Introducing Our Authors

■ ANETTE BROCKMANN

Image courtesy of Simone Pohlmann.

Current position: Ph.D. student at the Chair Pharmacology,Department of Biology, University of Konstanz (Germany), andthe Konstanz Research School Chemical BiologyEducation: Studies in Biological Sciences at the University

of Kassel and Wurzburg (Germany). Diploma in Biology, 2010.Diploma thesis at theUniversity of Pablo deOlavide, CentroAndaluzde Biologia del Desarrollo (Spain). Since 2011, Ph.D. student in thegroup of Prof. Dr. Brunner at the University of Konstanz with afellowship from the Konstanz Research School Chemical BiologyNonscientific interests: Dancing, sportI have a strong interest in analyzing the mechanism of drugs in

cellular systems. The dose-dependent mode of action of the drug incells and the analysis of signaling pathways involved is one of themaintopics inmy Ph.D. thesis in Prof. Dr. T. Brunner’s group. I am glad tobe a member of the Konstanz Research School Chemical Biology.The graduate school supports the interdisciplinary collaboration ofchemists, biologists, and computer scientists, facilitating collabo-rations and interactionswith other departments. In collaborationwiththe chemists new drugs derivatives were synthesized allowing for thestudy of the structure−function relationship of small molecules incolorectal cancer cells. Additionally, the school offers individualresearch training programs and gives me the possibility to expandmy personal skills not only scientifically but also in management,intercultural communication, and drug development. (ReadBrockmann’s article, DOI: 10.1021/cb4007562)■ MAJOR D. GOOYIT

Image courtesy of Reyna K. V. Lim.

Current position: Postdoctoral Fellow in the laboratory ofProf. Kim Janda at The Scripps Research Institute, La Jolla, CAEducation: University of Notre Dame, Ph.D. in Chemistry

with Profs. Shahriar Mobashery and Mayland Chang, 2013;University of the Philippines-Diliman, B.S. Chemistry, 2004Nonscientific interests: Music, food, travelMy graduate research focused on the elucidation of molecular

mechanisms of gelatinase-dependent diseases and developmentof therapeutic strategies to combat them. In this manuscript,we investigated the matrix metalloproteinase (MMP) expressionprofile of diabetic wounds using a novel affinity resin thatbinds only the active forms of MMPs. By proteomic analyses, wedetected and quantified MMP-8 andMMP-9 in a mouse diabeticwound model and then followed this up by using selectiveMMP-8 and MMP-9 inhibitors to ascertain the therapeutic rolesof these MMPs in diabetic wound healing. We document that theselective inhibition of the detrimental MMP-9, while leavingthe beneficial MMP-8 unaffected, provides a novel strategy inthe first demonstration of a potential therapy for this disease.(Read Gooyit’s article, DOI: 10.1021/cb4005468)

■ TYLER HARRIS

Image courtesy of Tyler Harris.

Current position:North Carolina State University, Departmentof Chemistry, Graduate Student in Professor ChristianMelander’s Lab since 2009Education: University of North Carolina at Wilmington, B.S.

Chemistry, 2006; University of North Carolina at Wilmington,M.S. Chemistry, 2009Nonscientific interests: Brewing beer, poker, fishingMy graduate research has focused on the development of novel

approaches to disable bacterial resistance mechanisms. This hasbeen accomplished by developing small molecules that interferewith two-component systems (TCS) involved in regulatingantimicrobial resistance. In our current work, we proved that a2-aminoimidazole derivative reverses colistin resistance in multi-drug resistant Acinetobacter baumannii by targeting the PmrABTCS. This work illustrates that targeting TCS is a viable solutionto the dire problem of antibiotic resistance. (Read Harris‘ article,DOI: 10.1021/cb400490k)

Published: January 17, 2014

Introducing Our Authors

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© 2014 American Chemical Society 3 dx.doi.org/10.1021/cb400951m | ACS Chem. Biol. 2014, 9, 3−7

pubs.acs.org/acschemicalbiology

■ JOSHUA KOLEV

Image courtesy of John R. Frost.

Current position: Graduate student in the Department ofChemistry, University of Rochester. Advisor: Rudi FasanEducation: Rochester Institute of Technology, B.S. in

Biochemistry, 2010. Advisor: Christina CollisonNonscientific interests: Fishing, home brewing, and watching

moviesThe selective functionalization of aliphatic C−H bonds in

complex molecules holds promise for the late stage elaborationof natural products. My thesis research involves the tuningand selection of cytochromes P450, a family of monooxygenaseenzymes, for the selective oxidation of complex natural productsand natural product-like molecules. In this work we utilized P450‘fingerprinting’ to rapidly select a diverse set of P450 catalystsand predict their activity on parthenolide, a natural productwith promising anticancer properties. We developed catalysts forthe selective oxidation of three positions on the scaffold andfurther modified parthenolide utilizing chemical methods. Theseparthenolide derivatives were tested for activity against primaryacute myelogenous leukemia and found to improve the activityof parthenolide while maintaining selectivity over healthy cells.(Read Kolev’s article, DOI: 10.1021/cb400626w)

■ CARLOS IGNACIO LORDA-DIEZ

Image courtesy of Carlos Ignacio Lorda-Diez.

Current position: Assistant Professor at the University ofCantabria, Department of Anatomy and Cell Biology, Santander,Spain.Education:University of Oviedo, Oviedo, Spain, B.S. Biology,

2004; University of Cantabria, Santander, Spain, Ph.D. inMolecular Biology and Biomedicine with Prof. Juan Hurle and

Prof. Juan A. Montero, 2010; University of Cantabria, Santander,Spain, Extraordinary Ph.D. Award in Health Sciences, 2012Nonscientific interests: Real Oviedo, music, and spending

time with friends and familyOur research group headed by Prof. Juan Hurle is located

at the School of Medicine of the University of Cantabria inSantander, Spain. We are interested in stem cells anddevelopmental biology, and our working model is the vertebratelimb, focusing on the analysis of the molecular control of digitmorphogenesis. We are especially interested in the control of thedifferentiation of connective tissue derivates. In our review, wesummarize investigations performed in the past years to unravelthe molecular signals which regulate the divergent differentiationmechanisms of same mesoderm progenitors into either cartilageor tendon tissues during the digit morphogenesis, focusingour studies on morphogens and intracellular transcriptionfactors revealed as key molecules controlling these processes.(Read Lorda-Diez’ article, DOI: 10.1021/cb400713v)

■ MATTHEW R. MELNICKI

Image courtesy of Bernard Santillan.

Current position: Postdoctoral Fellow in Microbial CellDynamics, Pacific Northwest National Laboratory.Education: George Washington University, B.S. in Biological

Sciences, 2002; University of California, Berkeley, Ph.D. inAgricultural & Environmental Chemistry with Anastasios Melis,2009Nonscientific interests: Literary art, experimental music,

bicyclingFascinated by photosynthesis, I pursue research that looks

at light conversion in highly productive phototrophs. Becausethese organisms can claim nearly all the energetic input to ourbiosphere, they merit our attention. I often joke about one oftheir peculiarities: they cannot turn off the light. During dynamicshifts, which can easily cause redox and/or metabolic “trafficjams”, electrons can back up into the photosystems, riskingdamage to their photocatalytic apparatus. Thus, they havedeveloped mechanisms to avoid photo-oxidation (eat your leafygreens!). But when you break open a cell to study it or remove itfrom its light environment, the features of these photoprotectivestrategies are often lost. Here we present chemical probes thatcan cross membranes and label redox-responsive proteins, andthus track homeostatic dynamics. (Read Melnicki’s article, DOI:10.1021/cb400769v)

ACS Chemical Biology Introducing Our Authors

dx.doi.org/10.1021/cb400951m | ACS Chem. Biol. 2014, 9, 3−74

■ GABRIELE MELONI

Image courtesy of Daniela Raciti.

Current position: Postdoctoral Fellow with Prof. Poul Nissen,Centre for Membrane Pumps in Cells and Disease−PUMPkin,Danish National Research Foundation, Department of MolecularBiology and Genetics, Aarhus University, DenmarkEducation: University of Milan, Italy, M.S. in Biotechnology,

Advisor: Prof. V. F. Sacchi; University of Zurich, Switzerland,Ph.D. in Biochemistry and Postdoctoral Fellow, Advisor: Prof.Milan Vasak; California Institute of Technology, PostdoctoralFellow, Advisor: Prof. Douglas C. Rees.Nonscientific interests: Nature, history, travelMy research focuses on investigating the mechanisms of metal

binding, reactivity and transport by biomolecules, exploring thebioinorganic chemistry underlying physiological and patholog-ical processes. In the current project, we are investigatingthe principles of transition metals selectivity and transport in aclass of ubiquitous membrane proteins which act as primaryactive ion pumps (P1B-Type ATPases) by a combinedbiochemical and biophysical approach. By performing character-ization and comparative analysis of pumps possessing differentmetal selectivity we aim to provide new highlights into thecoordination chemistry involved in metal transport across bio-logical membranes. We present the identification and character-ization of a peculiar high-affinity transmembrane Type-2-likeCu2+ center in CopB form Archaeoglobus fulgidus, the first site ofthis type described in a membrane protein involved in cupric iontransport. (Read Meloni’s article, DOI: 10.1021/cb400603t)

■ NICHOLAS PACE

Image courtesy of Nicholas Pace.

Current position: Ph.D. candidate at Boston College in theDepartment of Chemistry; Advisor: Professor EranthieWeerapana.

Education: Stonehill College, B.S. in Biochemistry, 2010;Undergraduate Advisor: Professor Louis Liotta.Nonscientific interests: Boston Celtics, running, weightlift-

ing, boating, skiingMy graduate research has focused on generating peptide-based

probe libraries to modulate physiologically important cysteine-mediated protein activities. As described in our manuscript, weutilized a peptide-based probe to identify zinc-binding cysteines.Our platform monitors changes in the nucleophilicity of Zn2+-binding cysteines upon treatment with Zn2+ and metal chelators.Through the application of in-gel fluorescence and mass-spectrometry methods, we were able to identify and characterizeknown Zn2+-binding cysteines, as well as previously unannotatedsites of Zn2+ chelation. Perhaps the most notable aspect of thisplatform is its versatility, as this strategy can easily be expanded tointerrogate other biologically relevant metal−cysteine complexesacross diverse proteomes. We hope this platform will aid futureendeavors by chemical biologists to characterize the functionalroles of metal−cysteine complexes in the proteome. (Read Pace’sarticle, DOI: 10.1021/cb400622q)

■ CHRISTOPHER P. PTAK

Image courtesy of Aurora Ptak.

Current position: Research Associate in the laboratory ofDr. Robert E. Oswald, Department of Molecular Medicine,College of Veterinary Medicine, Cornell UniversityEducation: Pennsylvania State University, B.S. in Molecular

and Cell Biology; University of Virginia, Ph.D. in Biophysics,Advisor: Dr. Eduardo PerozoNonscientific interests: Spending time with family, hiking,

yard work, drawingMy research is focused on membrane protein signal

transduction with an emphasis on understanding the underlyingstructural mechanisms. Recently, my effort has been on theionotropic glutamate receptor and the details of how allostericmodulators act to stabilize domain−domain interactionswithin the receptor, thereby enhancing receptor activation.The overall goal is to provide a basis for the development of drugsthat target learning and memory. In the present work, we showthat the ability of a modulator to induce domain dimerizationis significantly impacted by the modulator to dimer ratio. Theconcepts of equilibrium binding are applicable to a broad rangeof medically relevant targets as well as being of general interestin ligand-induced oligomerization. (Read Ptak’s article, DOI:10.1021/cb4007166)



■ NATALIE C. SADLER

Image courtesy of Carrie Nicora.

Current position: Post-Bachelors Research Associate in Dr.Aaron Wright’s Chemoproteomics group at Pacific NorthwestNational Laboratory.Education: Washington State University, B.S. in Biological

Sciences; current graduate student at Washington StateUniversity, Environmental Sciences; NIEHS trainee from 2011to presentNonscientific interests: Outdoor activities, reading, and

spending time with familyMy research aim is to use novel approaches for characterizing

proteins involved in dynamic redox modifications in livingcells. Cysteine plays crucial and diverse biological roles, many ofwhich are elusive. In this work we use chemical probes capableof live cell labeling of redox-sensitive cysteine thiols duringcarbon limitation, starvation, and replenishment.We were able tocapture and characterize the redox dynamics of 176 cysteine-containing protein, 77 previously identified in other photo-autotrophs and 99 newly identified. Additionally, we identifiedthe site of cysteine labeling in 60% of the 176 proteins. We areexpanding on this preliminary study and hope this research willfacilitate a more targeted approach to genetically engineeringcyanobacteria in the pursuit of exploiting this organism forbiofuel production. (Read Sadler’s article DOI: 10.1021/cb400769v)

■ VIPENDER SINGH

Image courtesy of Vipender Singh.

Current position: Massachusetts Institute of Technology,Departments of Chemistry and Biological Engineering, Post-doctoral Associate in the laboratory of Professor John Essigmann

Education: All India Institute of Medical Sciences, B.S. and

M.S.; Albert Einstein College of Medicine, Ph.D. in the

laboratory of Professor Vern Schramm; Yale University,

Postdoctoral fellowship in the laboratory of Scott StrobelNonscientific interests: Sailing, swimming, running, mentor-

ing and exchanging ideas with like-minded peopleI am a researcher interested in conceptually formulating and

developing innovative technologies in the area of biopharma-

ceutical and chemical sciences to solve challenging problems.

My research is focused on the following three areas: (i) studying

transition states of enzymes to understand their chemical

mechanisms and develop anticancer and antibacterial therapeu-

tics, (ii) developing antiviral drugs by chemically altering

viral mutation rates using tautomerizable nucleoside analogues,

and (ii) understanding chemical mechanisms of functional

noncoding RNAs. (Read Singh’s article, DOI: 10.1021/

cb400581f)

■ CONAN K. WANG

Image courtesy of Conan Wang.

Education: The University of New South Wales (BEng

Bioinformatics); The University of Queensland (Ph.D. Molec-

ular Bioscience); Hong Kong University of Science and

Technology (Postdoctoral Fellow); Griffith University (Post

Doctoral Fellow); The University of Queensland (Postdoctoral

Fellow); Research Advisor: David J. CraikNonscientific interests: Movies, reading, tennis, and wing

chunMy research interests include the development of peptide

drugs for the treatment of neurological disorders. One of the

challenges in this area is to develop stable peptide therapeutics to

treat multiple sclerosis (MS), a devastating inflammatory disease

that is still without an effective cure. In the present article, we use

an emerging technique in peptide chemistry, molecular grafting,

to design novel and stable drug leads, and we demonstrate their

effectiveness in a mouse model of MS. (Read Wang’s article,

DOI: 10.1021/cb400548s)



■ LIMEI ZHANG

Image courtesy of Qin Huang.

Current position: Postdoctoral Fellow with Prof. Douglas C.Rees, Division of Chemistry and Chemical Engineering, theCalifornia Institute of Technology.Education: Jilin University, B.S. in Biochemistry; University of

Victoria, M.S. in Biochemistry, advisor: Prof. Edward E. Ishiguro;University of Saskatchewan, Ph.D. in Biochemistry, advisor: Prof.Graham N. George.Nonscientific interests:Traveling, reading, hiking, swimming,

culture crossingMy current research interests include the structure−function

relationship studies on themetalloenzymes in biological nitrogenfixation and the metallotransporters P1B-type ATPases usingX-ray absorption spectroscopy and X-ray crystallography. In thismanuscript, we have captured for the first time the structuralinformation on the metal binding site of the Cu2+-selectiveP1B-type ATPase CopB from Archaeoglobus fulgidus; the absenceof such structural information has impeded our mechanisticunderstanding underlying the substrate- and oxidation state-selectivity by CopB. We are excited to extend structural studieson other P1B-type ATPases, aiming to shine light on how thetransmembrane coordination environment dictates the sub-strate selectivity on transition metals in these P1B-type ATPases.(Read Zhang’s article, DOI: 10.1021/cb400603t)



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Introducing Our Authors