Ernst Schonbrunn, PhD

Research from the Schonbrunn laboratory focuses on the elucidation of the three-dimensional structure of medicinally important proteins using X-ray crystallography as a main tool. We explore various proteins and protein-ligand complexes at the atomic level to identify "weak spots" that could be exploited for the rational design of novel therapeutics.

Associations

• Drug Discovery
• Malignant Hematology
• Molecular Medicine Program
• Molecular Oncology & Drug Discovery Program

Education & Training

Graduate:

• Max-Planck Research Unit for Structural Molecular Biology, PhD - Biology/Crystallography

Fellowship:

• Max-Planck Research Unit for Structural Molecular Biology - Structural Molecular Biology

The Schonbrunn lab is involved in several interdisciplinary drug discovery projects aimed at the development of small molecule inhibitors and degraders of promising cancer targets, particularly protein kinases and epigenetic proteins. A. Discovery and development of bromodomain inhibitors. Bromodomain (BRD)-containing proteins are essential for the recognition of acetylated lysine (KAc) residues of histones during transcriptional activation. They regulate transcription, chromatin remodeling, gene splicing, protein scaffolding and signal transduction, and therefore, play fundamental roles in cell proliferation and division. BRDs have emerged as promising drug targets for a number of disease pathways that are characterized by changes in the epigenetic cell signature, particularly in cancer. Intense efforts are underway to discover new chemical scaffolds for hit-to-lead development campaigns of BRD inhibitors as novel cancer therapeutics. A1. BET bromodomain inhibitors. Members of the BET family (BRD2, BRD3, BRD4, and BRDT) are the most studied drug targets among BRDs. BRD4 is overexpressed in various cancers and can undergo translocations that are a hallmark of the lethal tumor NUT midline carcinoma. Previously, my lab discovered that diverse kinase inhibitors used in the clinic also inhibit BRD4 and other BET bromodomains (dual BRD4-kinase inhibitors). During the past five years we expanded our research on the polypharmacologic properties of kinase inhibitors by determining the mode of action of chemical scaffolds originally designed to target the kinases PLK1, ERK5 and LRRK2. Our studies revealed new insights for the rational design of drugs that inhibit BET proteins and kinases differentially, depending on the disease (published in 2021; PMID: 34710325). Due to the high structural similarity of the KAc binding sites, most reported inhibitors lack intra-BET selectivity. We surmised that protein-protein interactions induced by homomeric bivalent inhibitors may differ between BRD4 and the other BET proteins, conferring an altered selectivity profile. Starting from nonselective monovalent inhibitors, we developed cell-active bivalent inhibitors with increased activity and intra-BET selectivity, caused by the differential plasticity of bromodomains upon inhibitor-induced dimerization (published in 2022; PMID: 35867655). A2. TAF1 bromodomain inhibitors and degraders. TAF1 is the largest subunit of the transcription factor IID (TFIID) and brings other factors to promoter regions. Recently it was demonstrated that TAF1 has a critical role in AML1-ETO driven acute myeloid leukemia (AML). In collaboration with Justin Lopchuk and Jiandong Chen, we discovered the ATR kinase inhibitor ceralasertib as a bona fide inhibitor of TAF1 bromodomain. Functional studies on p53 signaling in cancer cell lines provided new insights into the feasibility and challenges of small molecule TAF1 inhibitors as therapeutics (published in 2022, PMID 35191694). Although monovalent inhibitors are potent binders of TAF1 such compounds lack cancer cell kill potential. Therefore, we applied a structure-guided approach to generate cereblon recruiting PROTACs of TAF1. These PROTACs are highly effective in degrading TAF1. TAF1 depletion activates p53 and induces apoptosis in cell lines of AML and certain solid tumors. Importantly, an in vivo active TAF1 PROTAC inhibited the growth of AML tumor xenograft. A manuscript about these first-in-class TAF1 degraders has been submitted, and an NIH/NCI R01 grant including Eric Padron as co-I has been awarded in 2024 to develop TAF1 degraders as cancer therapeutics. A3. EP300 and CBP bromodomain inhibitors. Two key proteins that function to maintain and reinforce malignant gene expression programs through regulation of transcription are the multidomain and paralogous histone acetyltransferases (HATs), EP300 and CBP. These proteins contain several highly homologous domains, including KIX, BRDs and HAT domains, through which they interact with, dock to, and acetylate target proteins, respectively. In collaboration with Jun Qi (DFCI) and Wei Zhang (University of Massachusetts) we identified a new potent and selective EP300/CBP bromodomain inhibitor (published in 2021, PMID 33872011). In collaboration with Adam Durbin (St. Jude) and Jun Qi (DFCI) we further explored EP300 and CBP through a domain-specific inhibitory approach. We discovered that targeting EP300/CBP using the inhibitors A485 (HAT) or CCS1477 (BRD) have different effects in select tumor types. These studies provide a domain-specific structural foundation for drug discovery efforts targeting EP300/CBP and identify a selective role for the EP300/CBP bromodomain in maintaining genetic dependency networks in G3MB (published in 2022 and 2024, PMID 34772733 and 38664416). A4. BRD7 and BRD9 bromodomain inhibitors. BRD9 has attracted attention as a druggable subunit of mSWI/SNF chromatin remodeling complexes. In contrast, BRD7 is a potential tumor suppressor with critical functions in oligodendrocytes progenitor cell differentiation. As the role of BRD7 in human biology is not fully understood, off-target inhibition of BRD7 by non-selective BRD9 inhibitors bears the risk of unwanted pleiotropic effects. An obstacle to the rational design of inhibitors selective for BRD9 was the limited structural information on BRD7. My lab applied a multifaceted approach towards the characterization of diverse small molecule inhibitors with varying degrees of potency and selectivity for BRD7 and BRD9. We report the discovery of first-in-class dual BRD9-kinase inhibitors. Novel crystal structures of BRD7 and BRD9 liganded with new and known inhibitors were determined, and the data afford a new framework for the structure-based design of inhibitors with improved selectivity or additional polypharmacologic properties (published in 2020, PMID 32091206). B. Discovery and development of kinase inhibitors. Recent successes in the development of small molecule protein kinase inhibitors as drugs have led to an influx in kinase-directed drug discovery programs. Although a vast number of ATP-competitive small molecule kinase inhibitors have been developed, lack of efficacy and side effects caused by off-target interactions have prevented many of these from advancing through clinical trials. Using structure-based design we previously discovered and/or developed highly potent inhibitors of the kinases Aurora A, CDK2, Rock1, MST3, and of the entire family of Wee kinases (Wee1, Wee2 and PKMYT1). Since 2019 we have focused our attention on inhibitors and degraders of the following kinases: B1. Allosteric inhibitors of CDK2. Compared to most ATP-site kinase inhibitors, small molecules that target an allosteric pocket have the potential for improved selectivity due to the often observed lower structural similarity at these distal sites. CDK2 is a target for many therapeutic indications, including cancer. However, an inhibitor against this kinase with exquisite selectivity has not reached the market because of the structural similarity between CDKs. In collaboration with Gunda Georg (University of Minnesota) we exploited our previously identified allosteric site in CDK2 to develop a series of first-in-class allosteric inhibitors that bind CDK2 with nanomolar affinity, making them the most potent, structurally confirmed allosteric CDK inhibitors reported (published in 2023, PMIDs 36701569 and 37270540). Based on a series of high-resolution cocrystal structures that my lab determined, we have entered a collaboration with Justin Lopchuk and Erin George for the development of bivalent allosteric CDK2 inhibitors to treat cancers characterized by cyclin E amplification, such as ovarian cancer. For this project, we were recently awarded funding through an R21 grant from the NCI. B2. Inhibitors of JAK2. The discovery that aberrant activity of Janus kinase 2 (JAK2) is a driver of myeloproliferative neoplasms (MPNs) has led to significant efforts to develop small molecule inhibitors for this patient population. Ruxolitinib and fedratinib have been approved for use in MPN patients, while baricitinib, an achiral analogue of ruxolitinib, has been approved for rheumatoid arthritis. However, structural information on the interaction of these therapeutics with JAK2 remained unknown. In collaboration with Nicholas Lawrence and Gary Reuther, we determined the first crystal structures of JAK2 bound to these drugs and derivatives thereof. Along with biochemical and cellular data, the results provide a comprehensive view of the shape complementarity required for chiral and achiral inhibitors to achieve highest activity, which may facilitate the development of more effective JAK2 inhibitors as therapeutics (published in 2021, PMID 33570945). B3. Molecular glue degraders of cyclin K. CDK12 and its cognate cyclin co-activator protein, cyclin K, regulate transcription elongation and termination, co-transcriptional splicing, as well as RNA turnover. CDK12 has been shown to play essential roles in genome maintenance by regulating the expression of DNA damage repair genes. CDK12 inhibitors such as SR-4835 display molecular glue activity, which correlates with an enhanced ability to inhibit cell growth. This effect is achieved by facilitating the formation of a ternary complex that requires SR-4835, CDK12, and the adaptor protein DDB1, leading to the subsequent ubiquitination and degradation of cyclin K without the need for a DCAF substrate receptor. In collaboration with Andrii Monastyrskyi and Derek Duckett my lab performs biochemical and structural studies on a series of novel molecular glue degraders to determine the potential for this class of inhibitors as cancer therapeutics. This project is funded by a DoD grant and the first of a planned series of papers has just been published (PMID 39450271). B4. Inhibitors of ULK1. ULK1 is one of the central upstream regulators of the autophagy pathway and represents a key target for the development of molecular probes to abrogate autophagy and explore potential therapeutic avenues. In collaboration with Andrii Monastyrskyi and Derek Duckett my lab performed biochemical and structural studies on a series of novel ULK1 inhibitors. We have solved the crystal structure of a lead compound MR-2088 bound to the active site of ULK1. Combined, our findings underscore MR-2088’s potential to inhibit starvation/stimuli-induced autophagic flux, coupled with its suitability for in vivo studies (published in 2024, PMID 38232465). This project will soon be submitted as an R01 to the NCI. My lab is also involved in a similar project to target the autophagy kinase ULK3 with novel small molecule inhibitors headed by Nicholas Lawrence (Bankhead-Coley grant 2024 – 2027) and Conor Lynch (R01 NCI 2022 – 2027). B5. Covalent inhibitors of EGFR and BTK. EGFR mutations cause cancer by regulating metabolic processes that are critical for cancer cell proliferation: BTK plays a crucial role in the development and function of B cells, making it a key target for treating B-cell malignancies like chronic lymphocytic leukemia (CLL). While several next generation inhibitors have been successfully used to target these two tyrosine kinases, drug resistance eventually overcomes the efficacy of these treatments. The Justin Lopchuk laboratory has developed a series of novel strain-release covalent inhibitors to specifically target a specific cysteine residue in the ATP sites of EGFR and BTK. My lab has recently determined the first crystal structure of this novel class of inhibitors covalently attached to EGFR. A manuscript about these studies is in preparation, and recently submitted grants to the NCI and Bankhead-Coley are pending. C. Other proteins C1. Inhibitors and degraders of GRB2. GRB2 is an adaptor protein that mediates activation of mitogenic Ras signaling pathways. Aberrant GRB2-dependent Ras activation significantly contributes to cancer development and progression. In collaboration with Mark Ji and Eric Haura, we have determined a high-resolution crystal structure of GRB2 liganded with a novel peptidomimetic inhibitor. The structure revealed key structural features for GRB2–inhibitor binding and offers a new direction for structural optimization to generate cell-permeable inhibitors as well as PROTAC degraders for this key protein in aberrant Ras-MAPK signaling cascades. This project is funded through an R21 from the NCI. A first study was published in 2021 (PMID 32511789), and a new manuscript about recently developed first-in-class PROTAC degraders of GRB2 is in preparation.

• Chen L, Shultz ZP, Sansone M, Fang B, Liu X, Teng M, Schonbrunn E, Lopchuk JM, Chen J. PROTAC-Mediated Degradation of TAF1 Induces Apoptosis in AML Cells and Inhibits Tumor Growth In Vivo. Mol Cancer Ther. 2025 Nov.24(11):1712-1721. Pubmedid: 40376796. Pmcid: PMC12353786.
• Jiang J, Liang T, Solberg J, Chan A, Kalra P, Shi R, Pomerantz WCK, Hawkinson JE, Schönbrunn E, Georg GI. Macrocyclic dihydropyridine analogs as pan-BET BD2-preferred inhibitors. Eur J Med Chem. 2025 Jun.290:117504. Pubmedid: 40120495. Pmcid: PMC11993331.
• Tauro M, Li T, Sudalagunta PR, Meads M, Canevarolo RR, Nerlakanti N, Alugubelli RR, Lawrence HR, Gunawan S, Ayaz M, Nareddy P, Yun SY, Shay G, Yang K, Tran TH, Bishop RT, Nasr MM, Lawrence NNJ, Schönbrunn E, Cleveland JL, Silva AS, Shain KH, Lynch CC. Unc-51 Like Kinase 3 (ULK3) is essential for autophagy and cell survival in multiple myeloma. Res Sq. 2025 Aug. Pubmedid: 40831505. Pmcid: PMC12363935.
• Ghosh P, Schmitz M, Pandurangan T, Zeleke ST, Chan SC, Mosior J, Sun L, Palve V, Grassie D, Anand K, Frydman S, Roush WR, Schönbrunn E, Geyer M, Duckett D, Monastyrskyi A. Discovery and design of molecular glue enhancers of CDK12-DDB1 interactions for targeted degradation of cyclin K. RSC Chem Biol. 2024 Oct. Pubmedid: 39450271. Pmcid: PMC11494886.
• Morozova A, Chan SC, Bayle S, Sun L, Grassie D, Iermolaieva A, Kalaga MN, Frydman S, Sansil S, Schönbrunn E, Duckett D, Monastyrskyi A. Development of potent and selective ULK1/2 inhibitors based on 7-azaindole scaffold with favorable in vivo properties. Eur J Med Chem. 2024 Feb.266:116101. Pubmedid: 38232465.
• Shendy NAM, Bikowitz M, Sigua LH, Zhang Y, Mercier A, Khashana Y, Nance S, Liu Q, Delahunty IM, Robinson S, Goel V, Rees MG, Ronan MA, Wang T, Kocak M, Roth JA, Wang Y, Freeman BB, Orr BA, Abraham BJ, Roussel MF, Schonbrunn E, Qi J, Durbin AD. Group 3 medulloblastoma transcriptional networks collapse under domain specific EP300/CBP inhibition. Nat Commun. 2024 Apr.15(1):3483. Pubmedid: 38664416. Pmcid: PMC11045757.
• Faber EB, Sun L, Tang J, Roberts E, Ganeshkumar S, Wang N, Rasmussen D, Majumdar A, Hirsch LE, John K, Yang A, Khalid H, Hawkinson JE, Levinson NM, Chennathukuzhi V, Harki DA, Schönbrunn E, Georg GI. Development of allosteric and selective CDK2 inhibitors for contraception with negative cooperativity to cyclin binding. Nat Commun. 2023 Jun.14(1):3213. Pubmedid: 37270540. Pmcid: PMC10239507.
• Faber EB, Wang N, John K, Sun L, Wong HL, Burban D, Francis R, Tian D, Hong KH, Yang A, Wang L, Elsaid M, Khalid H, Levinson NM, Schönbrunn E, Hawkinson JE, Georg GI. Screening through Lead Optimization of High Affinity, Allosteric Cyclin-Dependent Kinase 2 (CDK2) Inhibitors as Male Contraceptives That Reduce Sperm Counts in Mice. J Med Chem. 2023 Feb.66(3):1928-1940. Pubmedid: 36701569.
• Liao Y, Chin Chan S, Welsh EA, Fang B, Sun L, Schönbrunn E, Koomen JM, Duckett DR, Haura EB, Monastyrskyi A, Rix U. Chemical Proteomics with Novel Fully Functionalized Fragments and Stringent Target Prioritization Identifies the Glutathione-Dependent Isomerase GSTZ1 as a Lung Cancer Target. Acs Chem Biol. 2023 Feb.18(2):251-264. Pubmedid: 36630201.
• Al Noman MA, Cuellar RAD, Kyzer JL, Chung SSW, Cheryala N, Holth TAD, Maitra S, Naqvi T, Wong HL, Schönbrunn E, Hawkinson JE, Wolgemuth DJ, Georg GI. Strategies for developing retinoic acid receptor alpha-selective antagonists as novel agents for male contraception. Eur J Med Chem. 2023 Dec.261:115821. Pubmedid: 37776573.
• Jiang J, Zhao PL, Sigua LH, Chan A, Schönbrunn E, Qi J, Georg GI. 1,4-Dihydropyridinebutyrolactone-derived ring-opened ester and amide analogs targeting BET bromodomains. Arch Pharm (Weinheim). 2022 Nov.355(11):e2200288. Pubmedid: 35941525. Pmcid: PMC9633406.
• Giuliano AR, Pilon-Thomas S, Schell MJ, Abrahamsen M, Islam JY, Isaacs-Soriano K, Kennedy K, Dukes CW, Whiting J, Rathwell J, Hensel JA, Mangual LN, Schonbrunn E, Bikowitz M, Grassie D, Yang Y. SARS-CoV-2 Period Seroprevalence and Related Factors, Hillsborough County, Florida, USA, October 2020-March 2021. Emerg Infect Dis. 2022 Mar.28(3):556-563. Pubmedid: 35081021. Pmcid: PMC8888241.
• Durbin AD, Wang T, Wimalasena VK, Zimmerman MW, Li D, Dharia NV, Mariani L, Shendy NAM, Nance S, Patel AG, Shao Y, Mundada M, Maxham L, Park PMC, Sigua LH, Morita K, Saur Conway A, Robichaud AL, Perez-Atayde AR, Bikowitz MJ, Quinn TR, Wiest OG, Easton J, Schonbrunn E, Bulyk ML, Abraham BJ, Stegmaier K, Look AT, Qi J. EP300 Selectively Controls the Enhancer Landscape of MYCN-Amplified Neuroblastoma. Cancer Discov. 2022 Mar.12(3):730-751. Pubmedid: 34772733. Pmcid: PMC8904277.
• Karim RM, Yang L, Chen L, Bikowitz MJ, Lu J, Grassie D, Shultz ZP, Lopchuk JM, Chen J, Schönbrunn E. Discovery of Dual TAF1-ATR Inhibitors and Ligand-Induced Structural Changes of the TAF1 Tandem Bromodomain. J Med Chem. 2022 Mar.65(5):4182-4200. Pubmedid: 35191694.
• Jiang J, Sigua LH, Chan A, Kalra P, Pomerantz WCK, Schönbrunn E, Qi J, Georg GI. Dihydropyridine Lactam Analogs Targeting BET Bromodomains. Chemmedchem. 2022 Jan.17(1):e202100407. Pubmedid: 34932262. Pmcid: PMC8762755.
• Guan X, Cheryala N, Karim RM, Chan A, Berndt N, Qi J, Georg GI, Schönbrunn E. Bivalent BET Bromodomain Inhibitors Confer Increased Potency and Selectivity for BRDT via Protein Conformational Plasticity. J Med Chem. 2022 Aug.65(15):10441-10458. Pubmedid: 35867655.
• Zahid H, Buchholz CR, Singh M, Ciccone MF, Chan A, Nithianantham S, Shi K, Aihara H, Fischer M, Schönbrunn E, Dos Santos CO, Landry JW, Pomerantz WCK. New Design Rules for Developing Potent Cell-Active Inhibitors of the Nucleosome Remodeling Factor (NURF) via BPTF Bromodomain Inhibition. J Med Chem. 2021 Sep.64(18):13902-13917. Pubmedid: 34515477. Pmcid: PMC9012132.
• Xiao T, Sun L, Zhang M, Li Z, Haura EB, Schonbrunn E, Ji H. Synthesis and structural characterization of a monocarboxylic inhibitor for GRB2 SH2 domain. Bioorg Med Chem Lett. 2021 Nov.51:128354. Pubmedid: 34506932. Pmcid: PMC8526398.
• Muthengi A, Wimalasena VK, Yosief HO, Bikowitz MJ, Sigua LH, Wang T, Li D, Gaieb Z, Dhawan G, Liu S, Erickson J, Amaro RE, Schönbrunn E, Qi J, Zhang W. Development of Dimethylisoxazole-Attached Imidazo[1,2-a]pyridines as Potent and Selective CBP/P300 Inhibitors. J Med Chem. 2021 May.64(9):5787-5801. Pubmedid: 33872011. Pmcid: PMC8856734.
• Lee JC, Hong KH, Becker A, Tash JS, Schönbrunn E, Georg GI. Tetrahydroindazole inhibitors of CDK2/cyclin complexes. Eur J Med Chem. 2021 Mar.214:113232. Pubmedid: 33550184. Pmcid: PMC7954990.
• Davis RR, Li B, Yun SY, Chan A, Nareddy P, Gunawan S, Ayaz M, Lawrence HR, Reuther GW, Lawrence NJ, Schönbrunn E. Structural Insights into JAK2 Inhibition by Ruxolitinib, Fedratinib, and Derivatives Thereof. J Med Chem. 2021 Feb.64(4):2228-2241. Pubmedid: 33570945. Pmcid: PMC8327781.
• Olson NM, Kroc S, Johnson JA, Zahid H, Ycas PD, Chan A, Kimbrough JR, Kalra P, Schönbrunn E, Pomerantz WCK. NMR Analyses of Acetylated H2A.Z Isoforms Identify Differential Binding Interactions with the Bromodomain of the NURF Nucleosome Remodeling Complex. Biochemistry-Us. 2020 May.59(20):1871-1880. Pubmedid: 32356653. Pmcid: PMC7771244.
• Karim RM, Chan A, Zhu JY, Schönbrunn E. Structural Basis of Inhibitor Selectivity in the BRD7/9 Subfamily of Bromodomains. J Med Chem. 2020 Mar.63(6):3227-3237. Pubmedid: 32091206. Pmcid: PMC7771325.
• Huang Q, Chen L, Schonbrunn E, Chen J. MDMX inhibits casein kinase 1α activity and stimulates Wnt signaling. Embo J. 2020 Jul.39(14):e104410. Pubmedid: 32511789. Pmcid: PMC7361285.
• Ycas PD, Zahid H, Chan A, Olson NM, Johnson JA, Talluri SK, Schonbrunn E, Pomerantz WCK. New inhibitors for the BPTF bromodomain enabled by structural biology and biophysical assay development. Org Biomol Chem. 2020 Jul.18(27):5174-5182. Pubmedid: 32588860. Pmcid: PMC7393680.
• Li Q, Karim RM, Cheng M, Das M, Chen L, Zhang C, Lawrence HR, Daughdrill GW, Schonbrunn E, Ji H, Chen J. Inhibition of p53 DNA binding by a small molecule protects mice from radiation toxicity. Oncogene. 2020 Jul.39(29):5187-5200. Pubmedid: 32555331. Pmcid: PMC7398576.
• Liu X, Huang Q, Chen L, Zhang H, Schonbrunn E, Chen J. Tumor-derived CK1α mutations enhance MDMX inhibition of p53. Oncogene. 2020 Jan.39(1):176-186. Pubmedid: 31462704. Pmcid: PMC7739390.
• Hanna CB, Mudaliar D, John K, Allen CL, Sun L, Hawkinson JE, Schönbrunn E, Georg GI, Jensen JT. Development of WEE2 kinase inhibitors as novel non-hormonal female contraceptives that target meiosis†. Biol Reprod. 2020 Aug.103(2):368-377. Pubmedid: 32667031. Pmcid: PMC7401407.
• Hanna CB, Yao S, Martin M, Schönbrunn E, Georg GI, Jensen JT, Cuellar RAD. Identification and Screening of Selective WEE2 Inhibitors to Develop Non-Hormonal Contraceptives that Specifically Target Meiosis. ChemistrySelect. 2019 Dec.4(45):13363-13369. Pubmedid: 32190728. Pmcid: PMC7079731.
• Divakaran A, Talluri SK, Ayoub AM, Mishra N, Cui H, Widen JC, Berndt N, Zhu JY, Carlson AS, Topczewski JJ, Schönbrunn E, Harki DA, Pomerantz WCK. Molecular Basis for the N-Terminal Bromodomain-and-Extra-Terminal-Family Selectivity of a Dual Kinase-Bromodomain Inhibitor. J Med Chem. 2018 Oct.61(20):9316-9334. Pubmedid: 30253095. Pmcid: PMC6245549.
• Chen Y, Zhu JY, Hong KH, Mikles DC, Georg GI, Goldstein AS, Amory JK, Schönbrunn E. Structural Basis of ALDH1A2 Inhibition by Irreversible and Reversible Small Molecule Inhibitors. Acs Chem Biol. 2018 Mar.13(3):582-590. Pubmedid: 29240402. Pmcid: PMC6089219.
• Nerlakanti N, Yao J, Nguyen DT, Patel AK, Eroshkin AM, Lawrence HR, Ayaz M, Kuenzi BM, Agarwal N, Chen Y, Gunawan S, Karim RM, Berndt N, Puskas J, Magliocco AM, Coppola D, Dhillon J, Zhang J, Shymalagovindarajan S, Rix U, Kim Y, Perera R, Lawrence NJ, Schonbrunn E, Mahajan K. Targeting the BRD4-HOXB13 Coregulated Transcriptional Networks with Bromodomain-Kinase Inhibitors to Suppress Metastatic Castration-Resistant Prostate Cancer. Mol Cancer Ther. 2018 Dec.17(12):2796-2810. Pubmedid: 30242092. Pmcid: PMC6528782.
• Paulson CN, Guan X, Ayoub AM, Chan A, Karim RM, Pomerantz WCK, Schönbrunn E, Georg GI, Hawkinson JE. Design, Synthesis, and Characterization of a Fluorescence Polarization Pan-BET Bromodomain Probe. ACS Med Chem Lett. 2018 Dec.9(12):1223-1229. Pubmedid: 30613330. Pmcid: PMC6295860.
• Akuffo AA, Alontaga AY, Metcalf R, Beatty MS, Becker A, McDaniel JM, Hesterberg RS, Goodheart WE, Gunawan S, Ayaz M, Yang Y, Karim MR, Orobello ME, Daniel K, Guida W, Yoder JA, Rajadhyaksha AM, Schonbrunn E, Lawrence HR, Lawrence NJ, Epling-Burnette PK. Ligand-mediated protein degradation reveals functional conservation among sequence variants of the CUL4-type E3 ligase substrate receptor cereblon. J Biol Chem. 2018 Apr.293(16):6187-6200. Pubmedid: 29449372. Pmcid: PMC5912449.
• Zhu JY, Cuellar RAD, Berndt N, Lee HE, Olesen SH, Martin MP, Jensen JT, Georg GI, Schönbrunn E. Structural Basis of Wee Kinases Functionality and Inactivation by Diverse Small Molecule Inhibitors. J Med Chem. 2017 Sep.60(18):7863-7875. Pubmedid: 28792760. Pmcid: PMC6200136.
• Xu Y, Greenberg RA, Schonbrunn E, Wang PJ. Meiosis-specific proteins MEIOB and SPATA22 cooperatively associate with the single-stranded DNA-binding replication protein A complex and DNA double-strand breaks. Biol Reprod. 2017 May.96(5):1096-1104. Pubmedid: 28453612. Pmcid: PMC6355104.
• Ember SW, Lambert QT, Berndt N, Gunawan S, Ayaz M, Tauro M, Zhu JY, Cranfill PJ, Greninger P, Lynch CC, Benes CH, Lawrence HR, Reuther GW, Lawrence NJ, Schonbrunn E. Potent Dual BET Bromodomain-Kinase Inhibitors as Value-Added Multitargeted Chemical Probes and Cancer Therapeutics. Mol Cancer Ther. 2017 Jun.16(6):1054-1067. Pubmedid: 28336808. Pmcid: PMC5457702.
• Ayoub AM, Hawk LML, Herzig RJ, Jiang J, Wisniewski AJ, Gee CT, Zhao P, Zhu JY, Berndt N, Offei-Addo NK, Scott TG, Qi J, Bradner JE, Ward TR, Schönbrunn E, Georg GI, Pomerantz WCK. BET Bromodomain Inhibitors with One-Step Synthesis Discovered from Virtual Screen. J Med Chem. 2017 Jun.60(12):4805-4817. Pubmedid: 28535045. Pmcid: PMC5558211.
• Wright G, Golubeva V, Remsing Rix LL, Berndt N, Luo Y, Ward GA, Gray JE, Schönbrunn E, Lawrence HR, Monteiro ANA, Rix U. Dual Targeting of WEE1 and PLK1 by AZD1775 Elicits Single Agent Cellular Anticancer Activity. Acs Chem Biol. 2017 Jul.12(7):1883-1892. Pubmedid: 28557434. Pmcid: PMC5551971.
• Georg GI, Gu X, Gupta V, Yang Y, Zhu J, Carlson E, Kingsley C, Tash J, Schonbrunn E, Hawkinson J. Structure-Activity Studies of N-Butyl-1-deoxynojirimycin (NB-DNJ) Analogues: Discovery of Potent and Selective Aminocyclopentitol Inhibitors of GBA1 and GBA2. Chemmedchem. 2017 Dec.12(23):1977-1984. Pubmedid: 28975712. Pmcid: PMC5725710.
• Allen BK, Mehta S, Ember SWJ, Zhu JY, Schönbrunn E, Ayad NG, Schürer SC. Identification of a Novel Class of BRD4 Inhibitors by Computational Screening and Binding Simulations. ACS Omega. 2017 Aug.2(8):4760-4771. Pubmedid: 28884163. Pmcid: PMC5579542.
• Berndt N, Karim RM, Schönbrunn E. Advances of small molecule targeting of kinases. Curr Opin Chem Biol. 2017 Aug.39:126-132. Pubmedid: 28732278. Pmcid: PMC5728163.
• Karim RM, Schönbrunn E. An Advanced Tool To Interrogate BRD9. J Med Chem. 2016 May.59(10):4459-4461. Pubmedid: 27120693.
• Olesen SH, Zhu JY, Martin MP, Schönbrunn E. Discovery of Diverse Small-Molecule Inhibitors of Mammalian Sterile20-like Kinase 3 (MST3). Chemmedchem. 2016 Jun.11(11):1137-1144. Pubmedid: 27135311. Pmcid: PMC7771544.
• Koblan LW, Buckley DL, Ott CJ, Fitzgerald ME, Ember SW, Zhu JY, Liu S, Roberts JM, Remillard D, Vittori S, Zhang W, Schonbrunn E, Bradner JE. Assessment of Bromodomain Target Engagement by a Series of BI2536 Analogues with Miniaturized BET-BRET. Chemmedchem. 2016 Dec.11(23):2575-2581. Pubmedid: 27862999.
• Mishra NK, Urick AK, Ember SW, Schönbrunn E, Pomerantz WC. Correction to Letter: Fluorinated Aromatic Amino Acids Are Sensitive (19)F NMR Probes for Bromodomain-Ligand Interactions. Acs Chem Biol. 2016 Apr.11(4):1149. Pubmedid: 26836633. Pmcid: PMC4835746.
• Allen BK, Mehta S, Ember SW, Schonbrunn E, Ayad N, Schürer SC. Large-Scale Computational Screening Identifies First in Class Multitarget Inhibitor of EGFR Kinase and BRD4. Sci Rep. 2015 Nov.5:16924. Pubmedid: 26596901. Pmcid: PMC4657038.
• Olesen SH, Ingles DJ, Zhu JY, Martin MP, Betzi S, Georg GI, Tash JS, Schönbrunn E. Stability of the human Hsp90-p50Cdc37 chaperone complex against nucleotides and Hsp90 inhibitors, and the influence of phosphorylation by casein kinase 2. Molecules. 2015 Jan.20(1):1643-1660. Pubmedid: 25608045. Pmcid: PMC4601640.
• Chen L, Borcherds W, Wu S, Becker A, Schonbrunn E, Daughdrill GW, Chen J. Autoinhibition of MDMX by intramolecular p53 mimicry. Proc Natl Acad Sci U S A. 2015 Apr.112(15):4624-4629. Pubmedid: 25825738. Pmcid: PMC4403185.
• Yang H, Lawrence HR, Kazi A, Gevariya H, Patel R, Luo Y, Rix U, Schonbrunn E, Lawrence NJ, Sebti SM. Dual Aurora A and JAK2 kinase blockade effectively suppresses malignant transformation. Oncotarget. 2014 May.5(10):2947-2961. Pubmedid: 24930769. Pmcid: PMC4102782.
• Ember SW, Zhu JY, Olesen SH, Martin MP, Becker A, Berndt N, Georg GI, Schonbrunn E. Acetyl-lysine binding site of bromodomain-containing protein 4 (BRD4) interacts with diverse kinase inhibitors. Acs Chem Biol. 2014 May.9(5):1160-1171. Pubmedid: 24568369. Pmcid: PMC4032195.
• Mishra NK, Urick AK, Ember S, Schonbrunn E, Pomerantz WC. Fluorinated aromatic amino acids are sensitive 19F NMR probes for bromodomain-ligand interactions. Acs Chem Biol. 2014 Dec.9(12):2755-2760. Pubmedid: 25290579. Pmcid: PMC4273984.
• Olesen SH, Ingles DJ, Yang Y, Schönbrunn E. Differential antibacterial properties of the MurA inhibitors terreic acid and fosfomycin. J Basic Microbiol. 2014 Apr.54(4):322-326. Pubmedid: 23686727. Pmcid: PMC4610358.
• Martin MP, Olesen SH, Georg GI, Schonbrunn E. Cyclin-dependent kinase inhibitor dinaciclib interacts with the acetyl-lysine recognition site of bromodomains. Acs Chem Biol. 2013 Nov.8(11):2360-2365. Pubmedid: 24007471. Pmcid: PMC3846258.
• Schonbrunn E, Betzi S, Alam R, Martin MP, Becker A, Han H, Francis R, Chakrasali R, Jakkaraj S, Kazi A, Sebti SM, Cubitt CL, Gebhard AW, Hazlehurst LA, Tash JS, Georg GI. Development of highly potent and selective diaminothiazole inhibitors of cyclin-dependent kinases. J Med Chem. 2013 May.56(10):3768-3782. Pubmedid: 23600925. Pmcid: PMC3714109.
• Martin MP, Alam R, Betzi S, Ingles DJ, Zhu JY, Schönbrunn E. A novel approach to the discovery of small-molecule ligands of CDK2. Chembiochem. 2012 Sep.13(14):2128-2136. Pubmedid: 22893598. Pmcid: PMC3483082.
• Lawrence HR, Martin MP, Luo Y, Pireddu R, Yang H, Gevariya H, Ozcan S, Zhu JY, Kendig R, Rodriguez M, Elias R, Cheng JQ, Sebti SM, Schonbrunn E, Lawrence NJ. Development of o-chlorophenyl substituted pyrimidines as exceptionally potent aurora kinase inhibitors. J Med Chem. 2012 Sep.55(17):7392-7416. Pubmedid: 22803810. Pmcid: PMC4429609.
• Patel RA, Forinash KD, Pireddu R, Sun Y, Sun N, Martin MP, Schönbrunn E, Lawrence NJ, Sebti SM. RKI-1447 is a potent inhibitor of the Rho-associated ROCK kinases with anti-invasive and antitumor activities in breast cancer. Cancer Res. 2012 Oct.72(19):5025-5034. Pubmedid: 22846914. Pmcid: PMC3463757.
• Doi K, Li R, Sung SS, Wu H, Liu Y, Manieri W, Krishnegowda G, Awwad A, Dewey A, Liu X, Amin S, Cheng C, Qin Y, Schonbrunn E, Daughdrill G, Loughran TP, Sebti S, Wang HG. Discovery of marinopyrrole A (maritoclax) as a selective Mcl-1 antagonist that overcomes ABT-737 resistance by binding to and targeting Mcl-1 for proteasomal degradation. J Biol Chem. 2012 Mar.287(13):10224-10235. Pubmedid: 22311987. Pmcid: PMC3323047.
• Li R, Martin MP, Liu Y, Wang B, Patel RA, Zhu JY, Sun N, Pireddu R, Lawrence NJ, Li J, Haura EB, Sung SS, Guida WC, Schonbrunn E, Sebti SM. Fragment-based and structure-guided discovery and optimization of Rho kinase inhibitors. J Med Chem. 2012 Mar.55(5):2474-2478. Pubmedid: 22272748. Pmcid: PMC4516226.
• Pireddu R, Forinash KD, Sun NN, Martin MP, Sung SS, Alexander B, Zhu JY, Guida WC, Schönbrunn E, Sebti SM, Lawrence NJ. Pyridylthiazole-based ureas as inhibitors of Rho associated protein kinases (ROCK1 and 2). Medchemcomm. 2012 Jun.3(6):699-709. Pubmedid: 23275831. Pmcid: PMC3531244.
• Wu S, Chen L, Becker A, Schonbrunn E, Chen J. Casein kinase 1α regulates an MDMX intramolecular interaction to stimulate p53 binding. Mol Cell Biol. 2012 Dec.32(23):4821-4832. Pubmedid: 23028042. Pmcid: PMC3497597.
• Martin MP, Zhu JY, Lawrence HR, Pireddu R, Luo Y, Alam R, Ozcan S, Sebti SM, Lawrence NJ, Schönbrunn E. A novel mechanism by which small molecule inhibitors induce the DFG flip in Aurora A. Acs Chem Biol. 2012 Apr.7(4):698-706. Pubmedid: 22248356. Pmcid: PMC4429595.
• Lee JC, Francis S, Dutta D, Gupta V, Yang Y, Zhu JY, Tash JS, Schönbrunn E, Georg GI. Synthesis and evaluation of eight- and four-membered iminosugar analogues as inhibitors of testicular ceramide-specific glucosyltransferase, testicular β-glucosidase 2, and other glycosidases. J Org Chem. 2012 Apr.77(7):3082-3098. Pubmedid: 22432895. Pmcid: PMC3431965.
• Zhu JY, Yang Y, Han H, Betzi S, Olesen SH, Marsilio F, Schönbrunn E. Functional consequence of covalent reaction of phosphoenolpyruvate with UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA). J Biol Chem. 2012 Apr.287(16):12657-12667. Pubmedid: 22378791. Pmcid: PMC3339971.
• Betzi S, Alam R, Martin M, Lubbers DJ, Han H, Jakkaraj SR, Georg GI, Schönbrunn E. Discovery of a potential allosteric ligand binding site in CDK2. Acs Chem Biol. 2011 May.6(5):492-501. Pubmedid: 21291269. Pmcid: PMC3098941.
• Pollegioni L, Schonbrunn E, Siehl D. Molecular basis of glyphosate resistance-different approaches through protein engineering. FEBS J. 2011 Aug.278(16):2753-2766. Pubmedid: 21668647. Pmcid: PMC3145815.
• Berndt N, Yang H, Trinczek B, Betzi S, Zhang Z, Wu B, Lawrence NJ, Pellecchia M, Schönbrunn E, Cheng JQ, Sebti SM. The Akt activation inhibitor TCN-P inhibits Akt phosphorylation by binding to the PH domain of Akt and blocking its recruitment to the plasma membrane. Cell Death Differ. 2010 Nov.17(11):1795-1804. Pubmedid: 20489726. Pmcid: PMC2952662.
• Han H, Yang Y, Olesen SH, Becker A, Betzi S, Schönbrunn E. The fungal product terreic acid is a covalent inhibitor of the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA) . Biochemistry-Us. 2010 May.49(19):4276-4282. Pubmedid: 20392080. Pmcid: PMC2884014.
• Mahajan K, Coppola D, Challa S, Fang B, Chen YA, Zhu W, Lopez AS, Koomen J, Engelman RW, Rivera C, Muraoka-Cook RS, Cheng JQ, Schönbrunn E, Sebti SM, Earp HS, Mahajan NP. Ack1 mediated AKT/PKB tyrosine 176 phosphorylation regulates its activation. PLoS One. 2010 Mar.5(3):e9646. Pubmedid: 20333297. Pmcid: PMC2841635.
• Phan J, Li Z, Kasprzak A, Li B, Sebti S, Guida W, Schönbrunn E, Chen J. Structure-based design of high affinity peptides inhibiting the interaction of p53 with MDM2 and MDMX. J Biol Chem. 2010 Jan.285(3):2174-2183. Pubmedid: 19910468. Pmcid: PMC2804373.
• Alontaga AY, Rodriguez JC, Schönbrunn E, Becker A, Funke T, Yukl ET, Hayashi T, Stobaugh J, Moënne-Loccoz P, Rivera M. Structural characterization of the hemophore HasAp from Pseudomonas aeruginosa: NMR spectroscopy reveals protein-protein interactions between Holo-HasAp and hemoglobin. Biochemistry-Us. 2009 Jan.48(1):96-109. Pubmedid: 19072037. Pmcid: PMC2666852.
• Funke T, Yang Y, Han H, Healy-Fried M, Olesen S, Becker A, Schonbrunn E. Structural basis of glyphosate resistance resulting from the double mutation Thr97 -> Ile and Pro101 -> Ser in 5-enolpyruvylshikimate-3-phosphate synthase from Escherichia coli. J Biol Chem. 2009 Apr.284(15):9854-9860. Pubmedid: 19211556. Pmcid: PMC2665107.
• Wang A, Rodríguez JC, Han H, Schönbrunn E, Rivera M. X-ray crystallographic and solution state nuclear magnetic resonance spectroscopic investigations of NADP+ binding to ferredoxin NADP reductase from Pseudomonas aeruginosa. Biochemistry-Us. 2008 Aug.47(31):8080-8093. Pubmedid: 18605699. Pmcid: PMC2792877.
• Wang A, Zeng Y, Han H, Weeratunga S, Morgan B, Moenne-Loccoz P, Schonbrunn E, Rivera M. Biochemical and structural characterization of Pseudomonas aeruginosa Bfd and FPR: ferredoxin NADP+ reductase and not ferredoxin is the redox partner of heme oxygenase under iron-starvation conditions. Biochemistry-Us. 2007 Oct.46(43):12198-12211. Pubmedid: 17915950.
• Healy-Fried M, Funke T, Priestman M, Han H, Schonbrunn E. Structural basis of glyphosate tolerance resulting from mutations of Pro101 in Escherichia coli 5-enolpyruvylshikimate-3-phosphate synthase. J Biol Chem. 2007 Nov.282(45):32949-32955. Pubmedid: 17855366.
• Funke T, Healy-Fried M, Han H, Alberg D, Bartlett P, Schonbrunn E. Differential inhibition of class I and class II 5-enolpyruvylshikimate-3-phosphate synthases by tetrahedral reaction intermediate analogues. Biochemistry-Us. 2007 Nov.46(46):13344-13351. Pubmedid: 17958399.
• Li Q, Hanzlik R, Weaver R, Schonbrunn E. Molecular mode of action of a covalently inhibiting peptidomimetic on the human calpain protease core. Biochemistry. 2006 Jan.45(3):701-708. Pubmedid: 16411745.
• Funke T, Han H, Healy-Fried ML, Fischer M, Schonbrunn E. Molecular basis for the herbicide resistance of Roundup Ready crops. Proc Natl Acad Sci U S A. 2006 Aug.103(35):13010-13015. Pubmedid: 16916934. Pmcid: PMC1559744.
• Priestman M, Healy M, Funke T, Becker A, Schonbrunn E. Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate. FEBS Lett. 2005 Oct.579(25):5773-5780. Pubmedid: 16225867.
• Priestman MA, Healy ML, Becker A, Alberg DG, Bartlett PA, Lushington GH, Schönbrunn E. Interaction of phosphonate analogues of the tetrahedral reaction intermediate with 5-enolpyruvylshikimate-3-phosphate synthase in atomic detail. Biochemistry. 2005 Mar.44(9):3241-3248. Pubmedid: 15736934.
• Priestman M, Funke T, Singh I, Crupper S, Schonbrunn E. 5-Enolpyruvylshikimate-3-phosphate synthase from Staphylococcus aureus is insensitive to glyphosate. FEBS Lett. 2005 Jan.579(3):728-732. Pubmedid: 15670836.
• Eschenburg S, Priestman M, Schonbrunn E. Evidence that the fosfomycin target Cys115 in UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is essential for product release. J Biol Chem. 2005 Feb.280(5):3757-3763. Pubmedid: 15531591.
• Eschenburg S, Priestman M, Abdul-Latif F, Delachaume C, Fassy F, Schonbrunn E. A novel inhibitor that suspends the induced fit mechanism of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA). J Biol Chem. 2005 Apr.280(14):14070-14075. Pubmedid: 15701635.
• Eschenburg S, Kabsch W, Healy M, Schonbrunn E. A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states. J Biol Chem. 2003 Dec.278(49):49215-49222. Pubmedid: 13129913.
• Eschenburg S, Healy M, Priestman M, Lushington G, Schonbrunn E. How the mutation glycine96 to alanine confers glyphosate insensitivity to 5-enolpyruvyl shikimate-3-phosphate synthase from Escherichia coli. Planta. 2002 Nov.216(1):129-135. Pubmedid: 12430021.
• Schonbrunn E, Eschenburg S, Shuttleworth W, Schloss J, Amrhein N, Evans J, Kabsch W. Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail. Proc Natl Acad Sci U S A. 2001 Feb.98(4):1376-1380. Pubmedid: 11171958.
• Schonbrunn E, Eschenburg S, Krekel F, Luger K, Amrhein N. Role of the loop containing residue 115 in the induced-fit mechanism of the bacterial cell wall biosynthetic enzyme MurA. Biochemistry. 2000 Mar.39(9):2164-2173. Pubmedid: 10694381.
• Schonbrunn E, Eschenburg S, Luger K, Kabsch W, Amrhein N. Structural basis for the interaction of the fluorescence probe 8-anilino-1-naphthalene sulfonate (ANS) with the antibiotic target MurA. Proc Natl Acad Sci U S A. 2000 Jun.97(12):6345-6349. Pubmedid: 10823915.
• Eschenburg S, Schonbrunn E. Comparative X-ray analysis of the un-liganded fosfomycin-target murA. Proteins. 2000 Aug.40(2):290-298. Pubmedid: 10842342.
• Schonbrunn E, Phlippen W, Trinczek B, Sack S, Eschenburg S, Mandelkow E, Mandelkow E. Crystallization of a macromolecular ring assembly of tubulin liganded with the anti-mitotic drug podophyllotoxin. J Struct Biol. 1999 Dec.128(2):211-215. Pubmedid: 10600574.
• Macheroux P, Schonbrunn E, Svergun D, Volkov V, Koch M, Bornemann S, Thorneley R. Evidence for a major structural change in Escherichia coli chorismate synthase induced by flavin and substrate binding. Biochem J. 1998 Oct.335 ( Pt 2):319-327. Pubmedid: 9761730 .
• Schonbrunn E, Svergun D, Amrhein N, Koch M. Studies on the conformational changes in the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine enolpyruvyltransferase (MurA). Eur J Biochem. 1998 Apr.253(2):406-412. Pubmedid: 9654090 .
• Kozielski F, Schonbrunn E, Sack S, Muller J, Brady S, Mandelkow E. Crystallization and preliminary X-ray analysis of the single-headed and double-headed motor protein kinesin. J Struct Biol. 1997 Jun.119(1):28-34. Pubmedid: 9216086 .
• Kozielski F, Sack S, Marx A, Thormahlen M, Schonbrunn E, Biou V, Thompson A, Mandelkow E, Mandelkow E. The crystal structure of dimeric kinesin and implications for microtubule-dependent motility. Cell. 1997 Dec.91(7):985-994. Pubmedid: 9428521 .
• Schonbrunn E, Sack S, Eschenburg S, Perrakis A, Krekel F, Amrhein N, Mandelkow E. Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin. Structure. 1996 Sep.4(9):1065-1075. Pubmedid: 8805592 .
• Sack S, Dauter Z, Wanke C, Amrhein N, Mandelkow E, Schonbrunn E. Crystallization and preliminary X-ray diffraction analysis of UDP-N-acetylglucosamine enolpyruvyltransferase of Enterobacter cloacae. J Struct Biol. 1996 Jul.117(1):73-76. Pubmedid: 8776890 .
• Schweers O, Schonbrunn-Hanebeck E, Marx A, Mandelkow E. Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure. J Biol Chem. 1994 Sep.269(39):24290-24297. Pubmedid: 7929085 .
• Schonbrunn-Hanebeck E, Laber B, Amrhein N. Slow-binding inhibition of the Escherichia coli pyruvate dehydrogenase multienzyme complex by acetylphosphinate. Biochemistry. 1990 May.29(20):4880-4885. Pubmedid: 2194562 .

• Title: Generation of co-crystal structures of ALDH1A1 and ALDH1A2 with an inhibitor
  Award Number: 75N94023D00006/74N94023F00003
  Sponsor: National Institute of Child Health and Human Development (NICHD)
  Schonbrunn, E. (PD/PI)
• Title: Selective Targeting of TAF1 Function in Acute Myeloid Leukemia
  Award Number: 1R01CA279378-01A1
  Sponsor: National Cancer Institute (NCI)
  Chen, J. (PD/PI), Lopchuk, J. (PD/PI), Schonbrunn, E. (PD/PI)
• Title: Development of bifunctional CDK2 inhibitors for treatment of CCNE1-driven cancers
  Award Number: 1R21CA288927-01
  Sponsor: National Cancer Institute (NCI)
  Lopchuk, J. (PD/PI), Schonbrunn, E. (PD/PI)