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Mechanism of 17α,20-Lyase and New Hydroxylation Reactions of Human Cytochrome P450 17A1: O LABELING AND OXYGEN SURROGATE EVIDENCE FOR A ROLE OF A PERFERRYL OXYGEN
Mechanism of 17α,20-Lyase and New Hydroxylation Reactions of Human Cytochrome P450 17A1: O LABELING AND OXYGEN SURROGATE EVIDENCE FOR A ROLE OF A PERFERRYL OXYGEN
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Mechanism of 17α,20-Lyase and New Hydroxylation Reactions of Human Cytochrome P450 17A1: O LABELING AND OXYGEN SURROGATE EVIDENCE FOR A ROLE OF A PERFERRYL OXYGEN

Yoshimoto, Francis K. ; Gonzalez, Eric ; Auchus, Richard J. ; Guengerich, F. Peter

The Journal of biological chemistry, 2016-08, Vol.291 (33), p.17143-17164 [Revista revisada por pares]

11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A: American Society for Biochemistry and Molecular Biology

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2
Single-molecule nanopore enzymology
Single-molecule nanopore enzymology
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Single-molecule nanopore enzymology

Willems, Kherim ; Van Meervelt, Veerle ; Wloka, Carsten ; Maglia, Giovanni

Philosophical transactions of the Royal Society of London. Series B. Biological sciences, 2017-08, Vol.372 (1726), p.20160230-20160230 [Revista revisada por pares]

England: The Royal Society

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3
Deimination, Intermediate Filaments and Associated Proteins
Deimination, Intermediate Filaments and Associated Proteins
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Deimination, Intermediate Filaments and Associated Proteins

Briot, Julie ; Simon, Michel ; Méchin, Marie-Claire

International journal of molecular sciences, 2020-11, Vol.21 (22), p.8746 [Revista revisada por pares]

Switzerland: MDPI AG

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4
Crystal structure of phytochromobilin synthase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phytochrome
Crystal structure of phytochromobilin synthase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phytochrome
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Crystal structure of phytochromobilin synthase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phytochrome

Sugishima, Masakazu ; Wada, Kei ; Fukuyama, Keiichi ; Yamamoto, Ken

The Journal of biological chemistry, 2020-01, Vol.295 (3), p.771-782 [Revista revisada por pares]

11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A: American Society for Biochemistry and Molecular Biology

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5
A structural and kinetic survey of GH5_4 endoglucanases reveals determinants of broad substrate specificity and opportunities for biomass hydrolysis
A structural and kinetic survey of GH5_4 endoglucanases reveals determinants of broad substrate specificity and opportunities for biomass hydrolysis
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A structural and kinetic survey of GH5_4 endoglucanases reveals determinants of broad substrate specificity and opportunities for biomass hydrolysis

Glasgow, Evan M. ; Kemna, Elias I. ; Bingman, Craig A. ; Ing, Nicole ; Deng, Kai ; Bianchetti, Christopher M. ; Takasuka, Taichi E. ; Northen, Trent R. ; Fox, Brian G.

The Journal of biological chemistry, 2020-10, Vol.295 (51), p.17752-17769 [Revista revisada por pares]

11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A: American Society for Biochemistry and Molecular Biology

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6
Evolving the naturally compromised chorismate mutase from Mycobacterium tuberculosis to top performance
Evolving the naturally compromised chorismate mutase from Mycobacterium tuberculosis to top performance
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Evolving the naturally compromised chorismate mutase from Mycobacterium tuberculosis to top performance

Fahrig-Kamarauskait≑, Jūrate˙ ; Würth-Roderer, Kathrin ; Thorbjørnsrud, Helen V. ; Mailand, Susanne ; Krengel, Ute ; Kast, Peter

The Journal of biological chemistry, 2020-10, Vol.295 (51), p.17514-17534 [Revista revisada por pares]

11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A: American Society for Biochemistry and Molecular Biology

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7
Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation
Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation
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Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation

Nandi, Suparno ; Razzaghi, Mortezaali ; Srivastava, Dhiraj ; Dey, Mishtu

The Journal of biological chemistry, 2020-09, Vol.295 (51), p.17425-17440 [Revista revisada por pares]

11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A: American Society for Biochemistry and Molecular Biology

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8
Structure and function of Bs164 β-mannosidase from Bacteroides salyersiae the founding member of glycoside hydrolase family GH164
Structure and function of Bs164 β-mannosidase from Bacteroides salyersiae the founding member of glycoside hydrolase family GH164
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Structure and function of Bs164 β-mannosidase from Bacteroides salyersiae the founding member of glycoside hydrolase family GH164

Armstrong, Zachary ; Davies, Gideon J.

The Journal of biological chemistry, 2019-12, Vol.295 (13), p.4316-4326 [Revista revisada por pares]

11200 Rockville Pike, Suite 302, Rockville, MD 20852-3110, U.S.A: American Society for Biochemistry and Molecular Biology

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9
Enzymology of extracellular NAD metabolism
Enzymology of extracellular NAD metabolism
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Enzymology of extracellular NAD metabolism

Gasparrini, Massimiliano ; Sorci, Leonardo ; Raffaelli, Nadia

Cellular and molecular life sciences : CMLS, 2021-04, Vol.78 (7), p.3317-3331 [Revista revisada por pares]

Cham: Springer International Publishing

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10
Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance
Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance
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Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance

Hove-Jensen, Bjarne ; Andersen, Kasper R ; Kilstrup, Mogens ; Martinussen, Jan ; Switzer, Robert L ; Willemoës, Martin

Microbiology and molecular biology reviews, 2017-03, Vol.81 (1) [Revista revisada por pares]

United States: American Society for Microbiology

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