Collaboration gets the most out of software

PHENIX : a comprehensive Python-based system for macromolecular structure solution

Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716

Phaser crystallographic software

McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612

Overview of the CCP 4 suite and current developments

Winn, M. D., Ballard, C. C., Cowtan, K. D., Dodson, E. J., Emsley, P., Evans, P. R., Keegan, R. M., Krissinel, E. B., Leslie, A. G. W., McCoy, A., et al. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910045749 · Cited by 12,353

Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., Graham, B. S., & McLellan, J. S. (2020) · Science · doi:10.1126/science.abb2507 · Cited by 8,897

Protein Data Bank: the single global archive for 3D macromolecular structure data

wwPDB consortium, Burley, S. K., Berman, H. M., Bhikadiya, C., Bi, C., Chen, L., Costanzo, L. D., Christie, C., Duarte, J. M., Dutta, S., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gky949 · Cited by 1,163

Distinct conformational states of SARS-CoV-2 spike protein

Cai, Y., Zhang, J., Xiao, T., Peng, H., Sterling, S. M., Walsh, R. M., Rawson, S., Rits-Volloch, S., & Chen, B. (2020) · Science · doi:10.1126/science.abd4251 · Cited by 1,221

Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen

Pallesen, J., Wang, N., Corbett, K. S., Wrapp, D., Kirchdoerfer, R. N., Turner, H. L., Cottrell, C. A., Becker, M. M., Wang, L., Shi, W., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707304114 · Cited by 1,073

Design of protein-binding proteins from the target structure alone

Cao, L., Coventry, B., Goreshnik, I., Huang, B., Sheffler, W., Park, J. S., Jude, K. M., Marković, I., Kadam, R. U., Verschueren, K. H. G., et al. (2022) · Nature · doi:10.1038/s41586-022-04654-9 · Cited by 577

Structural Basis for Potent Neutralization of Betacoronaviruses by Single-Domain Camelid Antibodies

Wrapp, D., De Vlieger, D., Corbett, K. S., Torres, G. M., Wang, N., Van Breedam, W., Roose, K., van Schie, L., Hoffmann, M., Pöhlmann, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.04.031 · Cited by 610

Plasticity in binding confers selectivity in ligand-induced protein degradation

Nowak, R. P., DeAngelo, S. L., Buckley, D., He, Z., Donovan, K. A., An, J., Safaee, N., Jedrychowski, M. P., Ponthier, C. M., Ishoey, M., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0055-y · Cited by 615

De novo design of potent and selective mimics of IL-2 and IL-15

Silva, D.-A., Yu, S., Ulge, U. Y., Spangler, J. B., Jude, K. M., Labão-Almeida, C., Ali, L. R., Quijano-Rubio, A., Ruterbusch, M., Leung, I., et al. (2019) · Nature · doi:10.1038/s41586-018-0830-7 · Cited by 531

Crystal structure of the human σ1 receptor

Schmidt, H. R., Zheng, S., Gurpinar, E., Koehl, A., Manglik, A., & Kruse, A. C. (2016) · Nature · doi:10.1038/nature17391 · Cited by 482

Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway

Saxton, R. A., Knockenhauer, K. E., Wolfson, R. L., Chantranupong, L., Pacold, M. E., Wang, T., Schwartz, T. U., & Sabatini, D. M. (2016) · Science · doi:10.1126/science.aad2087 · Cited by 457

Structure-based membrane dome mechanism for Piezo mechanosensitivity

Guo, Y. R., & MacKinnon, R. (2017) · eLife · doi:10.7554/elife.33660 · Cited by 446

Akkermansia muciniphila phospholipid induces homeostatic immune responses

Bae, M., Cassilly, C. D., Liu, X., Park, S.-M., Tusi, B. K., Chen, X., Kwon, J., Filipčík, P., Bolze, A. S., Liu, Z., et al. (2022) · Nature · doi:10.1038/s41586-022-04985-7 · Cited by 413

NLRP3 cages revealed by full-length mouse NLRP3 structure control pathway activation

Andreeva, L., David, L., Rawson, S., Shen, C., Pasricha, T., Pelegrin, P., & Wu, H. (2021) · Cell · doi:10.1016/j.cell.2021.11.011 · Cited by 292

Structure of cytoplasmic ring of nuclear pore complex by integrative cryo-EM and AlphaFold

Fontana, P., Dong, Y., Pi, X., Tong, A. B., Hecksel, C. W., Wang, L., Fu, T.-M., Bustamante, C., & Wu, H. (2022) · Science · doi:10.1126/science.abm9326 · Cited by 195

Structural basis for IL-12 and IL-23 receptor sharing reveals a gateway for shaping actions on T versus NK cells

Glassman, C. R., Mathiharan, Y. K., Jude, K. M., Su, L., Panova, O., Lupardus, P. J., Spangler, J. B., Ely, L. K., Thomas, C., Skiniotis, G., et al. (2021) · Cell · doi:10.1016/j.cell.2021.01.018 · Cited by 181

Eicosanoid signalling blockade protects middle-aged mice from severe COVID-19

Wong, L.-Y. R., Zheng, J., Wilhelmsen, K., Li, K., Ortiz, M. E., Schnicker, N. J., Thurman, A., Pezzulo, A. A., Szachowicz, P. J., Li, P., et al. (2022) · Nature · doi:10.1038/s41586-022-04630-3 · Cited by 178

Assessment of contact predictions in CASP12: Co‐evolution and deep learning coming of age

Schaarschmidt, J., Monastyrskyy, B., Kryshtafovych, A., & Bonvin, A. M. J. J. (2018) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.25407 · Cited by 177

Reconstitution and visualization of HIV-1 capsid-dependent replication and integration in vitro

Christensen, D. E., Ganser-Pornillos, B. K., Johnson, J. S., Pornillos, O., & Sundquist, W. I. (2020) · Science · doi:10.1126/science.abc8420 · Cited by 150

Structural basis and regulation of the reductive stress response

Manford, A. G., Mena, E. L., Shih, K. Y., Gee, C. L., McMinimy, R., Martínez-González, B., Sherriff, R., Lew, B., Zoltek, M., Rodríguez-Pérez, F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.09.002 · Cited by 152

Deconstruction of the Ras switching cycle through saturation mutagenesis

Bandaru, P., Shah, N. H., Bhattacharyya, M., Barton, J. P., Kondo, Y., Cofsky, J. C., Gee, C. L., Chakraborty, A. K., Kortemme, T., Ranganathan, R., et al. (2017) · eLife · doi:10.7554/elife.27810 · Cited by 117

KRAS G13D sensitivity to neurofibromin-mediated GTP hydrolysis

Rabara, D., Tran, T. H., Dharmaiah, S., Stephens, R. M., McCormick, F., Simanshu, D. K., & Holderfield, M. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1908353116 · Cited by 128

Structural basis of Gabija anti-phage defence and viral immune evasion

Antine, S. P., Johnson, A. G., Mooney, S. E., Leavitt, A., Mayer, M. L., Yirmiya, E., Amitai, G., Sorek, R., & Kranzusch, P. J. (2024) · Nature · doi:10.1038/s41586-023-06855-2 · Cited by 125

Acute pharmacological degradation of Helios destabilizes regulatory T cells

Wang, E. S., Verano, A. L., Nowak, R. P., Yuan, J. C., Donovan, K. A., Eleuteri, N. A., Yue, H., Ngo, K. H., Lizotte, P. H., Gokhale, P. C., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00802-w · Cited by 124

Structure and Dynamics of PD-L1 and an Ultra-High-Affinity PD-1 Receptor Mutant

Pascolutti, R., Sun, X., Kao, J., Maute, R. L., Ring, A. M., Bowman, G. R., & Kruse, A. C. (2016) · Structure · doi:10.1016/j.str.2016.06.026 · Cited by 102

Sph3 Is a Glycoside Hydrolase Required for the Biosynthesis of Galactosaminogalactan in Aspergillus fumigatus

Bamford, N. C., Snarr, B. D., Gravelat, F. N., Little, D. J., Lee, M. J., Zacharias, C. A., Chabot, J. C., Geller, A. M., Baptista, S. D., Baker, P., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.679050 · Cited by 102

Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients

Miller-Vedam, L. E., Bräuning, B., Popova, K. D., Schirle Oakdale, N. T., Bonnar, J. L., Prabu, J. R., Boydston, E. A., Sevillano, N., Shurtleff, M. J., Stroud, R. M., et al. (2020) · eLife · doi:10.7554/elife.62611 · Cited by 87

iSEE: Interface structure, evolution, and energy-based machine learning predictor of binding affinity changes upon mutations

Geng, C., Vangone, A., Folkers, G. E., Xue, L. C., & Bonvin, A. M. J. J. (2019) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.25630 · Cited by 82

Structural principles of B cell antigen receptor assembly

Dong, Y., Pi, X., Bartels-Burgahn, F., Saltukoglu, D., Liang, Z., Yang, J., Alt, F. W., Reth, M., & Wu, H. (2022) · Nature · doi:10.1038/s41586-022-05412-7 · Cited by 82

In vivo clonal expansion and phenotypes of hypocretin-specific CD4+ T cells in narcolepsy patients and controls

Jiang, W., Birtley, J. R., Hung, S.-C., Wang, W., Chiou, S.-H., Macaubas, C., Kornum, B., Tian, L., Huang, H., Adler, L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13234-x · Cited by 58

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

Cryptochrome–Timeless structure reveals circadian clock timing mechanisms

Lin, C., Feng, S., DeOliveira, C. C., & Crane, B. R. (2023) · Nature · doi:10.1038/s41586-023-06009-4 · Cited by 51

Machine Learning Modeling of Protein-Intrinsic Features Predicts Tractability of Targeted Protein Degradation

Zhang, W., Roy Burman, S. S., Chen, J., Donovan, K. A., Cao, Y., Shu, C., Zhang, B., Zeng, Z., Gu, S., Zhang, Y., et al. (2022) · Genomics, Proteomics & Bioinformatics · doi:10.1016/j.gpb.2022.11.008 · Cited by 51

Deciphering Bacteriophage T5 Host Recognition Mechanism and Infection Trigger

Degroux, S., Effantin, G., Linares, R., Schoehn, G., & Breyton, C. (2023) · Journal of Virology · doi:10.1128/jvi.01584-22 · Cited by 49

Targeted Degradation of the Oncogenic Phosphatase SHP2

Vemulapalli, V., Donovan, K. A., Seegar, T. C. M., Rogers, J. M., Bae, M., Lumpkin, R. J., Cao, R., Henke, M. T., Ray, S. S., Fischer, E. S., et al. (2021) · Biochemistry · doi:10.1021/acs.biochem.1c00377 · Cited by 43

FOXP3 recognizes microsatellites and bridges DNA through multimerization

Zhang, W., Leng, F., Wang, X., Ramirez, R. N., Park, J., Benoist, C., & Hur, S. (2023) · Nature · doi:10.1038/s41586-023-06793-z · Cited by 42

Defluorination Capability of l ‐2‐Haloacid Dehalogenases in the HAD‐Like Hydrolase Superfamily Correlates with Active Site Compactness

Chan, P. W. Y., Chakrabarti, N., Ing, C., Halgas, O., To, T. K. W., Wälti, M., Petit, A., Tran, C., Savchenko, A., Yakunin, A. F., et al. (2022) · ChemBioChem · doi:10.1002/cbic.202100414 · Cited by 41

Fungal-selective resorcylate aminopyrazole Hsp90 inhibitors: optimization of whole-cell anticryptococcal activity and insights into the structural origins of cryptococcal selectivity

Marcyk, P. T., LeBlanc, E. V., Kuntz, D. A., Xue, A., Ortiz, F., Trilles, R., Bengtson, S., Kenney, T. M. G., Huang, D. S., Robbins, N., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01777 · Cited by 40

Structural basis for the differential interaction of Scribble PDZ domains with the guanine nucleotide exchange factor β-PIX

Lim, K. Y. B., Gödde, N. J., Humbert, P. O., & Kvansakul, M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.799452 · Cited by 34

Breakage of the oligomeric CaMKII hub by the regulatory segment of the kinase

Karandur, D., Bhattacharyya, M., Xia, Z., Lee, Y. K., Muratcioglu, S., McAffee, D., McSpadden, E. D., Qiu, B., Groves, J. T., Williams, E. R., et al. (2020) · eLife · doi:10.7554/elife.57784 · Cited by 35

Cryo-EM structures of an LRRC8 chimera with native functional properties reveal heptameric assembly

Takahashi, H., Yamada, T., Denton, J. S., Strange, K., & Karakas, E. (2023) · eLife · doi:10.7554/elife.82431 · Cited by 35

Heterogeneity of tethered agonist signaling in adhesion G protein-coupled receptors

(2024) · doi:10.1016/j.chembiol.2024.03.004 · Cited by 33

Structural Determinants for Binding of Sorting Nexin 17 (SNX17) to the Cytoplasmic Adaptor Protein Krev Interaction Trapped 1 (KRIT1)

Stiegler, A. L., Zhang, R., Liu, W., & Boggon, T. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.584011 · Cited by 32

An amphipathic helix in Brl1 is required for nuclear pore complex biogenesis in S. cerevisiae

(2022) · doi:10.7554/elife.78385 · Cited by 29

Drosophila melanogaster Guk-holder interacts with the Scribbled PDZ1 domain and regulates epithelial development with Scribbled and Discs Large

Caria, S., Magtoto, C. M., Samiei, T., Portela, M., Lim, K. Y. B., How, J. Y., Stewart, B. Z., Humbert, P. O., Richardson, H. E., & Kvansakul, M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.817528 · Cited by 28

Automated multiconformer model building for X-ray crystallography and cryo-EM

Wankowicz, S. A., Ravikumar, A., Sharma, S., Riley, B., Raju, A., Hogan, D. W., Flowers, J., van den Bedem, H., Keedy, D. A., & Fraser, J. S. (2024) · eLife · doi:10.7554/elife.90606 · Cited by 28

Structural basis for non-canonical integrin engagement by Bordetella adenylate cyclase toxin

Goldsmith, J. A., DiVenere, A. M., Maynard, J. A., & McLellan, J. S. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111196 · Cited by 28

Conformational changes of the clamp of the protein translocation ATPase SecA

Chen, Y., Bauer, B. W., Rapoport, T. A., & Gumbart, J. C. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.05.003 · Cited by 27

Cryo-EM structure of the human somatostatin receptor 2 complex with its agonist somatostatin delineates the ligand-binding specificity

(2022) · doi:10.7554/elife.76823 · Cited by 24

Structure of the mature Rous sarcoma virus lattice reveals a role for IP6 in the formation of the capsid hexamer

Obr, M., Ricana, C. L., Nikulin, N., Feathers, J.-P. R., Klanschnig, M., Thader, A., Johnson, M. C., Vogt, V. M., Schur, F. K. M., & Dick, R. A. (2021) · Nature Communications · doi:10.1038/s41467-021-23506-0 · Cited by 23

A membrane protein complex docking benchmark

Koukos, P. I., Faro, I., van Noort, C. W., & Bonvin, A. M. J. J. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.11.005 · Cited by 23

Polymerization of ZBTB transcription factors regulates chromatin occupancy

Park, P. M. C., Park, J., Brown, J., Hunkeler, M., Roy Burman, S. S., Donovan, K. A., Yoon, H., Nowak, R. P., Słabicki, M., Ebert, B. L., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.06.010 · Cited by 22

Structure and flexibility of the yeast NuA4 histone acetyltransferase complex

Zukin, S. A., Marunde, M. R., Popova, I. K., Soczek, K. M., Nogales, E., & Patel, A. B. (2022) · eLife · doi:10.7554/elife.81400 · Cited by 22

Structural basis for activation of Arf1 at the Golgi complex

(2022) · doi:10.1016/j.celrep.2022.111282 · Cited by 22

Crystal structure of the human Scribble PDZ 1 domain bound to the PDZ ‐binding motif of APC

How, J. Y., Caria, S., Humbert, P. O., & Kvansakul, M. (2019) · FEBS Letters · doi:10.1002/1873-3468.13329 · Cited by 19

Molecular basis of C-S bond cleavage in the glycyl radical enzyme isethionate sulfite-lyase

Dawson, C. D., Irwin, S. M., Backman, L. R. F., Le, C., Wang, J. X., Vennelakanti, V., Yang, Z., Kulik, H. J., Drennan, C. L., & Balskus, E. P. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2021.03.001 · Cited by 21

Structural basis for competitive binding of productive and degradative co-transcriptional effectors to the nuclear cap-binding complex

(2024) · doi:10.1016/j.celrep.2023.113639 · Cited by 20

The TPR domain of PgaA is a multifunctional scaffold that binds PNAG and modulates PgaB-dependent polymer processing

Pfoh, R., Subramanian, A. S., Huang, J., Little, D. J., Forman, A., DiFrancesco, B. R., Balouchestani-Asli, N., Kitova, E. N., Klassen, J. S., Pomès, R., et al. (2022) · PLOS Pathogens · doi:10.1371/journal.ppat.1010750 · Cited by 17

Structure and organization of full-length epidermal growth factor receptor in extracellular vesicles by cryo-electron tomography

Gonzalez-Magaldi, M., Gullapalli, A., Papoulas, O., Liu, C., Leung, A. Y.-H., Guo, L., Brilot, A. F., Marcotte, E. M., Ke, Z., & Leahy, D. J. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2424678122 · Cited by 17

Structure and function of the human mitochondrial MRS2 channel

(2024) · doi:10.1038/s41594-024-01420-5 · Cited by 17

A communication hub for phosphoregulation of kinetochore-microtubule attachment

(2024) · doi:10.1016/j.cub.2024.04.067 · Cited by 17

Molecular basis for shifted receptor recognition by an encephalitic arbovirus

Fan, X., Li, W., Oros, J., Plante, J. A., Mitchell, B. M., Plung, J. S., Basu, H., Nagappan-Chettiar, S., Boeckers, J. M., Tjang, L. V., et al. (2025) · Cell · doi:10.1016/j.cell.2025.03.029 · Cited by 17

Metal cofactor stabilization by a partner protein is a widespread strategy employed for amidase activation

Page, J. E., Skiba, M. A., Do, T., Kruse, A. C., & Walker, S. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2201141119 · Cited by 12

Structural organization of p62 filaments and the cellular ultrastructure of calcium-rich p62-enwrapped lipid droplet cargo

Berkamp, S., Jungbluth, L., Katranidis, A., Mostafavi, S., Korculanin, O., Lu, P.-H., Ickert, L., Dierig, M. M., Sharma, L., Thukral, L., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-66785-7 · Cited by 12

Nanobody inhibitors of Plexin-B1 identify allostery in plexin–semaphorin interactions and signaling

Cowan, R., Trokter, M., Oleksy, A., Fedorova, M., Sawmynaden, K., Worzfeld, T., Offermanns, S., Matthews, D., Carr, M. D., & Hall, G. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104740 · Cited by 11

Pseudomonas aeruginosa AlgF is a protein–protein interaction mediator required for acetylation of the alginate exopolysaccharide

Low, K. E., Gheorghita, A. A., Tammam, S. D., Whitfield, G. B., Li, Y. E., Riley, L. M., Weadge, J. T., Caldwell, S. J., Chong, P. A., Walvoort, M. T. C., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105314 · Cited by 11

Structural mechanism of HP1⍺-dependent transcriptional repression and chromatin compaction

Sokolova, V., Miratsky, J., Svetlov, V., Brenowitz, M., Vant, J., Lewis, T. S., Dryden, K., Lee, G., Sarkar, S., Nudler, E., et al. (2024) · Structure · doi:10.1016/j.str.2024.09.013 · Cited by 11

Structural basis of aquaporin-4 autoantibody binding in neuromyelitis optica

Gupta, M., Khandelwal, N. K., Nelson, A., Hwang, P., Pourmal, S., Bennett, J. L., & Stroud, R. M. (2025) · Science Advances · doi:10.1126/sciadv.adq7560 · Cited by 11

Structure shows that the BIR2 domain of E3 ligase XIAP binds across the RIPK2 kinase dimer interface

Lethier, M., Huard, K., Hons, M., Favier, A., Brutscher, B., Boeri Erba, E., Abbott, D. W., Cusack, S., & Pellegrini, E. (2023) · Life Science Alliance · doi:10.26508/lsa.202201784 · Cited by 11

Octahedral small virus-like particles of dengue virus type 2

Johnson, A., Dodes Traian, M., Walsh, R. M., Jenni, S., & Harrison, S. C. (2025) · Journal of Virology · doi:10.1128/jvi.01809-24 · Cited by 9

Microtubules in the axon are GDP bound but adopt a stable GTP-like expanded state

Zehr, E. A., Sun, S., Sarbanes, S. L., & Roll-Mecak, A. (2026) · Nature Structural & Molecular Biology · doi:10.1038/s41594-026-01787-7 · Cited by 8

Uncovering Protein Ensembles: Automated Multiconformer Model Building for X-ray Crystallography and Cryo-EM

(2023) · doi:10.1101/2023.06.28.546963 · Cited by 8

Membrane recruitment of the polarity protein Scribble by the cell adhesion receptor TMIGD1

Thüring, E.-M., Hartmann, C., Maddumage, J. C., Javorsky, A., Michels, B. E., Gerke, V., Banks, L., Humbert, P. O., Kvansakul, M., & Ebnet, K. (2023) · Communications Biology · doi:10.1038/s42003-023-05088-3 · Cited by 7

Molecular mechanism of PP2A/B55α phosphatase inhibition by IER5

Cao, R., Jones, D. T. D., Pan, L., Yang, A., Wang, S., Padi, S. K. R., Rawson, S., Aster, J. C., & Blacklow, S. C. (2025) · Cell Chemical Biology · doi:10.1016/j.chembiol.2025.03.004 · Cited by 7

Degron-independent recruitment of KAT2A expands the target space of CRBN molecular glues

Ojeda, S., Wang, M., Baek, K., Bourgeois, W., Sommerschield, A., Yue, H., Metivier, R. J., Karagiannis, P., Levitz, T. S., Xiong, Y., et al. (2026) · Science · doi:10.1126/science.aef5391 · Cited by 5

Cryo-electron microscopy reveals a single domain antibody with a unique binding epitope on fibroblast activation protein alpha

Xu, Z., Sinha, A., Pandya, D. N., Schnicker, N. J., & Wadas, T. J. (2025) · RSC Chemical Biology · doi:10.1039/d4cb00267a · Cited by 5

Structural insight into guanylyl cyclase receptor hijacking of the kinase–Hsp90 regulatory mechanism

Caveney, N. A., Tsutsumi, N., & Garcia, K. C. (2023) · eLife · doi:10.7554/elife.86784 · Cited by 5

Structure and flexibility of the DNA polymerase holoenzyme of vaccinia virus

Burmeister, W. P., Boutin, L., Balestra, A. C., Gröger, H., Ballandras-Colas, A., Hutin, S., Kraft, C., Grimm, C., Böttcher, B., Fischer, U., et al. (2024) · PLOS Pathogens · doi:10.1371/journal.ppat.1011652 · Cited by 3

Distinct quaternary states, intermediates, and autoinhibition during loading of the DnaB-replicative helicase by the phage λP helicase loader

Shatarupa, A., Brown, D., Olinares, P. D. B., Chase, J., Isiorho, E., Chait, B. T., & Jeruzalmi, D. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1139 · Cited by 3

The TPR domain of PgaA is a multifunctional scaffold that binds PNAG and modulates PgaB-dependent polymer processing

(2023) · doi:10.32920/24746796 · Cited by 1

Structural insight into guanylyl cyclase receptor hijacking of the kinase–Hsp90 regulatory mechanism

Caveney, N. A., Tsutsumi, N., & Garcia, K. C. (2023) · doi:10.7554/elife.86784.2

The TPR domain of PgaA is a multifunctional scaffold that binds PNAG and modulates PgaB-dependent polymer processing

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