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1
A distal ligand mutes the interaction of hydrogen sulfide with human neuroglobin
A distal ligand mutes the interaction of hydrogen sulfide with human neuroglobin
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A distal ligand mutes the interaction of hydrogen sulfide with human neuroglobin

The Journal of biological chemistry, 2017-04, Vol.292 (16), p.6512-6528 [Peer Reviewed Journal]

2017 © 2017 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2017 by The American Society for Biochemistry and Molecular Biology, Inc. ;2017 by The American Society for Biochemistry and Molecular Biology, Inc. 2017 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M116.770370 ;PMID: 28246171

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2
Organization of the Human Mitochondrial Hydrogen Sulfide Oxidation Pathway
Organization of the Human Mitochondrial Hydrogen Sulfide Oxidation Pathway
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Organization of the Human Mitochondrial Hydrogen Sulfide Oxidation Pathway

The Journal of biological chemistry, 2014-11, Vol.289 (45), p.30901-30910 [Peer Reviewed Journal]

2014 © 2014 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2014 by The American Society for Biochemistry and Molecular Biology, Inc. ;2014 by The American Society for Biochemistry and Molecular Biology, Inc. 2014 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M114.602664 ;PMID: 25225291

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3
A carbohydrate-binding family 48 module enables feruloyl esterase action on polymeric arabinoxylan
A carbohydrate-binding family 48 module enables feruloyl esterase action on polymeric arabinoxylan
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A carbohydrate-binding family 48 module enables feruloyl esterase action on polymeric arabinoxylan

The Journal of biological chemistry, 2019-11, Vol.294 (46), p.17339-17353 [Peer Reviewed Journal]

2019 © 2019 Holck et al. ;2019 Holck et al. ;2019 Holck et al. 2019 Holck et al. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.RA119.009523 ;PMID: 31558605

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4
Hyperoxidation of peroxiredoxins 2 and 3: rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine
Hyperoxidation of peroxiredoxins 2 and 3: rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine
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Hyperoxidation of peroxiredoxins 2 and 3: rate constants for the reactions of the sulfenic acid of the peroxidatic cysteine

The Journal of biological chemistry, 2013-05, Vol.288 (20), p.14170-14177 [Peer Reviewed Journal]

2013 by The American Society for Biochemistry and Molecular Biology, Inc. 2013 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M113.460881 ;PMID: 23543738

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5
Glycoside hydrolase family 18 and 20 enzymes are novel targets of the traditional medicine berberine
Glycoside hydrolase family 18 and 20 enzymes are novel targets of the traditional medicine berberine
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Glycoside hydrolase family 18 and 20 enzymes are novel targets of the traditional medicine berberine

The Journal of biological chemistry, 2018-10, Vol.293 (40), p.15429-15438 [Peer Reviewed Journal]

2018 © 2018 Duan et al. ;2018 Duan et al. ;2018 Duan et al. 2018 Duan et al. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.RA118.004351 ;PMID: 30135205

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6
PqsBC, a Condensing Enzyme in the Biosynthesis of the Pseudomonas aeruginosa Quinolone Signal: CRYSTAL STRUCTURE, INHIBITION, AND REACTION MECHANISM
PqsBC, a Condensing Enzyme in the Biosynthesis of the Pseudomonas aeruginosa Quinolone Signal: CRYSTAL STRUCTURE, INHIBITION, AND REACTION MECHANISM
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PqsBC, a Condensing Enzyme in the Biosynthesis of the Pseudomonas aeruginosa Quinolone Signal: CRYSTAL STRUCTURE, INHIBITION, AND REACTION MECHANISM

The Journal of biological chemistry, 2016-03, Vol.291 (13), p.6610-6624 [Peer Reviewed Journal]

2016 by The American Society for Biochemistry and Molecular Biology, Inc. ;2016 by The American Society for Biochemistry and Molecular Biology, Inc. 2016 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M115.708453 ;PMID: 26811339

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7
The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects
The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects
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The small GTPases K-Ras, N-Ras, and H-Ras have distinct biochemical properties determined by allosteric effects

The Journal of biological chemistry, 2017-08, Vol.292 (31), p.12981-12993 [Peer Reviewed Journal]

2017 © 2017 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2017 by The American Society for Biochemistry and Molecular Biology, Inc. ;2017 by The American Society for Biochemistry and Molecular Biology, Inc. 2017 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M117.778886 ;PMID: 28630043

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8
Structure-based Conversion of the Coenzyme Requirement of a Short-chain Dehydrogenase/Reductase Involved in Bacterial Alginate Metabolism
Structure-based Conversion of the Coenzyme Requirement of a Short-chain Dehydrogenase/Reductase Involved in Bacterial Alginate Metabolism
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Structure-based Conversion of the Coenzyme Requirement of a Short-chain Dehydrogenase/Reductase Involved in Bacterial Alginate Metabolism

The Journal of biological chemistry, 2014-11, Vol.289 (48), p.33198-33214 [Peer Reviewed Journal]

2014 © 2014 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2014 by The American Society for Biochemistry and Molecular Biology, Inc. ;2014 by The American Society for Biochemistry and Molecular Biology, Inc. 2014 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M114.585661 ;PMID: 25288804

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9
Investigating the Sensitivity of NAD+-dependent Sirtuin Deacylation Activities to NADH
Investigating the Sensitivity of NAD+-dependent Sirtuin Deacylation Activities to NADH
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Investigating the Sensitivity of NAD+-dependent Sirtuin Deacylation Activities to NADH

The Journal of biological chemistry, 2016-03, Vol.291 (13), p.7128-7141 [Peer Reviewed Journal]

2016 © 2016 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2016 by The American Society for Biochemistry and Molecular Biology, Inc. ;2016 by The American Society for Biochemistry and Molecular Biology, Inc. 2016 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M115.668699 ;PMID: 26861872

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10
How Covalent Heme to Protein Bonds Influence the Formation and Reactivity of Redox Intermediates of a Bacterial Peroxidase
How Covalent Heme to Protein Bonds Influence the Formation and Reactivity of Redox Intermediates of a Bacterial Peroxidase
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How Covalent Heme to Protein Bonds Influence the Formation and Reactivity of Redox Intermediates of a Bacterial Peroxidase

The Journal of biological chemistry, 2014-11, Vol.289 (45), p.31480-31491 [Peer Reviewed Journal]

2014 © 2014 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2014 by The American Society for Biochemistry and Molecular Biology, Inc. ;2014 by The American Society for Biochemistry and Molecular Biology, Inc. 2014 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M114.595157 ;PMID: 25246525

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11
Mechanical Stability and Fibrinolytic Resistance of Clots Containing Fibrin, DNA, and Histones
Mechanical Stability and Fibrinolytic Resistance of Clots Containing Fibrin, DNA, and Histones
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Mechanical Stability and Fibrinolytic Resistance of Clots Containing Fibrin, DNA, and Histones

The Journal of biological chemistry, 2013-03, Vol.288 (10), p.6946-6956 [Peer Reviewed Journal]

2013 © 2013 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2013 by The American Society for Biochemistry and Molecular Biology, Inc. 2013 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M112.404301 ;PMID: 23293023

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12
Spectroscopic and Kinetic Properties of the Molybdenum-containing, NAD+-dependent Formate Dehydrogenase from Ralstonia eutropha
Spectroscopic and Kinetic Properties of the Molybdenum-containing, NAD+-dependent Formate Dehydrogenase from Ralstonia eutropha
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Spectroscopic and Kinetic Properties of the Molybdenum-containing, NAD+-dependent Formate Dehydrogenase from Ralstonia eutropha

The Journal of biological chemistry, 2016-01, Vol.291 (3), p.1162-1174 [Peer Reviewed Journal]

2016 © 2016 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2016 by The American Society for Biochemistry and Molecular Biology, Inc. ;2016 by The American Society for Biochemistry and Molecular Biology, Inc. 2016 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M115.688457 ;PMID: 26553877

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13
Kinetic processivity of the two-step oxidations of progesterone and pregnenolone to androgens by human cytochrome P450 17A1
Kinetic processivity of the two-step oxidations of progesterone and pregnenolone to androgens by human cytochrome P450 17A1
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Kinetic processivity of the two-step oxidations of progesterone and pregnenolone to androgens by human cytochrome P450 17A1

The Journal of biological chemistry, 2017-08, Vol.292 (32), p.13168-13185 [Peer Reviewed Journal]

2017 © 2017 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology ;2017 by The American Society for Biochemistry and Molecular Biology, Inc. ;2017 by The American Society for Biochemistry and Molecular Biology, Inc. 2017 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M117.794917 ;PMID: 28684414

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14
Insights into the Role of the Unusual Disulfide Bond in Copper-Zinc Superoxide Dismutase
Insights into the Role of the Unusual Disulfide Bond in Copper-Zinc Superoxide Dismutase
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Insights into the Role of the Unusual Disulfide Bond in Copper-Zinc Superoxide Dismutase

The Journal of biological chemistry, 2015-01, Vol.290 (4), p.2405-2418 [Peer Reviewed Journal]

2015 © 2015 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2015 by The American Society for Biochemistry and Molecular Biology, Inc. ;2015 by The American Society for Biochemistry and Molecular Biology, Inc. 2015 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M114.588798 ;PMID: 25433341

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15
Characterization of a Linked Jumonji Domain of the KDM5/JARID1 Family of Histone H3 Lysine 4 Demethylases
Characterization of a Linked Jumonji Domain of the KDM5/JARID1 Family of Histone H3 Lysine 4 Demethylases
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Characterization of a Linked Jumonji Domain of the KDM5/JARID1 Family of Histone H3 Lysine 4 Demethylases

The Journal of biological chemistry, 2016-02, Vol.291 (6), p.2631-2646 [Peer Reviewed Journal]

2016 © 2016 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2016 by The American Society for Biochemistry and Molecular Biology, Inc. ;2016 by The American Society for Biochemistry and Molecular Biology, Inc. 2016 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M115.698449 ;PMID: 26645689

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16
Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide
Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide
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Reaction of Hydrogen Sulfide with Disulfide and Sulfenic Acid to Form the Strongly Nucleophilic Persulfide

The Journal of biological chemistry, 2015-11, Vol.290 (45), p.26866-26880 [Peer Reviewed Journal]

2015 © 2015 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2015 by The American Society for Biochemistry and Molecular Biology, Inc. ;2015 by The American Society for Biochemistry and Molecular Biology, Inc. 2015 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M115.672816 ;PMID: 26269587

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17
Restricting the conformational freedom of the neuronal nitric-oxide synthase flavoprotein domain reveals impact on electron transfer and catalysis
Restricting the conformational freedom of the neuronal nitric-oxide synthase flavoprotein domain reveals impact on electron transfer and catalysis
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Restricting the conformational freedom of the neuronal nitric-oxide synthase flavoprotein domain reveals impact on electron transfer and catalysis

The Journal of biological chemistry, 2017-04, Vol.292 (16), p.6753-6764 [Peer Reviewed Journal]

2017 © 2017 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2017 by The American Society for Biochemistry and Molecular Biology, Inc. ;2017 by The American Society for Biochemistry and Molecular Biology, Inc. 2017 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M117.777219 ;PMID: 28232486

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18
Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase–rhodanese fusion protein functions in sulfur assimilation
Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase–rhodanese fusion protein functions in sulfur assimilation
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Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase–rhodanese fusion protein functions in sulfur assimilation

The Journal of biological chemistry, 2017-08, Vol.292 (34), p.14026-14038 [Peer Reviewed Journal]

2017 © 2017 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2017 by The American Society for Biochemistry and Molecular Biology, Inc. ;2017 by The American Society for Biochemistry and Molecular Biology, Inc. 2017 The American Society for Biochemistry and Molecular Biology, Inc. ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M117.790170 ;PMID: 28684420

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19
Highly Potent Inhibitors of Proprotein Convertase Furin as Potential Drugs for Treatment of Infectious Diseases
Highly Potent Inhibitors of Proprotein Convertase Furin as Potential Drugs for Treatment of Infectious Diseases
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Highly Potent Inhibitors of Proprotein Convertase Furin as Potential Drugs for Treatment of Infectious Diseases

The Journal of biological chemistry, 2012-06, Vol.287 (26), p.21992-22003 [Peer Reviewed Journal]

2012 © 2012 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2012 by The American Society for Biochemistry and Molecular Biology, Inc. 2012 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M111.332643 ;PMID: 22539349

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20
The Non-catalytic B Subunit of Coagulation Factor XIII Accelerates Fibrin Cross-linking
The Non-catalytic B Subunit of Coagulation Factor XIII Accelerates Fibrin Cross-linking
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The Non-catalytic B Subunit of Coagulation Factor XIII Accelerates Fibrin Cross-linking

The Journal of biological chemistry, 2015-05, Vol.290 (19), p.12027-12039 [Peer Reviewed Journal]

2015 © 2015 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. ;2015 by The American Society for Biochemistry and Molecular Biology, Inc. ;2015 by The American Society for Biochemistry and Molecular Biology, Inc. 2015 ;ISSN: 0021-9258 ;EISSN: 1083-351X ;DOI: 10.1074/jbc.M114.608570 ;PMID: 25809477

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