductase Family Protein in Type II Polyketide Biosynthesis
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Unexpected Role of a Short‐Chain Dehydrogenase/Reductase Family Protein in Type II Polyketide Biosynthesis

Gao, Yaojie ; Zhao, Yuchun ; Zhou, Jie ; Yang, Maohua ; Lin, Lin ; Wang, Wenning ; Tao, Meifeng ; Deng, Zixin ; Jiang, Ming

Angewandte Chemie International Edition, 2022-02, Vol.61 (7), p.e202110445-n/a [Periódico revisado por pares]

Germany: Wiley Subscription Services, Inc

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10
Functional analysis of BPSS2242 reveals its detoxification role in Burkholderia pseudomallei under salt stress
Functional analysis of BPSS2242 reveals its detoxification role in Burkholderia pseudomallei under salt stress
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Functional analysis of BPSS2242 reveals its detoxification role in Burkholderia pseudomallei under salt stress

Chamchoy, Kamonwan ; Pumirat, Pornpan ; Reamtong, Onrapak ; Pakotiprapha, Danaya ; Leartsakulpanich, Ubolsree ; Boonyuen, Usa

Scientific reports, 2020-06, Vol.10 (1), p.10453-14, Article 10453 [Periódico revisado por pares]

England: Nature Publishing Group

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