■ KATIE ALDRED

Image courtesy of Ashley Williams.

Current position: Ph.D. candidate, Dept. of Biochemistry,Vanderbilt University, Research Advisor: Dr. Neil OsheroffEducation: University of Evansville, B.S. in Biology, 2009,

Research Advisor: Dr. Brian ErnstingNonscientific interests: Outdoor activities, especially hiking;

traveling, especially abroad to experience different cultures andvisit historic sites; sports; drawing, painting, and scrapbookingMy current research focuses on studying quinolone interactions

with type II topoisomerases. Specificmutations in the bacterial typeII enzymes are the primary cause of quinolone resistance seen inclinical isolates. We believe that by understanding mechanisms ofquinolone action and resistance, we can design new quinolone-based drugs that overcome resistance in the bacterial enzymeswithout having cross reactivity with the human enzymes. In thepresent article, we determined why quinolones currently in clinicaluse do not have activity against human type II topoisomerases andthe roles of various substituents on the quinolone core inmediatinginteractions and activity with the bacterial and human enzymes andshow that resistance can be overcome without producing humancross reactivity. (Read Aldred’s article, DOI: 10.1021/cb400592n)

■ DAVID CARLSON

Image courtesy of David Carlson.

Current position: Post Doc, Duke University, Department ofPharmacology and Cancer Biology, Research Advisor: TimothyA. J. Haystead

Education: Duke University, Department of Chemistry,Ph.D., 2010, Research Advisor: Eric J. Toone; Allegheny College,B.S. Chemistry, 1999, Research Advisor: S. Shaun MurphreeNonscientific interests: Surfing, cooking, trying to be the best

at exercisingWe are focused on the discovery of therapeutic agents for the

treatment of human diseases whose onset and progression aredependent on ATP utilizing enzymes. The activity of thesepurine utilizing enzymes (i.e., the purinome) can be modulatedby small molecule inhibitors. In order to rapidly identify inhibitorsfor any element of the purinome, we have developed afluorescence linked enzyme chemoproteomic strategy (FLECS).FLECS was used to identify a potent, selective, and ATP-competitive inhibitor (HS38) of DAPK1 and ZIPK. DAPK1 andZIPK are serine/threonine kinases that regulate programmed celldeath and phosphorylation of smooth muscle myosin. HS38serves as a lead scaffold for therapeutics that will be used to treatsmooth muscle disorders and to attenuate programmed cell deathin ischemia-reperfusion induced tissue injuries. (Read Carlson’sarticle, DOI: 10.1021/cb400407c)

■ MICHAEL CUCCARESE

Image courtesy of Amit Singh.

Current position: Graduate research assistant, O’Dohertygroup, Northeastern UniversityEducation: The Ohio State University, B.S. Chemistry, 2008

(research in the laboratories of Jon Parquette); NortheasternUniversity, Ph.D., in progress, O’Doherty labNonscientific interests: Photography, hikingMy current research is at the intersection of organic chemistry

and molecular biology. My synthetic interests include a bi-directional glycosylation approach to novel aminoglycosidesand the synthesis of tethered digitoxin analogues. My molecularbiology interests involve the ability of aminoglycosides tosensitize cancer cells to apoptosis and the signaling pathwaysinvolved in this phenomenon. (Read Cuccarese’s article, DOI:10.1021/cb4007024)

Published: December 20, 2013

Introducing Our Authors

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© 2013 American Chemical Society 2597 dx.doi.org/10.1021/cb400862m | ACS Chem. Biol. 2013, 8, 2597−2600

■ YOUJUN FENG

Image courtesy of Youjun Feng.

Current position: Research Scientist at Department of Micro-biology, University of Illinois at Urbana−Champaign (UIUC),Urbana, IL 61801, USA.Education: Institute of Microbiology, Chinese Academy of

Sciences (CAS), Beijing, China, Ph.D. in Microbiology, 2007,(Supervisor: George FGao); College of Life Science&Technology,Guangxi University, Nanning, China, M.S. in Microbiology, 2004,(Supervisor: BaoshanChen);College of Life Science&Technology,Shaanxi University of Science &Technology (Northwest Universityof Light Industry), Xianyang, China, B.Sc. in Biotechnology, 2001Nonscientific interests: Fishing,music,movies, running, cookingMy research focuses on (1) molecular mechanisms for

infections of zoonotic pathogens, such as Streptococcus suis, anemerging/reemerging infectious agent, and (2) mechanism andregulation of bacterial fatty acid (and/or its two derivative vitaminsbiotin and lipoic acid) metabolism, a promising/effectiveantibacterial drug target. In this study, we are first to discover anovel enzyme CadD from human pathogen Leptospira interrogansthat catalyzes the deamination reaction of the universal secondmessenger cyclic-3′, 5′-adenosine monophosphate (cAMP). Weelucidated that expression of CadD in Escherichia coli mimics theloss of adenylate cyclase in that it blocks growth on carbon sourcesthat require the cAMP-CRP transcriptional activator complex forexpression of the cognate genes. Transcriptional analyses indicatethat CadD expression represses transcription of several cAMP-CRP dependent genes. Our finding supplements a new activity tothe cAMP metabolic network, and this CadD enzyme might beuseful in the intracellular study of cAMP-dependent processes.(Read Fengs’s article, DOI: 10.1021/cb4004628)

■ MONICA GATTI

Image courtesy of Monica Gatti.

Current position: Post Doc (Tullio Florio’s lab), Universityof Genova, Sect. of Pharmacology, Department of InternalMedicine, since November 2010Education: University of Genova, Degree in Medical and

Pharmaceutical Biotechnology (magna cum laude), 2006.Advisor: Prof. Tullio Florio; University of Genova, Ph.D. inExperimental Neuroscience, 2010Nonscientific interests: Dancing, traveling, photographyAll my research activity has been devoted to the study of

the intracellular second messenger systems involved in theproliferation and migration of tumor cells and their possiblepharmacological modulation. Initially, I contributed to the identifi-cation and characterization of the specific intracellular pathwaysactivated in vitro and in vivo by individual somatostatin-receptorsubtypes (MAPK, PI3K/Akt, phospho-tyrosine-phosphatases) indifferent human tumor models. Subsequently, I dealt with therole of CXCL12 and CXCR4 in the transactivation of EGFR asmechanisms to translate estrogen-dependent proliferation inbreast cancer cells and the antiproliferative effects induced byEGFR tyrosine kinase inhibitors. More recently, I partici-pated in studies concerning the expression of the chemokineCXCL12 and its receptors, CXCR4/CXCR7, in human braintumors (glioblastoma, meningioma, pituitary adenoma) ontissues, primary cultures and cell lines, the characterization ofthis chemokinergic system in cell proliferation and migration, andthe identification of involved transduction pathways (intracellularcalcium homeostasis, MAPK, and PI3K/Akt). Currently, I amworking on the characterization of the role of CXCR4/CXCR7 inhuman glioblastoma stem cells, focusing on the identification ofnovel antiproliferative dugs. (Read Gatti’s article, DOI: 10.1021/cb400521b)

■ SANJAY HARI

Image courtesy of Joe Lewis.

Education: Ohio State University, B.S. in Biochemistry, 2008;University of Washington, Ph.D. in chemistry, 2013, Advisor:Dustin MalyNonscientific interests: Reading, tennis, progressive rockMy graduate work has focused on the structural and functional

effects of small molecule inhibitors on protein kinases. Ligandssuch as imatinib stabilize discrete, catalytically inactive kinaseconformations; imatinib is also very selective for the kinase Ablover closely related kinases such as Src. In this paper, we analyzea number of other kinase inhibitors and reveal a correlative linkbetween Abl/Src selectivity, activation loop phosphorylationsensitivity, and sensitivity to clinically relevant mutations in theglycine-rich p-loop. We are excited about the contribution of

ACS Chemical Biology Introducing Our Authors

dx.doi.org/10.1021/cb400862m | ACS Chem. Biol. 2013, 8, 2597−26002598

this work to our understanding of kinase inhibitor potency andselectivity. (Read Hari’s article, DOI: 10.1021/cb400663k)

■ JEFFREY RUDOLF

Image courtesy of Jeffrey Rudolf.

Current position: The Scripps Research Institute, ScrippsFlorida, Postdoctoral Research Associate, Advisor: Ben ShenEducation: Walla Walla University, B.S. in Biochemistry,

2007; University of Utah, Ph.D. in Chemistry, 2013, Advisor:C. Dale PoulterNonscientific interests: Soccer, snowboarding, classical piano,

readingMy Ph.D. research focused on characterizing the remarkable

plasticity of two ABBA aromatic prenyltransferases, dimethy-lallyltryptophan synthase (4-DMATS), and dimethylallyltyro-sine synthase (SirD). We used aromatic substrate analogues tomanipulate the binding, orientation, and electronic interactionsof the substrate with the active site. We found that substituentsize, placement, and electronic effects determine the positionand type of prenylation. In this study, we show that theO-prenyltransferase, SirD, catalyzes S-prenylation of 4-mercap-tophenylalanine and normal and reverse prenylation at threepositions of the indole ring on tryptophan and tryptophanderivatives. My current research focuses on the identificationand characterization of diterpene natural products and the geneclusters responsible for their biosynthesis in Streptomyces. (ReadRudolf’s article, DOI: 10.1021/cb400691z)

■ HEIDI A SCHWANZ

Image courtesy of Heidi Schwanz.

Current position: NIH-sponsored postdoctoral fellow inDepartment of Physiology and Biophysics at the Whitaker

Cardiovascular Institute, Boston University School of Medicine,Research Advisor: James A. Hamilton.Education: Luther College, Decorah, IA, B.A. in Chemistry

and Biology, 2007; University of Iowa, College of Pharmacy,Department of Pharmaceutical Sciences and ExperimentalTherapeutics, Ph.D. in Medicinal and Natural ProductsChemistry, 2012, Research Advisor: Robert J. Kerns.Nonscientific interests: Traveling abroad, reading books,

exploring New England, trivia, Iowa Hawkeye football, spendingtime with my family.My graduate research focused on understanding the structural

features of fluoroquinolone-class antibiotics that result in celldeath by various lethal pathways and that enable select agentsto overcome resistance mutations. Consequently, I undertookan extensive project with Rob Kerns to synthesize numerousquinolone and quinolone-like derivatives, some of which areshowcased in this paper. It was challenging because thetheoretically “easy” small molecules to synthesize were oftenthe most difficult to create and yet rewarding because thesesame molecules often exhibited the most interesting biologicalactivity. Throughout the process I had the pleasure to workwith our collaborators, Katie Aldred and Neil Osheroff amongothers, in the iterative process of design, synthesis and testingof new quinolone-class antibiotics to better understand theirbiological mechanism(s). (Read Schwanz’s article, DOI:10.1021/cb400592n)

■ ANDREW J. STORASKA

Image courtesy of Andrew Storaska.

Current position:Graduate student in theDept. of Pharmacology,University of Michigan, Ann Arbor. I am working with ProfessorRichard Neubig, now at Michigan State University in the Dept. ofPharmacology and Toxicology.Education: University of Maryland, College Park, B.S. in Cell

Biology and Molecular Genetics, 2008. I worked with ProfessorDavid Fushman in the Dept. of Chemistry and Biochemistry,University of Maryland.Nonscientific interests: Cycling, running, cooking, moviesMy graduate research focuses on developing methods to

manipulate G-protein Coupled Receptor (GPCR) signal trans-duction by modulating the activity of downstream regulatoryproteins-Regulators of G-protein Signaling (RGS). My studieshave focused on understanding the biochemical and biophysicalmechanisms of small molecule inhibitors of RGS proteins.Our recent study exposed the existence of novel conformationalstate of RGS4 that showed the structural basis for the allostericmechanism of inhibition by a very potent RGS inhibitor. Thiswork will provide a useful model for structure-based drug design

ACS Chemical Biology Introducing Our Authors

dx.doi.org/10.1021/cb400862m | ACS Chem. Biol. 2013, 8, 2597−26002599

strategies targeting RGS proteins. Our current work is engagedon that aim. (Read Storaska’s article, DOI: 10.1021/cb400568g)

■ HARISH VASHISTH

Image courtesy of Kyung Jae Jeong.

Current position: Assistant Professor, Department of ChemicalEngineering, University of New HampshireEducation: National Institute of Technology, Warangal, B. Tech

in Chemical Engineering, 2005; Drexel University, Philadelphia, Ph.D.in Chemical and Biological Engineering, 2010, Advisor: Cameron F.Abrams; University of Michigan, Ann Arbor, Postdoctoral ResearchFellow, 2010−2013, Advisor: Charles L. Brooks IIINonscientific interests: Photography,music, movies, badmintonMy lab is interested in understanding the structure−function

relationships in biomolecules. A long-term goal is to study thefunctional behavior of proteins and nucleic acids using theory,modeling, and simulation approaches rooted in the physicalprinciples. This understanding is aimed at helping in the designof biobased materials and therapeutics capable of adopting andmimicking biomolecular characteristics in various environments.In this paper, we have studied the dynamics of a regulatorof G-protein signaling (RGS) protein using enhanced samplingsimulation methods and nuclear magnetic resonance (NMR)spectroscopy. The dynamic features of the RGS-protein studiedhere reveal a mechanism by which inhibitor molecules can gainaccess to the buried side-chains of cysteine residues. This worksuggests a direct role of conformational dynamics in inhibitorsensitivity. (Read Vashisth’s article, DOI: 10.1021/cb400568g)

■ JOSEPH WANG

Image courtesy of Joseph Wang.

Current position: Assistant Research Professor in Prof. AdamZlotnick’s Lab, Molecular andCellular BiochemistryDepartment,Indiana University, Bloomington.

Education: Catholic Fu-Jen University, B.S. in Biology, 1999;National Yang-Ming University, M.S. in Medical Informatics,2001 (Advisor: Yen-Jen Sung); National Yang-Ming University,Ph.D. in Structural Biology, 2008 (Advisor: Der-Ming Liou);Indiana University, Bloomington, Postdoctoral Fellow inStructural Biology, 2010−2013 (Advisor: Adam Zlotnick).Nonscientific interests:Movie, cooking, and everything about

coffee.My research interests focuses on exploring assembly principles

between protein/protein and protein/nucleic acid interactionsusing cryo-EM. Because the lack of characterization on SV40particles limits the development of the therapeutic applications,we have put our attention on studying its assembly mechanism.In this manuscript we examined SV40 assembly on several nucleicacid substrates: ssRNA, ssDNA, and dsDNA. I was involved in thestructural characterization of the particles assembled on 1.9 KntssRNA. We found that very flexible substrates preferentiallysupport assembly of 22-nm diameter particles composed of12 pentameric subunits, a T = 1 icosahedron. On substrates thatare too large to fit into that container, the nucleic acid may beextruded to support a multiplet of T = 1 particle or a larger,irregular particle, in contrast to the large T = 7 icosahedralparticles formed by dsDNA. (ReadWang’s article, DOI: 10.1021/cb4005518)

ACS Chemical Biology Introducing Our Authors

dx.doi.org/10.1021/cb400862m | ACS Chem. Biol. 2013, 8, 2597−26002600