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Article ; Online: Primaquine pharmacology in the context of CYP 2D6 pharmacogenomics: Current state of the art.

Marcsisin, Sean R / Reichard, Gregory / Pybus, Brandon S

2016 Volume 161, Page(s) 1–10

Abstract: Primaquine is the only antimalarial drug available to clinicians for the treatment of relapsing forms of malaria. Primaquine development and usage dates back to the 1940s and has been administered to millions of individuals to treat and eliminate malaria ...

Abstract	Primaquine is the only antimalarial drug available to clinicians for the treatment of relapsing forms of malaria. Primaquine development and usage dates back to the 1940s and has been administered to millions of individuals to treat and eliminate malaria infections. Primaquine therapy is not without disadvantages, however, as it can cause life threatening hemolysis in humans with glucose-6-phosphate dehydrogenase (G6PD) deficiency. In addition, the efficacy of primaquine against relapsing malaria was recently linked to CYP 2D6 mediated activation to an active metabolite, the structure of which has escaped definitive identification for over 75years. CYP 2D6 is highly polymorphic among various human populations adding further complexity to a comprehensive understanding of primaquine pharmacology. This review aims to discuss primaquine pharmacology in the context of state of the art understanding of CYP 2D6 mediated 8-aminoquinoline metabolic activation, and shed light on the current knowledge gaps of 8-aminoquinoline mechanistic understanding against relapsing malaria.
MeSH term(s)	Animals ; Antimalarials/adverse effects ; Antimalarials/metabolism ; Antimalarials/pharmacokinetics ; Antimalarials/pharmacology ; Cytochrome P-450 CYP2D6/genetics ; Cytochrome P-450 CYP2D6/metabolism ; Drug Interactions ; Humans ; Metabolomics ; Polymorphism, Genetic ; Primaquine/adverse effects ; Primaquine/metabolism ; Primaquine/pharmacokinetics ; Primaquine/pharmacology ; Prodrugs/adverse effects ; Prodrugs/metabolism ; Prodrugs/pharmacology
Chemical Substances	Antimalarials ; Prodrugs ; Cytochrome P-450 CYP2D6 (EC 1.14.14.1) ; Primaquine (MVR3634GX1)
Language	English
Publishing date	2016
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	194735-7
ISSN	1879-016X ; 0163-7258
ISSN (online)	1879-016X
ISSN	0163-7258
DOI	10.1016/j.pharmthera.2016.03.011
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Article ; Online: Hydrogen exchange mass spectrometry: what is it and what can it tell us?

Marcsisin, Sean R / Engen, John R

Analytical and bioanalytical chemistry

2010 Volume 397, Issue 3, Page(s) 967–972

Abstract: Proteins are undoubtedly some of the most essential molecules of life. While much is known about many proteins, some aspects still remain mysterious. One particularly important aspect of understanding proteins is determining how structure helps dictate ... ...

Abstract	Proteins are undoubtedly some of the most essential molecules of life. While much is known about many proteins, some aspects still remain mysterious. One particularly important aspect of understanding proteins is determining how structure helps dictate function. Continued development and implementation of biophysical techniques that provide information about protein conformation and dynamics is essential. In this review, we discuss hydrogen exchange mass spectrometry and how this method can be used to learn about protein conformation and dynamics. The basic concepts of the method are described, the workflow illustrated, and a few examples of its application are provided.
MeSH term(s)	Animals ; Humans ; Hydrogen/chemistry ; Mass Spectrometry/methods ; Mass Spectrometry/trends ; Protein Conformation ; Proteins/chemistry ; Proteins/metabolism
Chemical Substances	Proteins ; Hydrogen (7YNJ3PO35Z)
Language	English
Publishing date	2010-03-01
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	201093-8
ISSN	1618-2650 ; 0016-1152 ; 0372-7920
ISSN (online)	1618-2650
ISSN	0016-1152 ; 0372-7920
DOI	10.1007/s00216-010-3556-4
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Article ; Online: Molecular insight into the conformational dynamics of the Elongin BC complex and its interaction with HIV-1 Vif.

Marcsisin, Sean R / Engen, John R

Journal of molecular biology

2010 Volume 402, Issue 5, Page(s) 892–904

Abstract: The human immunodeficiency virus type 1 virion infectivity factor (Vif) inhibits the innate viral immunity afforded by the APOBEC3 family of cytidine deaminases. Vif targets the APOBEC3 family for poly-ubiquitination and subsequent proteasomal ... ...

Abstract	The human immunodeficiency virus type 1 virion infectivity factor (Vif) inhibits the innate viral immunity afforded by the APOBEC3 family of cytidine deaminases. Vif targets the APOBEC3 family for poly-ubiquitination and subsequent proteasomal degradation by linking the Elongin-BC-dependent ubiquitin ligase complex with the APOBEC3 proteins. The interaction between Vif and the heterodimeric Elongin BC complex, which is mediated by Vif's viral suppressor of cytokine signaling box, is essential for Vif function. The biophysical consequences of the full-length Vif:Elongin BC interaction have not been extensively reported. In this study, hydrogen exchange mass spectrometry was used to dissect the Vif:Elongin BC interaction. Elongin C was found to be highly dynamic in the Elongin BC complex while Elongin B was much more stable. Recombinant full-length Vif interacted with the Elongin BC complex in vitro with a K(d) of 1.9 μM and resulted in observable changes in deuterium uptake in both Elongin C and B. Upon binding to Elongin BC, no significant global conformational changes were detected in Vif by hydrogen exchange mass spectrometry, but a short fragment of Vif that consisted of the viral suppressor of cytokine signaling box showed decreased deuterium incorporation upon Elongin BC incubation, suggesting that this region folds upon binding.
MeSH term(s)	Amino Acid Sequence ; Elongin ; Humans ; Hydrogen/metabolism ; Mass Spectrometry ; Models, Chemical ; Models, Molecular ; Molecular Sequence Data ; Protein Binding ; Protein Conformation ; Protein Folding ; Protein Interaction Mapping ; Protein Structure, Quaternary ; Transcription Factors/chemistry ; Transcription Factors/metabolism ; vif Gene Products, Human Immunodeficiency Virus/chemistry ; vif Gene Products, Human Immunodeficiency Virus/metabolism
Chemical Substances	ELOB protein, human ; ELOC protein, human ; Elongin ; Transcription Factors ; vif Gene Products, Human Immunodeficiency Virus ; vif protein, Human immunodeficiency virus 1 ; Hydrogen (7YNJ3PO35Z)
Language	English
Publishing date	2010-08-20
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2010.08.026
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Article: Tag and Capture Flow Hydrogen Exchange Mass Spectrometry with a Fluorous-Immobilized Probe

Marcsisin, Sean R / Bradner James E / Engen John R / Liptak Cary / Marineau Jason

Analytical chemistry. 2015 June 16, v. 87, no. 12

2015

Abstract: Analysis of complex mixtures of proteins by hydrogen exchange (HX) mass spectrometry (MS) is limited by oneâs ability to resolve the protein(s) of interest from the proteins that are not of interest. One strategy for overcoming this problem is to tag ... ...

Abstract	Analysis of complex mixtures of proteins by hydrogen exchange (HX) mass spectrometry (MS) is limited by oneâs ability to resolve the protein(s) of interest from the proteins that are not of interest. One strategy for overcoming this problem is to tag the target protein(s) to allow for rapid removal from the mixture for subsequent analysis. Here we illustrate a new solution involving fluorous conjugation of a retrievable probe. The appended fluorous tag allows for facile immobilization on a fluorous surface. When a target protein is passed over the immobilized probe molecule, it can be efficiently captured and then exposed to a flowing stream of deuterated buffer for hydrogen exchange. The utility of this method is illustrated for a model system of the Elongin BC protein complex bound to a peptide from HIV Vif. Efficient capture is demonstrated, and deuteration when immobilized was identical to deuteration in conventional solution-phase hydrogen exchange MS. Protein captured from a crude bacterial cell lysate could also be deuterated without the need for separate purification steps before HX MS. The advantages and disadvantages of the method are discussed in light of miniaturization and automation.
Keywords	automation ; bacteria ; Human immunodeficiency virus ; hydrogen ; mass spectrometry ; proteins
Language	English
Dates of publication	2015-0616
Size	p. 6349-6356.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021%2Facs.analchem.5b01220
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Article ; Online: Tag and Capture Flow Hydrogen Exchange Mass Spectrometry with a Fluorous-Immobilized Probe.

Marcsisin, Sean R / Liptak, Cary / Marineau, Jason / Bradner, James E / Engen, John R

Analytical chemistry

2015 Volume 87, Issue 12, Page(s) 6349–6356

Abstract: Analysis of complex mixtures of proteins by hydrogen exchange (HX) mass spectrometry (MS) is limited by one's ability to resolve the protein(s) of interest from the proteins that are not of interest. One strategy for overcoming this problem is to tag the ...

Abstract	Analysis of complex mixtures of proteins by hydrogen exchange (HX) mass spectrometry (MS) is limited by one's ability to resolve the protein(s) of interest from the proteins that are not of interest. One strategy for overcoming this problem is to tag the target protein(s) to allow for rapid removal from the mixture for subsequent analysis. Here we illustrate a new solution involving fluorous conjugation of a retrievable probe. The appended fluorous tag allows for facile immobilization on a fluorous surface. When a target protein is passed over the immobilized probe molecule, it can be efficiently captured and then exposed to a flowing stream of deuterated buffer for hydrogen exchange. The utility of this method is illustrated for a model system of the Elongin BC protein complex bound to a peptide from HIV Vif. Efficient capture is demonstrated, and deuteration when immobilized was identical to deuteration in conventional solution-phase hydrogen exchange MS. Protein captured from a crude bacterial cell lysate could also be deuterated without the need for separate purification steps before HX MS. The advantages and disadvantages of the method are discussed in light of miniaturization and automation.
MeSH term(s)	Fluorocarbons/chemistry ; Hydrocarbons, Fluorinated ; Hydrogen/chemistry ; Mass Spectrometry ; Molecular Probe Techniques ; Proteins/analysis ; Solutions
Chemical Substances	Fluorocarbons ; Hydrocarbons, Fluorinated ; Proteins ; Solutions ; Hydrogen (7YNJ3PO35Z)
Language	English
Publishing date	2015-05-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1508-8
ISSN	1520-6882 ; 0003-2700
ISSN (online)	1520-6882
ISSN	0003-2700
DOI	10.1021/acs.analchem.5b01220
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Article ; Online: Comparison of Anti-Xa Activity in Patients Receiving Apixaban or Rivaroxaban.

Bookstaver, David A / Sparks, Kimberly / Pybus, Brandon S / Davis, Dustin K / Marcsisin, Sean R / Sousa, Jason C

The Annals of pharmacotherapy

2017 Volume 52, Issue 3, Page(s) 251–256

Abstract: ... and rivaroxaban. Linear correlation between serum levels and anti-Xa activity has been shown, with r ... The study enrolled 88 patients receiving each drug. The r: Conclusions: Good correlation was shown ...

Abstract	Background: There is no established method for monitoring the anticoagulant effects of apixaban and rivaroxaban. Linear correlation between serum levels and anti-Xa activity has been shown, with r Objective: To evaluate the anti-Xa activity and serum levels at those doses and compare the trough anti-Xa activity. Methods: This was a single-center prospective study,approved by the institutional review board. Patients on an inappropriate dose or receiving an interacting drug were excluded. Blood samples were drawn 0.5 to 3 hours before a dose for both agents, 2 to 3 hours after an apixaban dose, and 12 to 16 hours after a rivaroxaban dose. Anti-Xa activity and serum levels were determined, and correlation was done via regression analysis. Trough anti-Xa activity was compared using a t-test. Results: The study enrolled 88 patients receiving each drug. The r Conclusions: Good correlation was shown between anti-Xa activity and serum levels. The clinical utility of monitoring anti-Xa activity and the significance of the difference in trough anti-Xa activity for these agents remains to be established.
MeSH term(s)	Aged ; Factor Xa/analysis ; Factor Xa Inhibitors/blood ; Factor Xa Inhibitors/pharmacokinetics ; Factor Xa Inhibitors/therapeutic use ; Female ; Humans ; Male ; Middle Aged ; Pyrazoles/blood ; Pyrazoles/pharmacokinetics ; Pyrazoles/therapeutic use ; Pyridones/blood ; Pyridones/pharmacokinetics ; Pyridones/therapeutic use ; Rivaroxaban/blood ; Rivaroxaban/pharmacokinetics ; Rivaroxaban/therapeutic use
Chemical Substances	Factor Xa Inhibitors ; Pyrazoles ; Pyridones ; apixaban (3Z9Y7UWC1J) ; Rivaroxaban (9NDF7JZ4M3) ; Factor Xa (EC 3.4.21.6)
Language	English
Publishing date	2017-10-19
Publishing country	United States
Document type	Clinical Trial ; Journal Article
ZDB-ID	1101370-9
ISSN	1542-6270 ; 1060-0280
ISSN (online)	1542-6270
ISSN	1060-0280
DOI	10.1177/1060028017738262
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Article: Hydrogen exchange mass spectrometry: what is it and what can it tell us

Marcsisin, Sean R / Engen, John R

Analytical and bioanalytical chemistry. 2010 June, v. 397, no. 3

2010

Abstract	Proteins are undoubtedly some of the most essential molecules of life. While much is known about many proteins, some aspects still remain mysterious. One particularly important aspect of understanding proteins is determining how structure helps dictate function. Continued development and implementation of biophysical techniques that provide information about protein conformation and dynamics is essential. In this review, we discuss hydrogen exchange mass spectrometry and how this method can be used to learn about protein conformation and dynamics. The basic concepts of the method are described, the workflow illustrated, and a few examples of its application are provided. [graphic removed]
Keywords	deuterium ; protein conformation
Language	English
Dates of publication	2010-06
Size	p. 967-972.
Publisher	Springer-Verlag
Publishing place	Berlin/Heidelberg
Document type	Article
ISSN	1618-2642
DOI	10.1007/s00216-010-3556-4
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Article ; Online: Developmental differences in stress responding after repeated underwater trauma exposures in rats.

Altman, Daniel E / Simmons, Laurence P / Vuong, Chau T / Taylor, Rachel M / Sousa, Jason C / Marcsisin, Sean R / Zottig, Victor E / Moore, Nicole L T

Stress (Amsterdam, Netherlands)

2018 Volume 21, Issue 3, Page(s) 267–273

Abstract: Adolescence is a distinct developmental period characterized by behavioral and physiological maturation. Rapid ongoing changes during neurodevelopment in particular present potential opportunities for stress to have lasting effects on longitudinal ... ...

Abstract	Adolescence is a distinct developmental period characterized by behavioral and physiological maturation. Rapid ongoing changes during neurodevelopment in particular present potential opportunities for stress to have lasting effects on longitudinal outcomes of behavioral and neuroendocrine function. While adult stress effects on outcomes during adulthood have been characterized, little is known about the lasting effects of adolescent repeated stressor exposure on outcomes during adolescence. We have previously reported different stress responses in adolescent rats relative to adult rats, including a blunted fear response outcome in adulthood in rats stressed during adolescence. The present study characterized the ontogeny of behavioral and neuroendocrine responses to eight underwater trauma (UWT) exposures in rats over a two week poststress time period during adolescence (P34) or adulthood (P83) relative to age-matched control groups that underwent eight swimming episodes without UWT. Repeated UWT exposures starting in adolescence, but not adulthood, resulted in adverse behavioral responses on the elevated plus maze 1 day post-stress. Corticosterone responses did not differ between UWT-exposed and controls for either age group at 1 day or at 7 days poststress, although there was an effect of age on corticosterone levels. We conclude that repeated UWT stress events have a lasting, negative behavioral effect on adolescent rats that is not observed in adult rats after the two-week exposure window. These results suggest that neurophysiological mechanisms underlying recovery from a repeated stressor are immature in adolescence relative to adulthood in rats.
MeSH term(s)	Aging/psychology ; Animals ; Anxiety/psychology ; Behavior, Animal ; Corticosterone/blood ; Exploratory Behavior ; Immersion/physiopathology ; Rats ; Rats, Sprague-Dawley ; Reflex, Startle ; Stress, Psychological/psychology ; Swimming/psychology ; Water ; Wounds and Injuries/physiopathology
Chemical Substances	Water (059QF0KO0R) ; Corticosterone (W980KJ009P)
Language	English
Publishing date	2018-02-16
Publishing country	England
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1387706-9
ISSN	1607-8888 ; 1025-3890
ISSN (online)	1607-8888
ISSN	1025-3890
DOI	10.1080/10253890.2018.1439012
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Article ; Online: Corrigendum to: Determination of Cytochrome P450 Isoenzyme 2D6 (CYP2D6) Genotypes and Pharmacogenomic Impact on Primaquine Metabolism in an Active-Duty US Military Population.

The Journal of infectious diseases

2019 Volume 221, Issue 7, Page(s) 1204

Language	English
Publishing date	2019-11-26
Publishing country	United States
Document type	Journal Article ; Published Erratum
ZDB-ID	3019-3
ISSN	1537-6613 ; 0022-1899
ISSN (online)	1537-6613
ISSN	0022-1899
DOI	10.1093/infdis/jiz599
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Article ; Online: Structures of PGAM5 Provide Insight into Active Site Plasticity and Multimeric Assembly.

Chaikuad, Apirat / Filippakopoulos, Panagis / Marcsisin, Sean R / Picaud, Sarah / Schröder, Martin / Sekine, Shiori / Ichijo, Hidenori / Engen, John R / Takeda, Kohsuke / Knapp, Stefan

Structure (London, England : 1993)

2017 Volume 25, Issue 7, Page(s) 1089–1099.e3

Abstract: PGAM5 is a mitochondrial membrane protein that functions as an atypical Ser/Thr phosphatase and is a regulator of oxidative stress response, necroptosis, and autophagy. Here we present several crystal structures of PGAM5 including the activating N- ... ...

Abstract	PGAM5 is a mitochondrial membrane protein that functions as an atypical Ser/Thr phosphatase and is a regulator of oxidative stress response, necroptosis, and autophagy. Here we present several crystal structures of PGAM5 including the activating N-terminal regulatory sequences, providing a model for structural plasticity, dimerization of the catalytic domain, and the assembly into an enzymatically active dodecameric form. Oligomeric states observed in structures were supported by hydrogen exchange mass spectrometry, size-exclusion chromatography, and analytical ultracentrifugation experiments in solution. We report that the catalytically important N-terminal WDPNWD motif acts as a structural integrator assembling PGAM5 into a dodecamer, allosterically activating the phosphatase by promoting an ordering of the catalytic loop. Additionally the observed active site plasticity enabled visualization of essential conformational rearrangements of catalytic elements. The comprehensive biophysical characterization offers detailed structural models of this key mitochondrial phosphatase that has been associated with the development of diverse diseases.
MeSH term(s)	Allosteric Regulation ; Allosteric Site ; Catalytic Domain ; HEK293 Cells ; Humans ; Mitochondrial Proteins/chemistry ; Mitochondrial Proteins/metabolism ; Molecular Dynamics Simulation ; Phosphoprotein Phosphatases/chemistry ; Phosphoprotein Phosphatases/metabolism ; Protein Multimerization
Chemical Substances	Mitochondrial Proteins ; PGAM5 protein, human (EC 3.1.3.16) ; Phosphoprotein Phosphatases (EC 3.1.3.16)
Language	English
Publishing date	2017-06-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2017.05.020
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