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■ GIULIA AGNELLO
Image courtesy of Candice Lamb.
Current position: Graduate Research Assistant, Institute for
Cell and Molecular Biology, University of Texas at Austin;
Research Advisor: George Georgiou.Education: M.S. in Industrial and Molecular Biotechnology,
University of Bologna (Italy); Research Advisors: Laura Segatori
at Rice University and Antonio Contestabile at University of
Bologna. B.S. in Biotechnology, University of Palermo (Italy);
Research Advisor: Gregorio Seidita.Nonscientific interests: Traveling, cooking, swimming, swing
dancing.My primary research interest is to study the pathogenesis of
human diseases and develop novel therapeutic approaches.
The focus of my graduate studies is the engineering and
characterization of human enzymes for therapeutic applica-
tions. In this work, we report the identification and validation
of a substrate selectivity motif within enzymes of the aspar-
tate aminotransferase fold type I superfamily (AAT_I).
The AAT_I enzyme Cysteine Sulfinic Acid Decarboxylase
(CSAD) catalyzes the synthesis of taurine, a key chemical in
mammalians physiology long thought to exist only in
eukaryotes. To our surprise, we found that marine bacteria
expressing genes with the motif associated with CSAD
activity synthesize taurine in vivo. This study provides
evidence for fundamental biochemistry and applied research,
and reveals the unexpected and intriguing finding that
prokaryotes can also synthesize taurine. (Read Agnello’s
article, DOI: 10.1021/cb400335k)
■ STIJN APER
Image courtesy of Rien Meulman.
Current position: Ph.D. student at Eindhoven University ofTechnology in the Department of Biomedical Engineering;Advisor: Dr. M. Merkx.Education: Eindhoven University of Technology, B.S.
Biomedical Engineering, 2009; Eindhoven University ofTechnology, M.S. Biomedical Engineering, 2012.Nonscientific interests: Music, tennis, race cycling.The new antibody sensor approach described in our paper was the
topic of my master research project. In addition to its easy read-outand low limit of detection, themain appeal forme is themodularity ofthe sensor design. Inmy current Ph.D. project I use a similar, syntheticbiology type of approach to develop modular protein switches tointerfere with intracellular Zn2+ homeostasis and signaling. This kindof research requires one to have a detailed understanding of proteinfolding and the way proteins interact with each other. On the otherhand, I appreciate that our workmay find direct applications, either inthe development of low cost point-of-care diagnostic assays or forunraveling the molecular mechanisms behind complex cellularbehavior. (Read Aper’s article, DOI: 10.1021/cb400406x)
■ SAMBASHIVA BANALA
Image courtesy of Sambashiva Banala.
Published: October 18, 2013
Introducing Our Authors
pubs.acs.org/acschemicalbiology
© 2013 American Chemical Society 2103 dx.doi.org/10.1021/cb400746g | ACS Chem. Biol. 2013, 8, 2103−2107
Current position: Postdoctoral researcher with Dr. Luke Lavis,Janelia Farm Research Campus, Howard Hughes MedicalInstitute, USA.Education: Indian Institute of Technology, Roorkee, India,
M.Sc in Chemistry, 2004; Ecole Polytechnique Federale deLausanne, Switzerland, Ph.D. with Prof. Kai Johnsson, 2010;Eindhoven University of Technology, Netherlands, postdoctoralresearcher with Prof. Maarten Merkx, 2010−2012.Nonscientific interests: Reading history and scientific news
and books, melodious music, comedy and philosophical movies.I am interested in developing new chemical and biological
tools for visualizing cellular events and the detection of metalions and biomolecules. During my Ph.D. with Prof. Kai Johnsson,a truly interdisciplinary laboratory with expertise in chemistryand biology, I developed several photoactivatable probes forSNAP-tag labeling. The chemical biology atmosphere in the labinspired me to acquire knowledge in molecular biology andprotein engineering. I therefore joined in the laboratory of Prof.Maarten Merkx for my postdoctoral research, whose the grouphas extensive experience in and the development of protein-based sensors. In our article, we describe a novel method toconstruct reporter enzymes that allow simple colorimetricdetection of antibodies directly in solution. This approach isgenerally applicable as was demonstrated by constructingreporter enzymes for three different antibodies. (Read Banala’sarticle, DOI: 10.1021/cb400406x)
■ KENNETH D. CLEVENGER
Image courtesy of Sarah Sheldrick.
Education: Butler University, B.S. Chemistry, 2008; ResearchAdvisor: Geoffrey Hoops; The University of Texas in Austin,Doctoral Candidate in Biochemistry; Research Advisor: WalterFast.Nonscientific interests: Guitar, pro basketball, running, folk
music and classic rock.New strategies are needed to deal with the mounting crisis of
antibiotic resistance. Our paper reports the discovery of a boronicacid inhibitor with picomolar affinity for the Pseudomonasaeruginosa siderophore biosynthetic enzyme PvdQ. We alsodemonstrate the inhibitor’s power to recapitulate the growthphenotype of a pvdQ knockout in iron limited media,representing a potential starting point for development ofmore drug-like molecules against this target as well as a potentialprobe for elucidating the biology of PvdQ. Recent advances inblocking siderophore production support this approach as anattractive antibiotic strategy and here we introduce a covalent,
reversible, boron-based inhibitor to further these efforts. (ReadClevenger’s article, DOI: 10.1021/cb400345h)
■ KARRERA Y. DJOKO
Image courtesy of Karrera Y. Djoko.
Current position: Postdoctoral research associate with Prof.A.G. McEwan at the University of Queensland, Australia.Education: B.S. in Chemistry, PennState, 2004; Ph.D. in
Chemistry, U of Melbourne, 2009 with Prof. A. G. Wedd.Nonscientific interests: Classical music, Broadway musicals,
and chocolates.Copper (Cu) is a vital redox cofactor for bacteria, but an excess
is very toxic. After studying mechanisms of bacterial toleranceagainst Cu surplus, I became interested in the more fundamentalquestion of how Cu really exerts its antimicrobial effects. In thismanuscript, I showed that Cu arrests biosynthesis of another keyredox cofactor for life, heme. This has striking consequences forthe bacterium − the loss of heme interrupts respiration andrenders it defenseless against additional stresses (see Infect.Immun. DOI: 10.1128/IAI.06163-11). Given the continuing risein strains that are resistant to conventional antibiotics, I amexploring the potential for Cu as a new treatment for bacterialinfections, together with Prof. McEwan. I look forward to ournew adventures in this exciting field of chemical biology. (ReadDjoko’s article, DOI: 10.1021/cb4002443)
■ JEANE GOVAN
Image courtesy of Jie Zhang.
Current position: Postdoctoral Fellow at The University ofTexas MD Anderson Cancer Center under the direction of Prof.Shiaw-Yih Lin.
ACS Chemical Biology Introducing Our Authors
dx.doi.org/10.1021/cb400746g | ACS Chem. Biol. 2013, 8, 2103−21072104
Education: Ph.D. in Chemistry at North Carolina StateUniversity, Raleigh, North Carolina; Advisor: Prof. AlexanderDeiters. B.A. in Chemistry and Biology at Kalamazoo College,Kalamazoo, Michigan; Advisor: Prof. Laura Lowe Furge.Nonscientific interests: Scuba diving, zumba, baking, and
reading.My graduate research encompassed the development of
photochemical tools for the regulation of gene expression.Gene function is naturally controlled in a high spatial andtemporal manner. Therefore, to investigate and to re-engineerthese processes, the same level of spatiotemporal regulationfound in nature needs to be achieved. Toward this goal, I use lightas an external trigger to regulate gene function, as light irradiationis easily controlled in timing, location, and amplitude, thusenabling the precise activation of biological function. In thisstudy, I have applied this concept to the light-regulation ofantisense agents in conjunction with the conjugation of a cellpenetrating peptide to simultaneously achieve light-activationand delivery of the antisense agent into mammalian cell. (ReadGovan’s article, DOI: 10.1021/cb400293e)
■ MALGORZATA (GOSIA) KORBAS
Image courtesy of Malgorzata Korbas.
Current position: Staff Scientist for the BioXAS (BiologicalX-ray Absorption Spectroscopy) Facility at the Canadian LightSource (Saskatoon, Canada).Education: Jagiellonian University, Krakow, Poland, M.Sc.
and Ph.D. in Medical Physics.Nonscientific interests: Photography, reading, family road
trips, and pilates.My research interests focus on understanding how metals and
metalloids interact with biological systems. I am specificallyinterested in metals that pose environmental and human healthrisks such as mercury. In my research, I use synchrotron-basedimaging and chemical speciation techniques to study moleculartoxicology of methylmercury and selenium. In the present article,we have used high resolution X-ray fluorescence imaging todetermine the subcellular localization of mercury in the eye andthe pineal gland in zebrafish larvae exposed to methylmercurychloride. We have identified the outer segments of both retinaland pineal photoreceptors as the preferential sites formethylmercury accumulation. This new finding indicatesthat vision problems associated with methylmercury exposuremay have their roots not only in the brain but also in the sen-sory machinery in the eye. (Read Korbas’ article, DOI:10.1021/cb4004805)
■ FEIYANG LIU
Image courtesy of Feiyang Liu.
Current position: High Magnetic Field Laboratory, ChineseAcademy of Sciences, Ph.D. candidate with Prof. Qingsong Liu.Education: Anhui Medical University, B.S. Med in Pharmacy,
2008; China Pharmaceutical University, M.S. in IntegratedWestern and Chinese Medicine, 2011, with Prof. Hong Liao.Nonscientific interests: Traveling, movies, music, reading.My current research focuses on identifying synergistic drug
combinations using high throughput combinatorial screeningthat are efficacious against various intractable cancers. In thisstudy, we reported the discovery of a selective DDR1 inhibitor,DDR1-IN-1, which potently inhibits intracellular DDR1 kinaseactivity but only weakly inhibits the proliferation of cells thatpossess mutations in DDR1 kinase. This result suggests thatDDR1 inhibition by itself may be insufficient to block theproliferation of cancer cells in culture and may need to becombined with other agents. We employed a high throughputcombinatorial screening approach to discover that inhibitors ofPI3K and mTOR could potentiate the antiproliferative activity ofDDR1-IN-1 against colorectal cancer cell lines. Hopefully,DDR1-IN-1 will serve as a useful pharmacological probe ofDDR1-dependent biology as well as a means to establish thetherapeutic potential of DDR1 inhibition in the management ofcancer. (Read Liu’s article, DOI: 10.1021/cb400430t)
■ ELIZABETH I. PARKINSON
Image courtesy of Claire Knezevic.
Current position: Ph.D. student at the University of Illinois atUrbana−Champaign in the Department of Chemistry; Advisor:Prof. Paul J. Hergenrother.
ACS Chemical Biology Introducing Our Authors
dx.doi.org/10.1021/cb400746g | ACS Chem. Biol. 2013, 8, 2103−21072105
Education: Rhodes College, B.S. Chemistry, 2010; research atSt. Jude Children’s Research Hospital in the Department ofChemical Biology and Therapeutics with Dr. Philip M. Potter.Nonscientific interests: Yoga, running, baking, hiking, and
reading.My research focuses on deoxynyboquinone (DNQ) and its
potential as an anticancer therapy. DNQ was discovered in ahigh-throughput screen where it potently induced cancer celldeath. This death depended on reactive oxygen species (ROS)but the exact mechanism was unknown. I was part of the teamthat determined the mode of action of DNQ, reduction by theenzyme NQO1 to a hydroquinone that reduction−oxidationcycles, producing two moles of ROS per cycle (Cancer Res. DOI:10.1158/0008-5472.CAN-11-3135). We were excited by thisdiscovery because NQO1 is overexpressed in many solidtumors making it an excellent target. In the present article, wecompared DNQ to previously reported NQO1 substrates toexamine NQO1 bioactivation as an anticancer strategy.Additionally, DNQ derivatives were synthesized to furtherinvestigate the relationship between processing by NQO1 andanticancer activity. (Read Parkinson’s article, DOI: 10.1021/cb4005832)
■ DANIEL PASTOR-FLORES
Image courtesy of Daniel Pastor-Flores.
Current position: Ph.D. student in the laboratory of Dr. RicardoBiondi at the Frankfurt University Hospital, Frankfurt, Germany.Education:University of Zaragoza (Spain), Master in Cellular
and Molecular Biology, 2008; University of Zaragoza (Spain),Diploma in Biochemistry, 2006.Nonscientific interests: Mountain sports, photography, Jazz
music, enology.As a part of my Ph.D. research program, I spent one year in the
laboratory ofDr. AntonioCasamayor, at theAutonomousUniversityof Barcelona, learning yeast genetics. Then, I established a yeastlaboratory in Frankfurt and complemented my research withbiochemistry, crystallography and drug development method-ologies to study in depth organisms causing severe diseases suchas Candidiasis using a chemical biology approach. My Ph.D.thesis research led to identify the protein kinase Pkh fromCandida albicans, the ortholog of PDK1, as a potential drug targetfor antifungals. As part of the team I am also developing yeast-genetic tools to support the development of allosteric proteinkinase drugs to other human diseases. (Read Pastor-Flores’article, DOI: 10.1021/cb400452z)
■ FIONA ROWAN
Image courtesy of Mark Critchard.
Education: Cardiff University, U.K., B.Sc. Biochemistry, 2008;Imperial College, London, U.K., M.Res. Biochemical Research,2009; Institute of Cancer Research, London, U.K., Ph.D.candidate in Chemical and Structural Biology with RichardBayliss and Julian Blagg.Nonscientific interests: Cooking, traveling, running, and pub
quizzes.My research involves chemically engineering protein kinases
to modulate their structure and function. Kinases are implicatedas drug targets in many diseases, so it is really important tounderstand what ‘switches them on’. Activation of kinases isoften achieved through phosphorylation in a region known as theactivation loop. However, until now there had been no effectivemethod to permit site-specific control of kinase phosphorylation,making it difficult to study how modification at different sitesaffects activity. Our paper describes the use of a chemicallysynthesized phospho-mimic to selectively activate a kinase atspecific sites. This chemical modification was superior to existinggenetic phospho-mimic techniques; we were able to probe therole of phosphorylation at two adjacent sites, revealing a novelmechanism to regulate kinase activity. (Read Rowan’s article,DOI: 10.1021/cb400425t)
■ MERYL THOMAS
Image courtesy of Marie Thomas.
Current position: Fourth year graduate student in chemistry atNorth Carolina State University under the direction of Prof.Alexander Deiters.
ACS Chemical Biology Introducing Our Authors
dx.doi.org/10.1021/cb400746g | ACS Chem. Biol. 2013, 8, 2103−21072106
Education: B.S. and M.S. in Chemistry and processengineering at ESCPE Lyon (Lyon School of Chemistry, Physicsand Electronics), France.Nonscientific interests: Outdoor activities like biking and
hiking, water sports, reading, cooking. and traveling.In our group, we are interested in developing small organic
molecules as tools to study specific biological pathways,specifically those that have been associated with human diseases.Within my research, I am particularly interested in developingsmall molecules to inhibit the function of specific, endogenousoligonucleotides, most importantly microRNAs, as theirderegulation has been linked with various diseases, such ascancer and hepatitis C infection. These small molecule inhibitorsconstitute novel probes to investigate the implication of specificmicroRNAs in the development of diverse cancers. The approachthat was taken in this paper was the conjugation of a smallmolecule-targeting group to a light-activated antisense agent inorder to enable selective delivery of the reagent into cancer cells.(Read Thomas’ article, DOI: 10.1021/cb400293e)
■ XANDER VAN WIJK
Image courtesy of Theo Hafmans.
Current position: Postdoctoral Scholar in the laboratory of Prof.Jeffrey Esko at the University of California, San Diego.Education: Maastricht University, The Netherlands, B.Sc. in
Molecular Life Sciences, 2006; Hasselt University, Belgium,M.Sc. in Biomedical Sciences, 2007; Radboud UniversityNijmegen, The Netherlands, Ph.D. in Medical Sciences, 2013;Advisor: Toin van Kuppevelt.Nonscientific interests: Soccer, softball, scuba-diving,
snowboarding, traveling.My research focuses on the long polysaccharide heparan
sulfate. This glycan regulates many physiological and patho-logical processes and is an interesting therapeutic target. Forexample, heparan sulfate promotes (tumor) angiogenesis byacting as a coreceptor for FGF2 and VEGF. However, few drugsexist that target this glycan. In this paper, we describe a sugaranalogue that strongly inhibits heparan sulfate biosynthesis invitro and in vivo, and show that treatment with this analogueinhibits FGF2 and VEGF signaling and angiogenesis. In addition,we studied the analogue’s metabolic fate. Unexpectedly, the sugaranalogue is not incorporated into heparan sulfate. The mainworking mechanism likely involves the abundant UDP activationof the analogue thereby reducing the activation of the biologicalsugar. (Read van Wijk’s article, DOI: 10.1021/cb4004332)
ACS Chemical Biology Introducing Our Authors
dx.doi.org/10.1021/cb400746g | ACS Chem. Biol. 2013, 8, 2103−21072107