About

Sangjin Kim is an Assistant Professor in the Departments of Physics and Biomedical and Translational Sciences at the University of Illinois. He is also an affiliate of the Carl R. Woese Institute for Genomic Biology. His research focuses on the molecular biology and biophysics of RNA, particularly investigating the mechanisms of transcription and mRNA kinetics in bacterial systems such as Escherichia coli and Caulobacter crescentus. Kim's work involves studying RNA-dependent RNA polymerase, reverse transcriptase, RNA polymerase, and DNA supercoiling, with an emphasis on understanding gene synthesis and transcription dynamics. His research employs advanced techniques including single-particle tracking, fluorescence microscopy, and single-molecule fluorescence in situ hybridization to probe the spatial and temporal kinetics of mRNA. Kim has contributed to the understanding of how DNA supercoiling influences collective modes of gene synthesis and how transcription processes are coordinated with mRNA decay and translation. He has been recognized with honors such as the Searle Scholar Award in 2020 and the Kavli Frontiers of Science Fellowship in 2022.

Research topics

• Biology
• Cancer research
• Medicine
• Internal medicine
• Immunology
• Biochemistry
• Endocrinology
• Cell biology

Selected publications

• JAK/STAT1-interferon-ISGylation networks in breast cancer resistance to inhibitors of FOXM1 and CDK4/6

  npj Breast Cancer · 2026-02-12

  articleOpen access

  The oncogenic transcription factor FOXM1 and the cyclin-dependent kinases 4 and 6 all promote cancer progression and aggressiveness that can be suppressed initially by targeted inhibitors, but resistance almost always develops. We show that ER-positive breast cancer cells that acquire resistance to FOXM1 inhibitors (FOXM1i) or CDK4/6 inhibitors (CDK4/6i) exhibit some key similarities including an increased JAK/STAT-interferon-ISGylation signaling network with elevated ISG15 and ISG15 protein conjugates, but with differences in magnitudes and patterns of ISGylated proteins. All the resistant cell lines also express higher levels of enzymes critical for ISGylation which predict poorer survival outcomes in ER-positive breast cancer patients. Reduction of these proteins pharmacologically or by siRNA knockdown greatly impairs the viability, colony formation, and proliferation of the FOXM1i-resistant cells, with lesser impact on CDK4/6i resistant cells. Notably, CDK4/6i resistant cells and 3D-Matrigel cultures can still be growth inhibited by FOXM1i, and conversely the FOXM1i resistance can be overcome by palbociclib or abemaciclib, indicating that while the resistance mechanisms of these two classes of drugs have some similar features, they are sufficiently distinct so that sequential treatment approaches could be effective in supporting new options such as FOXM1 inhibitor use after progression on CDK4/6 inhibitors.

  PublisherOA PDFDOI

• Abstract 3040: FOXM1 as a drug target in NF1-associated malignant peripheral nerve sheath tumors

  Cancer Research · 2026-04-03

  article

  Abstract Purpose: Malignant peripheral nerve sheath tumors (MPNSTs) are deadly sarcomas that arise spontaneously or via transformation of benign tumors, called plexiform neurofibromas (PNFs) and atypical neurofibromatous neoplasms of uncertain biologic potential (ANNUBPs), in patients with Neurofibromatosis Type 1 (NF1). Understanding molecular events that cooperate to promote malignancy is a priority in the field. One putative driver, FOXM1, is a powerful transcription factor that heightens the activities of kinases, MEK and CDK4/6, known to drive MPNST growth. We sought to understand the role of FOXM1 in these deadly sarcomas and hypothesized it is a new druggable target that is essential for MPNST pathogenesis. Methods: FOXM1 mRNA and protein expression were evaluated in patient-matched PNFs, ANNUBPs, and MPNSTs via RNA-Seq and IHC. For in vitro studies, knockdown (KD) of FOXM1 was performed in MPNST cell lines (S462, sNF96.2, JH2-002). Proliferation, survival, and cell cycle progression were measured in response to FOXM1 inhibitors, including newly developed NB-55, NB-73 and NB-115 drugs. To directly test the in vivo role of FOXM1 in MPNST initiation and progression, de novo MPNSTs were initiated by Nf1/Ink4a/Arf editing in the sciatic nerve of Nf1+/-, DhhCre, Foxm1 floxed mice relative to Nf1+/-;DhhCre controls. Results: In patient-matched tumor sets, FOXM1 mRNA was significantly elevated in MPNSTs relative to PNF/ANNUBP precursor lesions. FOXM1 protein expression rose dramatically in a stepwise manner from normal nerve to PNFs, ANNUBPs, and MPNSTs. FOXM1 KD slowed MPNST cell growth. FOXM1 inhibitors (thiostrepton, FDI-6, and multiple NB drugs) effectively inhibited MPNST proliferation and induced apoptosis. Synergistic killing of MPNST cells was obtained by combining thiostrepton with a MEK inhibitor (mirdametinib), CDK4/6 inhibitor (palbociclib), or EGFR inhibitor (gefitinib), while NB drugs synergized best with gefitinib. Excitingly, targeted in vivo deletion of Foxm1 in the sciatic nerve significantly slowed tumor progression. Conclusion: Our data demonstrate FOXM1 is an important driver of MPNST pathogenesis. FOXM1 expression and transcriptional activity are greatly increased in MPNSTs compared to benign precursors from the same patients. In agreement, genetic and therapeutic inactivation of FOXM1 promoted MPNST cell arrest and death. Synergistic killing of MPNSTs was achieved by combined inhibition of FOXM1 with MEK, CDK4/6, or EGFR while Foxm1 ablation in the sciatic nerve significantly slowed tumor progression in vivo. Together, these findings reveal that FOXM1 inhibition in specific combination therapies represents a new treatment strategy for MPNST patients. Citation Format: Ellen M. Voigt, Quinn Hanigan, Joshua J. Lingo, Altay Koyas, Rebecca D. Dodd, Benjamin W. Darbro, Dragana Kopanja, Sung Hoon Kim, Benita S. Katzenellenbogen, John A. Katzenellenbogen, Dawn E. Quelle. FOXM1 as a drug target in NF1-associated malignant peripheral nerve sheath tumors [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2026; Part 1 (Regular Abstracts); 2026 Apr 17-22; San Diego, CA. Philadelphia (PA): AACR; Cancer Res 2026;86(7 Suppl):Abstract nr 3040.

  PublisherDOI

• Tumor suppressive effect of low-frequency repetitive transcranial magnetic stimulation on glioblastoma progression

  Neurotherapeutics · 2025-03-29 · 5 citations

  articleOpen access

  Repetitive transcranial magnetic stimulation (rTMS) is used as a non-invasive treatment for various diseases, and its potential application in cancer treatment has been proposed by researchers. However, the precise mechanisms and effects of rTMS on many types of cancer, including glioblastoma (GBM), remain largely unknown. This study aimed to investigate the effects of low-frequency rTMS on in vitro and in vivo GBM models and to elucidate an underlying biological mechanism of rTMS on GBM. In vitro and in vivo GBM models were treated with low-frequency rTMS (0.5 ​Hz, 10 ​min per day), and the effects of rTMS were assessed using various assays, including CCK-8 assay, sphere formation assay, 3D invasion assay, RT-qPCR, Western blot, immunohistochemistry, TUNEL assay, MRI, and IVIS. The results showed that treatment of GBM models in vitro with low-frequency rTMS significantly inhibited cell proliferation. Transcriptome array analysis revealed a substantial downregulation of FLNA and FLNC expression after low-frequency rTMS treatment. Moreover, in an in vitro GBM tumor sphere model, low-frequency rTMS suppressed the activation of EGFR and EphA2, inhibited ERK/JNK/p38 and PI3K/AKT/mTOR pathways, and induced apoptosis. Low-frequency rTMS also suppressed the invasion of GBM by downregulating MMP2 and MMP9 expression. Additionally, in an in vivo GBM model, low-frequency rTMS suppressed GBM progression by downregulating FLNA and FLNC expression. The results demonstrated that low-frequency rTMS could be a potential treatment for GBM, achieved by downregulating FLNA and FLNC expression. This study sheds light on the potential for rTMS as a therapeutic strategy for glioblastoma as well as other types of cancers.

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• OR04-08 Ligand Class Analysis Enables Predictive Models for Effective Antagonism of Endocrine Resistant Breast Cancer

  Journal of the Endocrine Society · 2025-10-01

  articleOpen access

  Abstract Disclosure: J.C. Nwachukwu: None. C.K. Min: None. R.R. Kobylski: None. T.J. Kim: None. Y. Hou: None. S. Kim: None. G.R. Hancock: None. T. Izard: None. S.W. Fanning: None. B.S. Katzenellenbogen: None. J.A. Katzenellenbogen: None. K.W. Nettles: None. Drugs targeting the estrogen receptor-α (ER) fall into two chemical classes, selective estrogen receptor modulators and degraders (SERMs and SERDs), which are effective treatments for hormone-responsive breast cancer. Compounds in these chemical classes typically show similar optimized efficacy in pre-clinical models of breast cancer, including in the context of ER-activating mutations (e.g. ER Y537S) and other resistance pathways, limiting our ability to identify small differences that may be more impactful clinically. To understand structural and molecular drivers of ER antagonism, we expanded the repertoire of ER targeting strategies. We characterized 108 compounds derived from a high-affinity adamantyl scaffold, incorporating 8 distinct classes of pharmacophores, each featuring a diverse array of chemical groups. The chemically diverse ligands revealed that non-canonical targeting approaches produced complex structure activity relationships across a panel of hormone sensitive and resistant breast cancer cell lines and reporter systems, activity that was often more efficacious than existing ER-targeted therapies. We obtained X-ray crystal structures of 25 adamantyl ligands bound to ER resistance mutants. This revealed how the different ligand chemical groups generated diverse structural effects on the surface binding site for transcriptional regulatory proteins that regulate gene expression. Molecular dynamics simulations showed that ER Y537S and D538G stabilized different antagonist conformers, or substates, from the wild type receptor, suggesting a structural basis for resistance to ER antagonists. We selected a subset of 11 adamantyls for a computational approach called “ligand class analysis” (LCA). LCA leverages the wide range of growth inhibitory effects of these related compounds (i.e. a compound class) to provide the statistical robustness for machine learning the underlying mechanisms of action. RNA-seq from MCF-7 cells expressing the ER Y537S resistance allele revealed ∼1600 genes differentially regulated by the 11 adamantyl ligands. We used the growth inhibitory effect of each ligand as the dependent variable in machine learning and identified a gene set response pattern with >95% predictive power for ligand efficacy. Defining causal links from ligand to receptor structure and the cellular mediators of growth inhibition revealed basic principles of allosteric signaling and transcriptional regulation. LCA differentiated these outcome-focused ER signaling pathways from the full set of ligand-regulated cellular effects, while diversification of the ligand-receptor structures identified new ways of modulating ER activity for targeting endocrine resistant breast cancer. Supported by NIH R01CA275142, R01CA220284, R37CA27934, and the Breast Cancer Research Foundation BCRF-083 and BCRF-084 Presentation: Saturday, July 12, 2025

  PublisherOA PDFDOI

• Inhibition of FOXM1 Synergizes with BH3 Mimetics Venetoclax and Sonrotoclax in Killing Multiple Myeloma Cells through Repressing MYC Pathway

  Advanced Science · 2025-07-14 · 3 citations

  articleOpen access

  Relapsed and refractory multiple myeloma (RRMM) remains the leading cause of MM mortality. FOXM1 is strongly associated with RRMM, making it a compelling therapeutic target. Through three low-throughput screenings, we have identified nine FDA-approved drugs, including the BH3 mimetic Venetoclax, that synergize with FOXM1 inhibitor NB73 in killing MM cells. Venetoclax has shown effects in 6% of non-t(11;14) and 27% of t(11;14) MM cases. The NB73-Venetoclax combination barely induces acute toxicity in vivo and represses MM cells in vivo and ex vivo. NB73 enhances the ubiquitination and proteasomal degradation of FOXM1, an effect further amplified by Venetoclax. The NB73-Venetoclax combination abolishes FOXM1's binding to promoters of key MYC pathway genes, such as PLK1, leading to significant downregulation of their expression. Furthermore, the PLK1-specific inhibitor GSK461364 synergizes with NB73 to inhibit MM cell growth. Interestingly, NB73 does not sensitize U266 cells, a Venetoclax-resistant t(11;14) MM cell line expressing high FOXM1, to Venetoclax treatment, which is corrected by a new-generation BH3 mimetic Sonrotoclax and ALK inhibitor Ceritinib. Collectively, targeting FOXM1 demonstrates significant potential for enhancing the efficacy of FDA-approved drugs in RRMM. These findings shed new light on the discouraging outcomes of the Phase-III CANOVA study centering Venetoclax with an encouraging molecular clue.

  PublisherDOI

• Benzestrol Isomer Stereochemistry Determines the Distinct Estrogenic Activities and Conformations of the Eight Isomers When Bound to Estrogen Receptor α

  ACS Pharmacology & Translational Science · 2025-07-09 · 1 citations

  articleOpen access

  The nonsteroidal estrogen, benzestrol, has potent estrogenic activity, and through a recent stereocontrolled synthesis, we have obtained all eight of its constituent stereoisomers. We find that only one of them, RSS benzestrol, has very high binding affinity for estrogen receptor alpha (ERα); the other seven isomers have 60 to 600-fold lower affinity. We now show that the potencies of the isomers in two cell activity assays, proliferation of ER-positive breast cancer cells and stimulation of estrogenic gene activity, reflect their varying binding affinities for ERα. The crystal structure of the RSS isomer itself is consistent with its presumed absolute configuration and also reveals its conformational flexibility within the solid crystal lattice. We modeled each of the 8 benzestrol stereoisomers bound to ERα. Their calculated binding energies and internal torsional energies grouped with their experimentally measured binding affinities and biological activities, and the conformation for the highest affinity RSS isomer bound to ERα maps closely onto the conformation of the ERα-bound potent nonsteroidal estrogen, trans-diethylstilbestrol. Hence, we now provide a structural context for this congeneric series of benzestrol stereoisomers by proposing energy-based conformations they adopt when bound to ERα that underlie their effectiveness as estrogens.

  PublisherDOI

• Chloroindazole based estrogen receptor β ligands with favorable pharmacokinetics promote functional remyelination and visual recovery

  Scientific Reports · 2025-10-08

  articleOpen access

  Multiple sclerosis (MS) is a chronic autoimmune, demyelinating, and neurodegenerative disease that results in motor, visual, and cognitive deficits. While existing treatments can slow disease progression, they rarely restore lost neurological function or significantly enhance quality of life. Estrogen receptor β (ERβ) has emerged as a promising therapeutic target due to its ability to activate non-classical signaling pathways involved in neuroprotection, immune modulation, and remyelination. In this study, two chloroindazole-based ERβ-selective ligands, K102 and K110, were identified for their favorable pharmacokinetic profiles and performance in preclinical absorption, distribution, metabolism, and elimination (ADME) screening. These compounds demonstrated biological activity by promoting oligodendrocyte (OL) differentiation in both primary mouse and human OL cultures. In vivo, they enhanced axonal remyelination and improved functional electrophysiological outcomes in two mouse models of MS: experimental autoimmune encephalomyelitis (EAE) and cuprizone diet-induced demyelination. Additionally, K102 and K110 modulated immune responses, supporting OL survival and contributing to motor and visual recovery in EAE mice. These findings provide compelling preclinical evidence for advancing K102 and K110 to clinical development. By simultaneously addressing neurodegeneration and inflammation through ERβ-mediated signaling, these compounds offer a novel and potentially transformative approach to MS therapy.

  PublisherOA PDFDOI

• Abstract 435: JAK/STAT1-interferon-ISGylation networks in breast cancer resistance to inhibitors of FOXM1 and CDK4/6

  Cancer Research · 2025-04-21

  article

  Abstract Resistance to targeted therapies often develops in advanced estrogen receptor (ER)-positive breast cancer, but the mechanisms underlying this resistance are still not fully known. We show that ER-positive FOXM1 inhibitor resistant cells and CDK4/6 inhibitor (Palbociclib and Abemaciclib) resistant cells all exhibit an increased JAK/STAT1-interferon responsive gene and protein signaling network with elevated interferon stimulated gene15 (ISG15). ISG15 protein is present as high intracellular free ISG15 and also as increased ISGylated protein conjugates that can be markedly reduced by treatment of resistant cells with the JAK1/2 inhibitor ruxolitinib. Likewise, resistant cells contain increased levels of ubiquitin-like conjugating enzymes HERC5 and HERC6 and ubiquitin ligases (e.g., UBE2L6) known to facilitate the transfer of ISG15 onto cell proteins. Notably, elevated ISG15 and elevated HERC5 and HERC6 are all associated with poorer relapse-free and overall patient survival. Breast cancer cells resistant to the CDK4/6 inhibitors Palbo or Abema, which are often used in first line treatment of patients with HR-positive breast cancer, and cells resistant to FOXM1 inhibitor show some similarities in the ISGylated protein patterns. However, there are also some differences observed in these patterns between Palbo and Abema and FOXM1 inhibitor (NB73) resistant cells. Upregulation of this STAT1-interferon-ISGylation network in ER-positive breast cancers displaying resistance to three different drugs suggests it may be centrally involved in supporting the drug-resistant state. Importantly, Palbo and Abema resistant cells and organoids can still be effectively growth inhibited by FOXM1 inhibitor NB73, and likewise, FOXM1 inhibitor resistant cells and organoids are sensitive to suppression of viability by Palbo or Abema. This suggests that sequential treatment approaches might be effective in overcoming resistance and enabling the suppression of these drug-resistant cancers.(Supported by Breast Cancer Research Foundation grant BCRF-083 and NIH R01CA220284 to BSK and BCRF grant BCRF-145 to RS) Citation Format: Benita S. Katzenellenbogen, Yvonne Ziegler, Sandeep Kumar, Blake N. Plotner, Carlos M. Saeh, Grace O. Pento, Sung Hoon Kim, Rachel Schiff, John A. Katzenellenbogen. JAK/STAT1-interferon-ISGylation networks in breast cancer resistance to inhibitors of FOXM1 and CDK4/6 [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2025; Part 1 (Regular Abstracts); 2025 Apr 25-30; Chicago, IL. Philadelphia (PA): AACR; Cancer Res 2025;85(8_Suppl_1):Abstract nr 435.

  PublisherDOI

• Estrogen Receptor Mutants with Endocrine Therapies Stabilize Multiple Receptor Antagonist Substates to Drive Efficacy and Resistance

  Endocrinology · 2025-04-01

  articleOpen access

  Abstract Text Current endocrine therapies for breast cancer are used to treat the 70 percent of estrogen receptor (ER) positive breast cancers, but de novo and acquired resistance drive progressive metastatic disease. Hormone therapy development efforts have used similar chemical targeting strategies such that the structural basis of ligand efficacy is not clear. More than a third of patients who develop endocrine therapy resistance have hotspot constitutively activating mutations in the ligand binding domain, most notably Y537S and D538G. While these mutants have been studied extensively in stabilizing agonist conformation and constitutive activity in the absence of estradiol, the structural basis for why these mutations cause loss of efficacy for antagonists is not as well studied. To improve our understanding of structural mechanisms of therapeutic efficacy in the ESR1 mutant setting, we synthesized a diverse series of compounds including ∼100 ligands based on a high affinity adamantyl scaffold. We diversified the ligand side chains with various pharmacophores to understand the structural basis of ligand potency and efficacy on wild type and mutant ERs. Crystal structures of 20 ligands bound to Erα-LBD revealed how the chemical side chain modulated receptor structure to stabilize different conformational states to drive anti-cancer activity. Previous work revealed how the ER mutants drive constitutive activity by stabilizing the active ER conformation, but this state does not occur with antagonist bound ER. Long timescale molecular dynamics simulations were used to understand conformational changes induced by these mutations in the context of the antagonist conformation of the key helix 12 (h12), which determines pathogenic versus therapeutic activity states. The Y537S mutation stabilized h12 in one of two stable antagonist substates with implications for generating treatment resistance. In contrast, the D538G mutation, which is characterized by a helix-breaking effect, generated multiple metastable conformational substates. These findings support a model where the ligand side chains alter the relative stability of different antagonist substates to drive efficacy, with conformations that are different in the wild type versus mutant ERα bound to endocrine therapies. Date of Presentation October 17, 2024

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• Nuclear Receptor NR2E3 Activates Both Wild-Type and Mutated p53 in Multiple Myeloma Cells

  Blood · 2024-11-05 · 2 citations

  article

  Background: Tumor cell plasticity and genome instability contribute to tumor heterogeneity, leading to drug resistance and relapse in cancer patients. Despite great progress in improving 5-year survival rate in multiple myeloma (MM), relapsed and refractory MM (RRMM) remains a major challenge. Given that p53 mutations account for 8% of MM cases, we constructed 50 nonsynonymous mutations of p53 detected in MM patients which include 37 mutations in MMRF database and 13 from published studies. We aim to investigate their functions and interactions with a new tumor suppressor NR2E3, nuclear receptor subfamily 2 group E member 3. We previously demonstrated that NR2E3 stimulates p53 acetylation and its small-molecule agonist 11a represses cancer cells bearing p53 signaling in NCI-60 cancer cell panel. Results: Our study of TCGA and “All of US” databases uncovered the association of NR2E3 nonsynonymous mutations with 4 cancers including MM. We constructed all NR2E3 mutations detected in MM patients, and NR2E3R334W lost the capability of activating p53 transactivity. In contrast, high expression of NR2E3 correlated to superior disease-free and overall survivals of 33 cancers. Co-expressing NR2E3 with p53 mutation partially rescued a subgroup, including 4 hotspot mutations, of 50 p53 mutations in p53-responsive reporter assay. For example, p53R175H was activated by NR2E3 through stimulating the acetylation of p53R175H at K317/K386 and/or K373/K382. Activated p53R175H increased the expressions of its downstream tumor-suppressing genes, such as p21, Puma, DDIT3 and ATF3. NR2E3's agonist 11a enhanced p53 acetylation and transactivation of downstream tumor-suppressing genes. Disrupting NR2E3 by RNAi or overexpression modulated 11a-stimulated p53 acetylation and transactivities. Interestingly, 11a synergized with FDA-approved HDAC inhibitor Romidepsin in killing MM1S myeloma cells that express p53WT and with a new small-molecule FOXM1 inhibitor NB73 in killing OPM2 myeloma cells that carry homozygous alleles of p53R175H. FOXM1 is a master transcription factor of metabolism and cell cycle progression in Forkhead box family, and a critical molecular vulnerability in RRMM. Our recent study demonstrated that FOXM1 inhibitor NB73 synergizes with BCL2 inhibitor Venetoclax in killing non-t(11;14) myeloma cell lines via transcriptional inhibition of MYC pathway. The ChIP-seq study also resolved the DNA binding sites of FOXM1 on the promoters of both p53 and NR2E3 in myeloma cell lines. Degrading FOXM1 protein by NB73 decreased the binding of FOXM1 to the promoters of NR2E3 and p53, enhanced their transcriptions and protein levels in myeloma cell lines. For instance, these NB73-treated OPM2 cells expressed more NR2E3WT and p53R175H. The addition of 11a stimulated NR2E3WT which further rescued p53R175H, leading to intensive cell apoptosis. Ongoing experiments: Rescuing p53 mutations by NR2E3 and its agonist 11a is a very interesting observation. U266 cells bearing t(11;14) translocation are resistant to Venetoclax. We found that U266 cells express NR2E3WT, p53A161T and substantial amount of FOXM1. NR2E3 activated p53A161T, and 11a synergized with NB73 but not Venetoclax in killing U266 cells, which may provide a new therapy to t(11;14)-positive myeloma. Moreover, we are conducting the pharmacokinetics study of 11a in 3 mice using oral gavage route, with which we will be able to perform the pharmacodynamics studies of 11a alone and in combination with NB73, Romidepsin or other FDA-approved anti-cancer drugs in NSG mice engrafted with myeloma cell lines bearing various molecular signatures, including p53 mutations. Detailed mechanisms are studied with multifaceted techniques such as ChIP-Seq and molecular/cellular tools. Significance & conclusion: Nuclear receptors are the main targets of drug development. NR2E3 used to be a retinal photoreceptor-specific transcription factor, but the expression of NR2E3 has been detected in various tissues in human and mouse with new antibodies, which has led to interesting findings in multiple cancers over the past few years. We showed for the first time that NR2E3 is transcriptionally repressed by FOXM1 and pharmaceutically stimulated to activate p53 by its agonist in myeloma cells. Our studies will provide a new drug candidate for MM that is notoriously difficult to cure and burdened with large societal health care expenditures and high mortality rates.

  PublisherDOI

Frequent coauthors

• John A. Katzenellenbogen

  University of Illinois Urbana-Champaign

  78 shared

• Benita S. Katzenellenbogen

  University of Illinois Urbana-Champaign

  57 shared

• Yvonne Ziegler

  University of Illinois Urbana-Champaign

  28 shared

• Valeria Sanabria Guillen

  20 shared

• Jian Min

  Hubei University

  19 shared

• K.W. Nettles

  Scripps Research Institute

  16 shared

• Kathryn E. Carlson

  University of Illinois Urbana-Champaign

  15 shared

• Shunchao Yan

  China Medical University

  14 shared

Labs

• Kim LabPI

Awards & honors

• Searle Scholar (2020)