Introducing Our Authors pubs.acs.org/acschemicalbiology
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PHI DOAN
Education: University of Balamand, Beirut, Lebanon, B.Sc. in Medical Laboratory Sciences, 2011; University of Central Lancashire, Preston, United Kingdom, MSc. in Cancer Biology and Therapy, 2013, Advisor: Prof Timothy J. Snape Current Position: Ph.D. candidate in Chemical Biology and Drug Discovery at the European Molecular Biology Laboratory in Heidelberg, Germany, Advisor: Dr Maja Köhn Nonscientific Interests: Climbing, creative writing, and philosophy Despite their notable role in promoting cancer formation and progression, the phosphatases of regenerating liver (PRL-1, PRL2, and PRL-3) remain insufficiently characterized in terms of their substrates and mechanisms. One of these phosphatases, PRL-3, which promotes cancer metastasis formation, is barely understood yet remains an attractive target for tool and drug development. My graduate research consists of investigating the roles of metastasis-promoting phosphatase PRL-3 by designing inhibitors for PRL-3 to help study its mechanisms and roles and to address its targetability for future therapy. This represents an example of the recent applicable tools emphasized in this review, which assists in tackling phosphatase research. (Read Fahs’ article DOI: 10.1021/acschembio.6b00570.)
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Education: University of Minnesota, B.S. Chemistry, Advisor: Prof. Valerie Pierre, 2012 Current Position: University of Michigan, Ph.D. Chemistry, Advisor: Prof. Theodore Goodson III, 2016 Nonscientific Interests: Snowboarding, football, wine, television, and movies One major aspect of my Ph.D. research focused on investigating the DNA-binding interactions of small molecules by employing ultrafast nonlinear spectroscopy. It is important to understand the DNA-binding mechanism of small molecules, including drugs, because their selectivity and performance are dependent on this property. We developed a methodology to differentiate between the DNA-binding modes (intercalation vs groove binding) utilizing two-photon spectroscopy. This technique offers advantages as it can be applied at biologically relevant conditions and allows for unambiguous interpretation contrarily to traditional methods. In this report, we implemented our newly developed methodology as well as ultrafast timeresolved spectroscopy to examine the DNA-binding mechanism of a series of novel small molecules that possess a crescentshaped structural motif. Our results reveal that the DNA-binding mechanism can be tailored by structurally modifying the electron acceptor properties of the central heterocyclic core. We hope this new design strategy will be used in the development of small molecules aimed at DNA, such as DNA-targeted therapies. (Read Doan’s article DOI: 10.1021/acschembio.6b00448.)
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PABLO LUJAN MIRALLES
Image courtesy of Marietta Schupp
Education: Valencia University, Spain, B.S. in Biochemistry, 2011 and M.S. in Molecular Approach in Medicine, 2012, Advisor: Dr. Pascual Sanz (Instituto de Biomedicina de Valencia, CSIC, ́ Spain); Centro de Investigación Principe Felipe, Spain, Research Assistant in Dr. Enrique Pérez-Payá’s lab, 2012−2013 Current Position: European Molecular Biology Laboratory (EMBL), Heidelberg, Germany, Ph.D. student in Dr. Maja Köhn’s lab since July 2013 Nonscientific Interests: Film critic at www.videodromo.es Since my current graduate research is focused on the discovery of new substrates for specific phosphatases, I have realized how important it is to be aware of the newest tools developed to investigate a phosphatase. Unfortunately, studying phosphatases is very challenging, as they are not as thoroughly studied as their partners, the kinases; so the available tools were aging, restricted,
SARA FAHS
Published: November 18, 2016
Image courtesy of Marietta Schupp
© 2016 American Chemical Society
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DOI: 10.1021/acschembio.6b00951 ACS Chem. Biol. 2016, 11, 2938−2939
ACS Chemical Biology
Introducing Our Authors
and unspecific. However, in recent years, a range of specialized technologies has been developed to overcome the challenges that phosphatase research presents, but there was still the demand of bringing them all together. In our manuscript, we highlight general questions concerning phosphatases and which are the applicable tools to study them as a guide for both the inexperienced and the experienced phosphatase researcher. (Read Lujan’s article DOI: 10.1021/acschembio.6b00570.)
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Education: B.S. in Biochemistry from the University of Notre Dame in 2006 with a minor in Theology; Ph.D. from Texas A&M UniversityCollege Station in 2015 from the Department of Biochemistry and Biophysics; Research advisor: Professor David Barondeau Current Position: National Research Council Fellow in the lab of Dr. Igor Medintz at the U.S. Naval Research Laboratory Nonscientific Interests: Roman Catholicism, playing with my three boys, spending time with my wife, and triathlons My scientific interests encompass understanding and improving complex metabolic pathways that involve numerous proteins and substrates. In my Ph.D., I developed a new fluorescent approach to monitoring the biosynthesis and transfer of iron− sulfur clusters in in vitro reactions. My current work involves trying to harness the power of enzymatic catalysis to produce immobilized enzyme cascades on nanoparticle surfaces. In this current work, we present our efforts to utilize our new fluorescent assay to elucidate the mechanistic details of a complex Fe−S cluster transfer pathway. By coupling the results with global fit modeling, we develop a kinetic model of the pathway. In doing so, we demonstrate that this approach can uniquely probe reactions containing the numerous components of the Fe−S cluster synthesis pathway. (Read Vranish’s article DOI: 10.1021/ acschembio.6b00632.)
ALESSANDRO PANATTONI
Image courtesy of Nemanja Milisavljević
Education: Università di Pisa, Italy, BSc in Chemistry, (supervisor Prof. Adriano Carpita), 2011; Università di Pisa, Italy, MScspecialization in Organic Chemistry (supervisor Prof. Fabio Bellina), 2014 Current Position: Ph.D. student under the supervision of Prof. Michal Hocek at the Institute of Organic Chemistry and Biochemistry, Prague, Czech Republic Nonscientific Interests: Basketball, climbing, fishing, music, reading, and wine tasting Polymerase synthesis of base-modified nucleic acids using functionalized nucleoside triphosphates as substrates gains growing attention and is widely used for the preparation of nucleic acid probes for diagnostics and chemical biology. In this paper, we present a comprehensive study of competitive incorporations using basemodified 2′-deoxyribonucleoside triphosphates in the presence of their natural counterparts (dNTPs). We found that some modified dNRTPs (especially 7-deazapurine dNTPs bearing π-electroncontaining modifications at position 7) were better substrates for DNA polymerases than the corresponding natural dNTPs. These findings are important for better understanding the mechanism of incorporation of modified dNTPs by DNA polymerases, as well as for the prospective in vivo synthesis of base-modified DNA. (Read Panattoni’s article DOI: 10.1021/acschembio.6b00714.)
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JAMES VRANISH
Image courtesy of Colleen Vranish
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DOI: 10.1021/acschembio.6b00951 ACS Chem. Biol. 2016, 11, 2938−2939
