LigPlot+: Multiple Ligand–Protein Interaction Diagrams for Drug Discovery

A general method applicable to the search for similarities in the amino acid sequence of two proteins

Needleman, S. B., & Wunsch, C. D. (1970) · Journal of Molecular Biology · doi:10.1016/0022-2836(70)90057-4 · Cited by 11,288

PLIP: fully automated protein–ligand interaction profiler

Salentin, S., Schreiber, S., Haupt, V. J., Adasme, M. F., & Schroeder, M. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv315 · Cited by 2,340

Structural basis of PROTAC cooperative recognition for selective protein degradation

Gadd, M. S., Testa, A., Lucas, X., Chan, K.-H., Chen, W., Lamont, D. J., Zengerle, M., & Ciulli, A. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2329 · Cited by 1,242

Psychedelics promote plasticity by directly binding to BDNF receptor TrkB

Moliner, R., Girych, M., Brunello, C. A., Kovaleva, V., Biojone, C., Enkavi, G., Antenucci, L., Kot, E. F., Goncharuk, S. A., Kaurinkoski, K., et al. (2023) · Nature Neuroscience · doi:10.1038/s41593-023-01316-5 · Cited by 478

Roseburia intestinalis generated butyrate boosts anti-PD-1 efficacy in colorectal cancer by activating cytotoxic CD8 + T cells

Kang, X., Liu, C., Ding, Y., Ni, Y., Ji, F., Lau, H. C. H., Jiang, L., Sung, J. J., Wong, S. H., & Yu, J. (2023) · Gut · doi:10.1136/gutjnl-2023-330291 · Cited by 394

Inhibition of Angiotensin-Converting Enzyme Activity by Flavonoids: Structure-Activity Relationship Studies

Guerrero, L., Castillo, J., Quiñones, M., Garcia-Vallvé, S., Arola, L., Pujadas, G., & Muguerza, B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0049493 · Cited by 391

Shared structural mechanisms of general anaesthetics and benzodiazepines

Kim, J. J., Gharpure, A., Teng, J., Zhuang, Y., Howard, R. J., Zhu, S., Noviello, C. M., Walsh, R. M., Lindahl, E., & Hibbs, R. E. (2020) · Nature · doi:10.1038/s41586-020-2654-5 · Cited by 382

Molecular Mechanism for Plant Steroid Receptor Activation by Somatic Embryogenesis Co-Receptor Kinases

Santiago, J., Henzler, C., & Hothorn, M. (2013) · Science · doi:10.1126/science.1242468 · Cited by 357

The Molecular Mechanism of Transport by the Mitochondrial ADP/ATP Carrier

Ruprecht, J. J., King, M. S., Zögg, T., Aleksandrova, A. A., Pardon, E., Crichton, P. G., Steyaert, J., & Kunji, E. R. S. (2019) · Cell · doi:10.1016/j.cell.2018.11.025 · Cited by 319

Host Cofactors and Pharmacologic Ligands Share an Essential Interface in HIV-1 Capsid That Is Lost upon Disassembly

Price, A. J., Jacques, D. A., McEwan, W. A., Fletcher, A. J., Essig, S., Chin, J. W., Halambage, U. D., Aiken, C., & James, L. C. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004459 · Cited by 284

Structural basis for the neutralization of SARS-CoV-2 by an antibody from a convalescent patient

Zhou, D., Duyvesteyn, H. M. E., Chen, C.-P., Huang, C.-G., Chen, T.-H., Shih, S.-R., Lin, Y.-C., Cheng, C.-Y., Cheng, S.-H., Huang, Y.-C., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0480-y · Cited by 274

An artificial intelligence accelerated virtual screening platform for drug discovery

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Neurodegenerative disease mutations in TREM2 reveal a functional surface and distinct loss-of-function mechanisms

Kober, D. L., Alexander-Brett, J. M., Karch, C. M., Cruchaga, C., Colonna, M., Holtzman, M. J., & Brett, T. J. (2016) · eLife · doi:10.7554/elife.20391 · Cited by 238

Structures of β-klotho reveal a ‘zip code’-like mechanism for endocrine FGF signalling

Lee, S., Choi, J., Mohanty, J., Sousa, L. P., Tome, F., Pardon, E., Steyaert, J., Lemmon, M. A., Lax, I., & Schlessinger, J. (2018) · Nature · doi:10.1038/nature25010 · Cited by 236

Inhibition of delta-secretase improves cognitive functions in mouse models of Alzheimer’s disease

Zhang, Z., Obianyo, O., Dall, E., Du, Y., Fu, H., Liu, X., Kang, S. S., Song, M., Yu, S.-P., Cabrele, C., et al. (2017) · Nature Communications · doi:10.1038/ncomms14740 · Cited by 146

Bapineuzumab captures the N-terminus of the Alzheimer's disease amyloid-beta peptide in a helical conformation

Miles, L. A., Crespi, G. A. N., Doughty, L., & Parker, M. W. (2013) · Scientific Reports · doi:10.1038/srep01302 · Cited by 130

Structure and mechanism of human diacylglycerol O-acyltransferase 1

Wang, L., Qian, H., Nian, Y., Han, Y., Ren, Z., Zhang, H., Hu, L., Prasad, B. V. V., Laganowsky, A., Yan, N., et al. (2020) · Nature · doi:10.1038/s41586-020-2280-2 · Cited by 123

Defining molecular glues with a dual-nanobody cannabidiol sensor

Cao, S., Kang, S., Mao, H., Yao, J., Gu, L., & Zheng, N. (2022) · Nature Communications · doi:10.1038/s41467-022-28507-1 · Cited by 125

Mutations in DCC cause isolated agenesis of the corpus callosum with incomplete penetrance

Marsh, A. P. L., Heron, D., Edwards, T. J., Quartier, A., Galea, C., Nava, C., Rastetter, A., Moutard, M.-L., Anderson, V., Bitoun, P., et al. (2017) · Nature Genetics · doi:10.1038/ng.3794 · Cited by 101

Discovery of Novel Thiazole Carboxamides as Antifungal Succinate Dehydrogenase Inhibitors

Guo, X., Zhao, B., Fan, Z., Yang, D., Zhang, N., Wu, Q., Yu, B., Zhou, S., Kalinina, T. A., & Belskaya, N. P. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b06935 · Cited by 96

Recognition of the Diglycine C-End Degron by CRL2KLHDC2 Ubiquitin Ligase

Rusnac, D.-V., Lin, H.-C., Canzani, D., Tien, K. X., Hinds, T. R., Tsue, A. F., Bush, M. F., Yen, H.-C. S., & Zheng, N. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.10.021 · Cited by 93

Peptide inhibitors of the Keap1–Nrf2 protein–protein interaction with improved binding and cellular activity

Hancock, R., Schaap, M., Pfister, H., & Wells, G. (2013) · Organic & Biomolecular Chemistry · doi:10.1039/c3ob40249e · Cited by 91

Identification of the nicotinamide salvage pathway as a new toxification route for antimetabolites

Buonvicino, D., Mazzola, F., Zamporlini, F., Resta, F., Ranieri, G., Camaioni, E., Muzzi, M., Zecchi, R., Pieraccini, G., Dölle, C., et al. (2018) · Cell Chemical Biology · doi:10.1016/j.chembiol.2018.01.012 · Cited by 73

Structural Basis for Inhibitor-Induced Aggregation of HIV Integrase

Gupta, K., Turkki, V., Sherrill-Mix, S., Hwang, Y., Eilers, G., Taylor, L., McDanal, C., Wang, P., Temelkoff, D., Nolte, R. T., et al. (2016) · PLOS Biology · doi:10.1371/journal.pbio.1002584 · Cited by 68

Structural basis for the ligand-dependent activation of heterodimeric AHR-ARNT complex

Diao, X., Shang, Q., Guo, M., Huang, Y., Zhang, M., Chen, X., Liang, Y., Sun, X., Zhou, F., Zhuang, J., et al. (2025) · Nature communications · doi:10.1038/s41467-025-56574-7 · Cited by 72

Identification of FDA approved drugs and nucleoside analogues as potential SARS-CoV-2 A1pp domain inhibitor: An in silico study

Singh, A. K., Kushwaha, P. P., Prajapati, K. S., Shuaib, M., Gupta, S., & Kumar, S. (2021) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2020.104185 · Cited by 58

High-resolution electron cryomicroscopy of V-ATPase in native synaptic vesicles

Coupland, C. E., Karimi, R., Bueler, S. A., Liang, Y., Courbon, G. M., Di Trani, J. M., Wong, C. J., Saghian, R., Youn, J.-Y., Wang, L.-Y., et al. (2024) · Science · doi:10.1126/science.adp5577 · Cited by 58

Autoinducer-2 and bile salts induce c-di-GMP synthesis to repress the T3SS via a T3SS chaperone

Li, S., Sun, H., Li, J., Zhao, Y., Wang, R., Xu, L., Duan, C., Li, J., Wang, Z., Liu, Q., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34607-9 · Cited by 58

Phytochemicals present in Indian ginseng possess potential to inhibit SARS-CoV-2 virulence: A molecular docking and MD simulation study

Kushwaha, P. P., Singh, A. K., Prajapati, K. S., Shuaib, M., Gupta, S., & Kumar, S. (2021) · Microbial Pathogenesis · doi:10.1016/j.micpath.2021.104954 · Cited by 53

Cryo-EM structure of the cytosolic AhR complex.

Wen, Z., Zhang, Y., Zhang, B., Hang, Y., Xu, L., Chen, Y., Xie, Q., Zhao, Q., Zhang, L., Li, G., et al. (2023) · Structure · doi:10.1016/j.str.2022.12.013 · Cited by 51

Conformational motions and ligand-binding underlying gating and regulation in IP3R channel

Fan, G., Baker, M. R., Terry, L. E., Arige, V., Chen, M., Seryshev, A. B., Baker, M. L., Ludtke, S. J., Yule, D. I., & Serysheva, I. I. (2022) · Nature Communications · doi:10.1038/s41467-022-34574-1 · Cited by 52

Structure of the Wnt–Frizzled–LRP6 initiation complex reveals the basis for coreceptor discrimination

Tsutsumi, N., Hwang, S., Waghray, D., Hansen, S., Jude, K. M., Wang, N., Miao, Y., Glassman, C. R., Caveney, N. A., Janda, C. Y., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2218238120 · Cited by 52

SARS-CoV-2 Variants Show a Gradual Declining Pathogenicity and Pro-Inflammatory Cytokine Stimulation, an Increasing Antigenic and Anti-Inflammatory Cytokine Induction, and Rising Structural Protein Instability: A Minimal Number Genome-Based Approach

Barh, D., Tiwari, S., Rodrigues Gomes, L. G., Ramalho Pinto, C. H., Andrade, B. S., Ahmad, S., Aljabali, A. A. A., Alzahrani, K. J., Banjer, H. J., Hassan, S. S., et al. (2023) · Inflammation · doi:10.1007/s10753-022-01734-w · Cited by 50

Combined x-ray crystallography and computational modeling approach to investigate the Hsp90 C-terminal peptide binding to FKBP51

Kumar, R., Moche, M., Winblad, B., & Pavlov, P. F. (2017) · Scientific Reports · doi:10.1038/s41598-017-14731-z · Cited by 40

Deciphering Dimerization Modes of PAS Domains: Computational and Experimental Analyses of the AhR:ARNT Complex Reveal New Insights Into the Mechanisms of AhR Transformation

Corrada, D., Soshilov, A. A., Denison, M. S., & Bonati, L. (2016) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1004981 · Cited by 43

Structure-function analyses unravel distinct effects of allosteric inhibitors of HIV-1 integrase on viral maturation and integration

Bonnard, D., Le Rouzic, E., Eiler, S., Amadori, C., Orlov, I., Bruneau, J.-M., Brias, J., Barbion, J., Chevreuil, F., Spehner, D., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.816793 · Cited by 42

Broadly inhibitory antibodies to severe malaria virulence proteins

Reyes, R. A., Raghavan, S. S. R., Hurlburt, N. K., Introini, V., Bol, S., Kana, I. H., Jensen, R. W., Martinez-Scholze, E., Gestal-Mato, M., López-Gutiérrez, B., et al. (2024) · Nature · doi:10.1038/s41586-024-08220-3 · Cited by 35

Uncovering an allosteric mode of action for a selective inhibitor of human Bloom syndrome protein

Chen, X., Ali, Y. I., Fisher, C. E., Arribas-Bosacoma, R., Rajasekaran, M. B., Williams, G., Walker, S., Booth, J. R., Hudson, J. J., Roe, S. M., et al. (2021) · eLife · doi:10.7554/elife.65339 · Cited by 34

Structure and mechanism of a tripartite ATP-independent periplasmic TRAP transporter

Davies, J. S., Currie, M. J., North, R. A., Scalise, M., Wright, J. D., Copping, J. M., Remus, D. M., Gulati, A., Morado, D. R., Jamieson, S. A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36590-1 · Cited by 34

Structural basis of prostaglandin efflux by MRP4

Pourmal, S., Green, E., Bajaj, R., Chemmama, I. E., Knudsen, G. M., Gupta, M., Sali, A., Cheng, Y., Craik, C. S., Kroetz, D. L., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01176-4 · Cited by 29

Phenyl Bis-Sulfonamide Keap1-Nrf2 Protein–Protein Interaction Inhibitors with an Alternative Binding Mode

Georgakopoulos, N., Talapatra, S., Dikovskaya, D., Dayalan Naidu, S., Higgins, M., Gatliff, J., Ayhan, A., Nikoloudaki, R., Schaap, M., Valko, K., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00457 · Cited by 33

Highly potent and broadly neutralizing anti-CD4 trimeric nanobodies inhibit HIV-1 infection by inducing CD4 conformational alteration

Zhu, L., Huang, B., Wang, X., Ni, F., Ao, M., Wang, R., Zheng, B., Chen, C., Xue, J., Zhu, L., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51414-6 · Cited by 25

Structural and mechanistic basis of substrate transport by the multidrug transporter MRP4

Bloch, M., Raj, I., Pape, T., & Taylor, N. M. I. (2023) · Structure · doi:10.1016/j.str.2023.08.014 · Cited by 23

Study on tumour cell-derived hybrid exosomes as dasatinib nanocarriers for pancreatic cancer therapy

Zhou, X., Zhuang, Y., Liu, X., Gu, Y., Wang, J., Shi, Y., Zhang, L., Li, R., Zhao, Y., Chen, H., et al. (2023) · Artificial Cells, Nanomedicine, and Biotechnology · doi:10.1080/21691401.2023.2264358 · Cited by 23

A C-type lectin induces NLRP3 inflammasome activation via TLR4 interaction in human peripheral blood mononuclear cells

Ikenohuchi, Y. J., Silva, M. D. S., Rego, C. M. A., Francisco, A. F., da Silva Setúbal, S., Ferreira e Ferreira, A. A., Boeno, C. N., Santana, H. M., Felipin, K. P., de Lima, A. M., et al. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04839-z · Cited by 20

The structure of bradyzoite-specific enolase from Toxoplasma gondii reveals insights into its dual cytoplasmic and nuclear functions

Ruan, J., Mouveaux, T., Light, S. H., Minasov, G., Anderson, W. F., Tomavo, S., & Ngô, H. M. (2015) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s1399004714026479 · Cited by 20

Neutralizing antibodies reveal cryptic vulnerabilities and interdomain crosstalk in the porcine deltacoronavirus spike protein

Du, W., Debski-Antoniak, O., Drabek, D., van Haperen, R., van Dortmondt, M., van der Lee, J., Drulyte, I., van Kuppeveld, F. J. M., Grosveld, F., Hurdiss, D. L., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49693-0 · Cited by 19

Structural basis for autoinhibition by the dephosphorylated regulatory domain of Ycf1

Khandelwal, N. K., & Tomasiak, T. M. (2024) · Nature Communications · doi:10.1038/s41467-024-46722-w · Cited by 17

Cryo-EM reveals the conformational epitope of human monoclonal antibody PAM1.4 broadly reacting with polymorphic malarial protein VAR2CSA

Raghavan, S. S. R., Dagil, R., Lopez-Perez, M., Conrad, J., Bassi, M. R., Quintana, M. D. P., Choudhary, S., Gustavsson, T., Wang, Y., Gourdon, P., et al. (2022) · PLOS Pathogens · doi:10.1371/journal.ppat.1010924 · Cited by 14

Retromer‐mediated recruitment of the WASH complex involves discrete interactions between VPS35 , VPS29, and FAM21

Romano‐Moreno, M., Astorga‐Simón, E. N., Rojas, A. L., & Hierro, A. (2024) · Protein Science · doi:10.1002/pro.4980 · Cited by 15

Anti-inflammatory effects of banana (Musa balbisiana) peel extract on acne vulgaris: In vivo and in silico study

Savitri, D., Wahyuni, S., Bukhari, A., Djawad, K., Hatta, M., Riyanto, P., Bahar, B., Wahab, S., Hamid, F., & Rifai, Y. (2023) · Journal of Taibah University Medical Sciences · doi:10.1016/j.jtumed.2023.07.008 · Cited by 13

Proteome profiling of enriched membrane-associated proteins unraveled a novel sophorose and cello-oligosaccharide transporter in Trichoderma reesei

Nogueira, K. M. V., Mendes, V., Kamath, K. S., Cheruku, A., Oshiquiri, L. H., de Paula, R. G., Carraro, C., Pedersoli, W. R., Pereira, L. M. S., Vieira, L. C., et al. (2024) · Microbial Cell Factories · doi:10.1186/s12934-023-02279-9 · Cited by 12

Deciphering the RNA-binding protein network during endosomal mRNA transport

Devan, S.-K., Shanmugasundaram, S., Müntjes, K., Postma, J., Smits, S. H. J., Altegoer, F., & Feldbrügge, M. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2404091121 · Cited by 11

The structure of the Orm2-containing serine palmitoyltransferase complex reveals distinct inhibitory potentials of yeast Orm proteins

Körner, C., Schäfer, J.-H., Esch, B. M., Parey, K., Walter, S., Teis, D., Januliene, D., Schmidt, O., Moeller, A., & Fröhlich, F. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114627 · Cited by 10

Structure of the yeast ceramide synthase

Schäfer, J.-H., Clausmeyer, L., Körner, C., Esch, B. M., Wolf, V. N., Sapia, J., Ahmed, Y., Walter, S., Vanni, S., Januliene, D., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01415-2 · Cited by 10

Water-soluble 4-(dimethylaminomethyl)heliomycin exerts greater antitumor effects than parental heliomycin by targeting the tNOX-SIRT1 axis and apoptosis in oral cancer cells

(2024) · doi:10.7554/elife.87873.3 · Cited by 6

DrugDomain : The evolutionary context of drugs and small molecules bound to domains

Medvedev, K. E., Schaeffer, R. D., & Grishin, N. V. (2024) · Protein Science · doi:10.1002/pro.5116 · Cited by 6

Broadly potent spike-specific human monoclonal antibodies inhibit SARS-CoV-2 Omicron sub-lineages

Walker, M. R., Underwood, A., Björnsson, K. H., Raghavan, S. S. R., Bassi, M. R., Binderup, A., Pham, L. V., Ramirez, S., Pinholt, M., Dagil, R., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-06951-7 · Cited by 6

DNA-encoded library screening uncovers potent DNMT2 inhibitors targeting a cryptic allosteric binding site

Frey, A. F., Schwan, M., Weldert, A. C., Kadenbach, V., Kopp, J., Nidoieva, Z., Zimmermann, R. A., Gleue, L., Zimmer, C., Jörg, M., et al. (2025) · iScience · doi:10.1016/j.isci.2025.113300 · Cited by 5

Computational simulations of microalgae-derived bioactive compounds as a novel inhibitor against B-Raf V600E driven melanoma

Prasetiya, F. S., Destiarani, W., Prihastaningtyas, I. R. C., Agung, M. U. K., & Yusuf, M. (2023) · Journal of Applied Pharmaceutical Science · doi:10.7324/japs.2023.10012 · Cited by 3

Canonical and Alternative Auxin Signaling Systems in Mono-, Di-, and Tetraploid Potatoes

Lomin, S. N., Kolachevskaya, O. O., Arkhipov, D. V., & Romanov, G. A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411408 · Cited by 3

Design principles of a membrane-spanning ubiquitin ligase

Williams, C., Nocka, L. M., Hedger, G., Parashara, P., Pardon, E., Latorraca, N. R., Pusapati, G. V., Sarkar, P., Lartey, D., Gao, L., et al. (2026) · Molecular Cell · doi:10.1016/j.molcel.2026.05.001 · Cited by 3

Reprogramming of bacterial virulence by lysine acetylation

Schmöker, O., Girbardt, B., Schulze, S., Palm, G. J., Berndt, L., Hoppen, J., Kara, N., Schöps, X., Al-Abdulla, R., Garz, K., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-72244-8 · Cited by 2

Visualizing the mechanism of quinol oxidation and inhibition of a bd -type oxidase using cryo-EM

van der Velden, T. T., Kayastha, K., Pelser, F., Brünle, S., & Jeuken, L. J. C. (2026) · Science Advances · doi:10.1126/sciadv.aec9946 · Cited by 2

Water-soluble 4-(dimethylaminomethyl)heliomycin exerts greater antitumor effects than parental heliomycin by targeting the tNOX-SIRT1 axis and apoptosis in oral cancer cells

(2023) · doi:10.7554/elife.87873 · Cited by 2

Distribution and molecular evolution of the anti-CRISPR family AcrIF7

Figueroa, W., Cazares, A., Cazares, D., Wu, Y., de la Cruz, A., Welch, M., Kameyama, L., Nobrega, F. L., & Guarneros, G. (2023) · PLOS Biology · doi:10.1371/journal.pbio.3002072 · Cited by 2

Unveiling novel hyperglycosylated analog of human erythropoietin: A comprehensive computational exploration

Thahsin, N., Khan, K. I., Sarwar, A. N. M. R., Sakib, M. N., & Rahman, M. S. (2025) · Computational and Structural Biotechnology Reports · doi:10.1016/j.csbr.2024.100029 · Cited by 2

Structure of the human systemic RNAi defective transmembrane protein 1 (hSIDT1) reveals the conformational flexibility of its lipid binding domain

(2024) · doi:10.26508/lsa.202402624 · Cited by 2

De novo protein–ligand design including protein flexibility and conformational adaptation

Agamia, J., & Zacharias, M. (2026) · Bioinformatics · doi:10.1093/bioinformatics/btag027 · Cited by 2

Identification of interaction partners of outer inflammatory protein A: Computational and experimental insights into how Helicobacter pylori infects host cells

Akcelik-Deveci, S., Kılıç, E., Mansur-Ozen, N., Timucin, E., Buyukcolak, Y., & Oktem-Okullu, S. (2024) · PLOS ONE · doi:10.1371/journal.pone.0300557 · Cited by 2

A unique inhibitor conformation selectively targets the DNA polymerase PolC of Gram-positive priority pathogens

Urem, M., Friggen, A. H., Musch, N., Silverman, M. H., Swain, C. J., Barbachyn, M. R., Mortin, L. I., Yu, X., DeLuccia, R. J., Lamers, M. H., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-65324-8 · Cited by 2

Elucidating the binding specificity of interactive compounds targeting ATP-binding cassette subfamily G member 2 (ABCG2)

Kumar, P., Kumari, I., Prasad, R., Ray, S., Banerjee, A., & Prakash, A. (2025) · Molecular Diversity · doi:10.1007/s11030-024-11078-2 · Cited by 1

Dimerization of MilM Is Essential for Catalyzing the Pyridoxal-5′-phosphate (PLP)-Dependent Cγ-Hydroxylation of l -Arginine during Mildiomycin Biosynthesis

(2026) · doi:10.1021/acs.biochem.6c00271 · Cited by 1

DrugDomain 2.0: Comprehensive database of protein domains-ligands/drugs interactions across the whole Protein Data Bank

Medvedev, K. E., Schaeffer, R. D., & Grishin, N. V. (2025) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2025.09.018 · Cited by 1

Structure and catalytic mechanism of methylisocitrate lyase, a potential drug target against Coxiella burnetii

Stuart, W. S., Jenkins, C. H., Ireland, P. M., Isupov, M. N., Norville, I. H., & Harmer, N. J. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108517 · Cited by 1

Investigating the ATP-binding pocket of CX3CL1-binding protein 2 using in silico approach

Kumari, R., Kaur, S., Hora, R., & Mishra, P. C. (2024) · Journal of Proteins and Proteomics · doi:10.1007/s42485-024-00133-z

Water-soluble 4-(dimethylaminomethyl)heliomycin exerts greater antitumor effects than parental heliomycin by targeting the tNOX-SIRT1 axis and apoptosis in oral cancer cells

Islam, A., Chang, Y.-C., Chen, X.-C., Weng, C.-W., Chen, C.-Y., Wang, C.-W., Chen, M.-K., Tikhomirov, A. S., Shchekotikhin, A. E., & Chueh, P. J. (2023) · doi:10.1101/2023.03.29.534690

Integrative network-based construction of ecologically relevant computational adverse outcome pathways for organic mercury-induced toxicity

Madgaonkar, S. R., Chivukula, N., Garisetti, V., Marigoudar, S. R., Sharma, K. V., & Samal, A. (2026) · Environmental Toxicology and Chemistry · doi:10.1093/etojnl/vgag026

Water-soluble 4-(dimethylaminomethyl)heliomycin exerts greater antitumor effects than parental heliomycin by targeting the tNOX-SIRT1 axis and apoptosis in oral cancer cells

Islam, A., Chang, Y.-C., Chen, X.-C., Weng, C.-W., Chen, C.-Y., Wang, C.-W., Chen, M.-K., Tikhomirov, A. S., Shchekotikhin, A. E., & Chueh, P. J. (2024) · doi:10.7554/elife.87873.2