UCSF Chimera—A visualization system for exploratory research and analysis

PROSITE: a documented database using patterns and profiles as motif descriptors

Sigrist, C. J. A. (2002) · Briefings in Bioinformatics · doi:10.1093/bib/3.3.265 · Cited by 913

Regulation of RAS palmitoyltransferases by accessory proteins and palmitoylation

Yang, A., Liu, S., Zhang, Y., Chen, J., Fan, Y., Wang, F., Zou, Y., Feng, S., Wu, J., & Hu, Q. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01183-5 · Cited by 38

From primordial clocks to circadian oscillators

Pitsawong, W., Pádua, R. A. P., Grant, T., Hoemberger, M., Otten, R., Bradshaw, N., Grigorieff, N., & Kern, D. (2023) · Nature · doi:10.1038/s41586-023-05836-9 · Cited by 37

The Arp1/11 minifilament of dynactin primes the endosomal Arp2/3 complex

Fokin, A. I., David, V., Oguievetskaia, K., Derivery, E., Stone, C. E., Cao, L., Rocques, N., Molinie, N., Henriot, V., Aumont-Nicaise, M., et al. (2021) · Science Advances · doi:10.1126/sciadv.abd5956 · Cited by 37

A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins

Aiyer, S., Swapna, G. V. T., Ma, L.-C., Liu, G., Hao, J., Chalmers, G., Jacobs, B. C., Montelione, G. T., & Roth, M. J. (2021) · Structure · doi:10.1016/j.str.2021.01.010 · Cited by 35

Ranking power of the SQM/COSMO scoring function on carbonic anhydrase II-inhibitor complexes.

Pecina, A., Brynda, J., Vrzal, L., Gnanasekaran, R., Hořejší, M., Eyrilmez, S. M., Řezáč, J., Lepšík, M., Řezáčová, P., Hobza, P., et al. (2018) · ChemPhysChem · doi:10.1002/cphc.201701104 · Cited by 36

Nano-scale resolution of native retinal rod disk membranes reveals differences in lipid composition

Sander, C. L., Sears, A. E., Pinto, A. F. M., Choi, E. H., Kahremany, S., Gao, F., Salom, D., Jin, H., Pardon, E., Suh, S., et al. (2021) · Journal of Cell Biology · doi:10.1083/jcb.202101063 · Cited by 36

A modular DNA origami nanocompartment for engineering a cell-free, protein unfolding and degradation pathway

Huang, J., Jaekel, A., van den Boom, J., Podlesainski, D., Elnaggar, M., Heuer-Jungemann, A., Kaiser, M., Meyer, H., & Saccà, B. (2024) · Nature Nanotechnology · doi:10.1038/s41565-024-01738-7 · Cited by 35

‘Generating chromosome geometries in a minimal cell from cryo-electron tomograms and chromosome conformation capture maps’

Gilbert, B. R., Thornburg, Z. R., Lam, V., Rashid, F.-Z. M., Glass, J. I., Villa, E., Dame, R. T., & Luthey-Schulten, Z. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.644133 · Cited by 30

Affinity maturation, humanization, and co-crystallization of a rabbit anti-human ROR2 monoclonal antibody for therapeutic applications

Goydel, R. S., Weber, J., Peng, H., Qi, J., Soden, J., Freeth, J., Park, H., & Rader, C. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.012791 · Cited by 34

Pharmacological hallmarks of allostery at the M4 muscarinic receptor elucidated through structure and dynamics

Vuckovic, Z., Wang, J., Pham, V., Mobbs, J. I., Belousoff, M. J., Bhattarai, A., Burger, W. A., Thompson, G., Yeasmin, M., Nawaratne, V., et al. (2023) · eLife · doi:10.7554/elife.83477 · Cited by 34

Structural basis for plasmid restriction by SMC JET nuclease

Roisné-Hamelin, F., Liu, H. W., Taschner, M., Li, Y., & Gruber, S. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.01.009 · Cited by 34

Cryo-EM Structure of a Novel Calicivirus, Tulane Virus

Yu, G., Zhang, D., Guo, F., Tan, M., Jiang, X., & Jiang, W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0059817 · Cited by 34

Hepatic SREBP signaling requires SPRING to govern systemic lipid metabolism in mice and humans

Hendrix, S., Kingma, J., Ottenhoff, R., Valiloo, M., Svecla, M., Zijlstra, L. F., Sachdev, V., Kovac, K., Levels, J. H. M., Jongejan, A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40943-1 · Cited by 34

Structural mechanism of outer kinetochore Dam1-Ndc80 complex assembly on microtubules

Muir, K. W., Batters, C., Dendooven, T., Yang, J., Zhang, Z., Burt, A., & Barford, D. (2023) · Science · doi:10.1126/science.adj8736 · Cited by 34

The giant mimivirus 1.2 Mb genome is elegantly organized into a 30-nm diameter helical protein shield

Villalta, A., Schmitt, A., Estrozi, L. F., Quemin, E. R., Alempic, J.-M., Lartigue, A., Pražák, V., Belmudes, L., Vasishtan, D., Colmant, A. M., et al. (2022) · eLife · doi:10.7554/elife.77607 · Cited by 34

A Docking Model Based on Mass Spectrometric and Biochemical Data Describes Phage Packaging Motor Incorporation

Fu, C.-Y., Uetrecht, C., Kang, S., Morais, M. C., Heck, A. J. R., Walter, M. R., & Prevelige, P. E. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900625-mcp200 · Cited by 33

Structure comparison of the chimeric AAV2.7m8 vector with parental AAV2

Bennett, A., Keravala, A., Makal, V., Kurian, J., Belbellaa, B., Aeran, R., Tseng, Y.-S., Sousa, D., Spear, J., Gasmi, M., et al. (2020) · Journal of Structural Biology · doi:10.1016/j.jsb.2019.107433 · Cited by 33

Autism-associated SHANK3 missense point mutations impact conformational fluctuations and protein turnover at synapses

Bucher, M., Niebling, S., Han, Y., Molodenskiy, D., Hassani Nia, F., Kreienkamp, H.-J., Svergun, D., Kim, E., Kostyukova, A. S., Kreutz, M. R., et al. (2021) · eLife · doi:10.7554/elife.66165 · Cited by 33

A cyclin-dependent kinase-mediated phosphorylation switch of disordered protein condensation

Valverde, J. M., Dubra, G., Phillips, M., Haider, A., Elena-Real, C., Fournet, A., Alghoul, E., Chahar, D., Andrés-Sanchez, N., Paloni, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42049-0 · Cited by 33

Cryo-EM structure of the inner ring from the Xenopus laevis nuclear pore complex

Huang, G., Zhan, X., Zeng, C., Liang, K., Zhu, X., Zhao, Y., Wang, P., Wang, Q., Zhou, Q., Tao, Q., et al. (2022) · Cell Research · doi:10.1038/s41422-022-00633-x · Cited by 33

Mapping and Identification of Antifungal Peptides in the Putative Antifungal Protein AfpB from the Filamentous Fungus Penicillium digitatum

Garrigues, S., Gandía, M., Borics, A., Marx, F., Manzanares, P., & Marcos, J. F. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00592 · Cited by 32

Rieske head domain dynamics and indazole-derivative inhibition of Candida albicans complex III

Di Trani, J. M., Liu, Z., Whitesell, L., Brzezinski, P., Cowen, L. E., & Rubinstein, J. L. (2022) · Structure · doi:10.1016/j.str.2021.08.006 · Cited by 32

Inhibition of ergosterol synthesis in Candida albicans by novel eugenol tosylate congeners targeting sterol 14α-demethylase (CYP51) enzyme

Lone, S. A., Khan, S., & Ahmad, A. (2020) · Archives of Microbiology · doi:10.1007/s00203-019-01781-2 · Cited by 32

Binding and sequestration of poison frog alkaloids by a plasma globulin

Alvarez-Buylla, A., Fischer, M.-T., Moya Garzon, M. D., Rangel, A. E., Tapia, E. E., Tanzo, J. T., Soh, H. T., Coloma, L. A., Long, J. Z., & O'Connell, L. A. (2023) · eLife · doi:10.7554/elife.85096 · Cited by 32

Proteasome activation is mediated via a functional switch of the Rpt6 C-terminal tail following chaperone-dependent assembly

Sokolova, V., Li, F., Polovin, G., & Park, S. (2015) · Scientific Reports · doi:10.1038/srep14909 · Cited by 31

Cryo-EM structure of the deltaretroviral intasome in complex with the PP2A regulatory subunit B56γ

Barski, M. S., Minnell, J. J., Hodakova, Z., Pye, V. E., Nans, A., Cherepanov, P., & Maertens, G. N. (2020) · Nature Communications · doi:10.1038/s41467-020-18874-y · Cited by 29

Cryo‐EM structures of human ABCA7 provide insights into its phospholipid translocation mechanisms

Le, L. T. M., Thompson, J. R., Dehghani‐Ghahnaviyeh, S., Pant, S., Dang, P. X., French, J. B., Kanikeyo, T., Tajkhorshid, E., & Alam, A. (2023) · The EMBO Journal · doi:10.15252/embj.2022111065 · Cited by 31

Cryo-EM structure of the HIV-1 Pol polyprotein provides insights into virion maturation

Harrison, J. J. E. K., Passos, D. O., Bruhn, J. F., Bauman, J. D., Tuberty, L., DeStefano, J. J., Ruiz, F. X., Lyumkis, D., & Arnold, E. (2022) · Science Advances · doi:10.1126/sciadv.abn9874 · Cited by 31

Structure and mechanism of NALCN-FAM155A-UNC79-UNC80 channel complex

Kang, Y., & Chen, L. (2022) · Nature Communications · doi:10.1038/s41467-022-30403-7 · Cited by 31

Structural basis of HIV-1 maturation inhibitor binding and activity

Sarkar, S., Zadrozny, K. K., Zadorozhnyi, R., Russell, R. W., Quinn, C. M., Kleinpeter, A., Ablan, S., Meshkin, H., Perilla, J. R., Freed, E. O., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36569-y · Cited by 28

Archaeal bundling pili of Pyrobaculum calidifontis reveal similarities between archaeal and bacterial biofilms

Wang, F., Cvirkaite-Krupovic, V., Krupovic, M., & Egelman, E. H. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2207037119 · Cited by 30

Safe and effective two-in-one replicon-and-VLP minispike vaccine for COVID-19: Protection of mice after a single immunization

Hennrich, A. A., Sawatsky, B., Santos-Mandujano, R., Banda, D. H., Oberhuber, M., Schopf, A., Pfaffinger, V., Wittwer, K., Riedel, C., Pfaller, C. K., et al. (2021) · PLOS Pathogens · doi:10.1371/journal.ppat.1009064 · Cited by 30

Nanodiamond integration into niosomes as an emerging and efficient gene therapy nanoplatform for central nervous system diseases

AL Qtaish, N., Gallego, I., Paredes, A. J., Villate-Beitia, I., Soto-Sánchez, C., Martínez-Navarrete, G., Sainz-Ramos, M., Lopez-Mendez, T. B., Fernández, E., Puras, G., et al. (2022) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.2c02182 · Cited by 29

Bile Salt Hydrolase Degrades β-Lactam Antibiotics and Confers Antibiotic Resistance on Lactobacillus paragasseri

Kusada, H., Arita, M., Tohno, M., & Tamaki, H. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.858263 · Cited by 29

Dps Functions as a Key Player in Bacterial Iron Homeostasis

Williams, S. M., & Chatterji, D. (2023) · ACS Omega · doi:10.1021/acsomega.3c03277 · Cited by 29

Extracellular domain of PepT1 interacts with TM1 to facilitate substrate transport

Shen, J., Hu, M., Fan, X., Ren, Z., Portioli, C., Yan, X., Rong, M., & Zhou, M. (2022) · Structure · doi:10.1016/j.str.2022.04.011 · Cited by 29

Discovery and characterization of potent pan-variant SARS-CoV-2 neutralizing antibodies from individuals with Omicron breakthrough infection

Guo, Y., Zhang, G., Yang, Q., Xie, X., Lu, Y., Cheng, X., Wang, H., Liang, J., Tang, J., Gao, Y., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39267-x · Cited by 28

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

Compounds from the marine sponge Cribrochalina vasculum offer a way to target IGF-1R mediated signaling in tumor cells

Zovko, A., Novak, M., Hååg, P., Kovalerchick, D., Holmlund, T., Färnegårdh, K., Ilan, M., Carmeli, S., Lewensohn, R., & Viktorsson, K. (2016) · Oncotarget · doi:10.18632/oncotarget.10361 · Cited by 28

Transcriptomic and genomic studies classify NKL54 as a histone deacetylase inhibitor with indirect influence on MEF2-dependent transcription

Minisini, M., Di Giorgio, E., Kerschbamer, E., Dalla, E., Faggiani, M., Franforte, E., Meyer-Almes, F.-J., Ragno, R., Antonini, L., Mai, A., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac081 · Cited by 28

Cryo-EM structure of the human Kv3.1 channel reveals gating control by the cytoplasmic T1 domain

Chi, G., Liang, Q., Sridhar, A., Cowgill, J. B., Sader, K., Radjainia, M., Qian, P., Castro-Hartmann, P., Venkaya, S., Singh, N. K., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29594-w · Cited by 28

Glucocorticoid receptor complexes form cooperatively with the Hsp90 co-chaperones Pp5 and FKBPs

Kaziales, A., Barkovits, K., Marcus, K., & Richter, K. (2020) · Scientific Reports · doi:10.1038/s41598-020-67645-8 · Cited by 24

Quantifying ERK2–protein interactions by fluorescence anisotropy: PEA-15 inhibits ERK2 by blocking the binding of DEJL domains

Callaway, K., Rainey, M. A., & Dalby, K. N. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.11.002 · Cited by 26

Antibody affinity maturation by computational design

Kuroda, D., & Tsumoto, K. (2018) · Methods in molecular biology · doi:10.1007/978-1-4939-8648-4_2 · Cited by 26

Best templates outperform homology models in predicting the impact of mutations on protein stability

Pak, M. A., & Ivankov, D. N. (2022) · Bioinformatics · doi:10.1093/bioinformatics/btac515 · Cited by 26

Anti-CRISPR AcrIIC5 is a dsDNA mimic that inhibits type II-C Cas9 effectors by blocking PAM recognition

(2023) · doi:10.1093/nar/gkad052 · Cited by 26

Structure of the yeast Swi/Snf complex in a nucleosome free state

Wang, C., Guo, Z., Zhan, X., Yang, F., Wu, M., & Zhang, X. (2020) · Nature Communications · doi:10.1038/s41467-020-17229-x · Cited by 25

Structural basis of mRNA decay by the human exosome–ribosome supercomplex

Kögel, A., Keidel, A., Loukeri, M.-J., Kuhn, C. C., Langer, L. M., Schäfer, I. B., & Conti, E. (2024) · Nature · doi:10.1038/s41586-024-08015-6 · Cited by 25

Structural insights into binding-site access and ligand recognition by human ABCB1

Kurre, D., Dang, P. X., Le, L. T. M., Gadkari, V. V., & Alam, A. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00361-z · Cited by 25

3D imaging and quantitative analysis of small solubilized membrane proteins and their complexes by transmission electron microscopy

Vahedi-Faridi, A., Jastrzebska, B., Palczewski, K., & Engel, A. (2013) · Microscopy · doi:10.1093/jmicro/dfs091 · 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 cereblon-based glue degrader of NEK7 regulates NLRP3 inflammasome in a context-dependent manner

Sylvain, A., Stoehr, N., Ma, F., Cernijenko, A., Schröder, M., Khoshouei, M., Vogelsanger, M., Schoenboerner, M., Burke, A., Rao, P., et al. (2025) · Cell Chemical Biology · doi:10.1016/j.chembiol.2025.06.005 · Cited by 23

Structural basis for Retriever-SNX17 assembly and endosomal sorting

Singla, A., Boesch, D. J., Fung, H. Y. J., Ngoka, C., Enriquez, A. S., Song, R., Kramer, D. A., Han, Y., Banarer, E., Lemoff, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-54583-6 · Cited by 23

Phage display enables machine learning discovery of cancer antigen–specific TCRs

Croce, G., Lani, R., Tardivon, D., Bobisse, S., de Tiani, M., Bragina, M., Perez, M. A. S., Michaux, J., Pak, H. S., Michel, A., et al. (2025) · Science Advances · doi:10.1126/sciadv.ads5589 · Cited by 23

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

Spodoptera littoralis genome mining brings insights on the dynamic of expansion of gustatory receptors in polyphagous noctuidae

(2022) · doi:10.1093/g3journal/jkac131 · Cited by 23

GTalign: spatial index-driven protein structure alignment, superposition, and search

(2024) · doi:10.1038/s41467-024-51669-z · Cited by 23

Large-Scale Discovery of Microbial Fibrillar Adhesins and Identification of Novel Members of Adhesive Domain Families

(2022) · doi:10.1128/jb.00107-22 · Cited by 23

Rational exploration of fold atlas for human solute carrier proteins

Xie, T., Chi, X., Huang, B., Ye, F., Zhou, Q., & Huang, J. (2022) · Structure · doi:10.1016/j.str.2022.05.015 · Cited by 23

Mechanistic insights explain the transforming potential of the T507K substitution in the protein-tyrosine phosphatase SHP2

Zhang, R.-Y., Yu, Z.-H., Chen, L., Walls, C. D., Zhang, S., Wu, L., & Zhang, Z.-Y. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010274 · Cited by 22

Tetracenomycin X sequesters peptidyl-tRNA during translation of QK motifs

Leroy, E. C., Perry, T. N., Renault, T. T., & Innis, C. A. (2023) · Nature Chemical Biology · doi:10.1038/s41589-023-01343-0 · Cited by 22

Molecular model of the ferroportin intracellular gate and implications for the human iron transport cycle and hemochromatosis type 4A

Guellec, J., Elbahnsi, A., Tertre, M. L., Uguen, K., Gourlaouen, I., Férec, C., Ka, C., Callebaut, I., & Gac, G. L. (2019) · The FASEB Journal · doi:10.1096/fj.201901857r · Cited by 21

PAM binding ensures orientational integration during Cas4-Cas1-Cas2-mediated CRISPR adaptation

Dhingra, Y., Suresh, S. K., Juneja, P., & Sashital, D. G. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.09.030 · Cited by 21

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 delineation and computational design of SARS-CoV-2-neutralizing antibodies against Omicron subvariants

Moriyama, S., Anraku, Y., Taminishi, S., Adachi, Y., Kuroda, D., Kita, S., Higuchi, Y., Kirita, Y., Kotaki, R., Tonouchi, K., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39890-8 · Cited by 22

Structural features stabilized by divalent cation coordination within hepatitis E virus ORF1 are critical for viral replication

LeDesma, R., Heller, B., Biswas, A., Maya, S., Gili, S., Higgins, J., & Ploss, A. (2023) · eLife · doi:10.7554/elife.80529 · Cited by 22

A Peptide Derived from Lens Epithelium–Derived Growth Factor Stimulates HIV-1 DNA Integration and Facilitates Intasome Structural Studies

Li, M., Chen, X., Wang, H., Jurado, K. A., Engelman, A. N., & Craigie, R. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.040 · Cited by 18

AlphaFold-predicted protein structures and small-angle X-ray scattering: insights from an extended examination of selected data in the Small-Angle Scattering Biological Data Bank

Brookes, E., Rocco, M., Vachette, P., & Trewhella, J. (2023) · Journal of Applied Crystallography · doi:10.1107/s1600576723005344 · Cited by 21

Natural Killer Cell Activation Receptor NKp30 Oligomerization Depends on Its N-Glycosylation

Skořepa, O., Pazicky, S., Kalousková, B., Bláha, J., Abreu, C., Ječmen, T., Rosůlek, M., Fish, A., Sedivy, A., Harlos, K., et al. (2020) · Cancers · doi:10.3390/cancers12071998 · Cited by 21

A Potent and Protective Human Neutralizing Antibody Against SARS-CoV-2 Variants

Shan, S., Mok, C. K., Zhang, S., Lan, J., Li, J., Yang, Z., Wang, R., Cheng, L., Fang, M., Aw, Z. Q., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.766821 · Cited by 21

Comparison of native and non-native ubiquitin oligomers reveals analogous structures and reactivities

Pham, G. H., Rana, A. S. J. B., Korkmaz, E. N., Trang, V. H., Cui, Q., & Strieter, E. R. (2016) · Protein Science · doi:10.1002/pro.2834 · Cited by 21

Mutational Analysis of Sigma-1 Receptor’s Role in Synaptic Stability

Ryskamp, D. A., Zhemkov, V., & Bezprozvanny, I. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01012 · Cited by 21

Structure of the recombinant RNA polymerase from African Swine Fever Virus

Pilotto, S., Sýkora, M., Cackett, G., Dulson, C., & Werner, F. (2024) · Nature Communications · doi:10.1038/s41467-024-45842-7 · Cited by 21

Mutagenesis and structural studies reveal the basis for the specific binding of SARS-CoV-2 SL3 RNA element with human TIA1 protein

Zhang, D., Qiao, L., Lei, X., Dong, X., Tong, Y., Wang, J., Wang, Z., & Zhou, R. (2023) · Nature Communications · doi:10.1038/s41467-023-39410-8 · Cited by 21

CyToStruct: augmenting the network visualization of cytoscape with the power of molecular viewers

Nepomnyachiy, S., Ben-Tal, N., & Kolodny, R. (2015) · Structure · doi:10.1016/j.str.2015.02.013 · Cited by 20

Markov models of the apo-MDM2 lid region reveal diffuse yet two-state binding dynamics and receptor poses for computational docking

Mukherjee, S., Pantelopulos, G. A., & Voelz, V. A. (2016) · Scientific Reports · doi:10.1038/srep31631 · Cited by 20

30S subunit recognition and G1405 modification by the aminoglycoside-resistance 16S ribosomal RNA methyltransferase RmtC

Srinivas, P., Nosrati, M., Zelinskaya, N., Dey, D., Comstock, L. R., Dunham, C. M., & Conn, G. L. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2304128120 · Cited by 20

Research resource: correlating human cytochrome P450 21A2 crystal structure and phenotypes of mutations in congenital adrenal hyperplasia

Pallan, P. S., Lei, L., Wang, C., Waterman, M. R., Guengerich, F. P., & Egli, M. (2015) · Molecular Endocrinology · doi:10.1210/me.2015-1127 · Cited by 19

Modeling single nucleotide polymorphisms in the human AKR1C1 and AKR1C2 genes: implications for functional and genotyping analyses

Arthur, J. W., & Reichardt, J. K. V. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015604 · Cited by 18

BBS9 gene in nonsyndromic craniosynostosis: Role of the primary cilium in the aberrant ossification of the suture osteogenic niche

Barba, M., Di Pietro, L., Massimi, L., Geloso, M. C., Frassanito, P., Caldarelli, M., Michetti, F., Della Longa, S., Romitti, P. A., Di Rocco, C., et al. (2018) · Bone · doi:10.1016/j.bone.2018.04.013 · Cited by 19

Analysing the visible conformational substates of the FK506 binding protein FKBP12

Mustafi, S. M., Chen, H., Li, H., LeMaster, D. M., & Hernández, G. (2013) · Biochemical Journal · doi:10.1042/bj20130276 · Cited by 19

The small CRL4CSA ubiquitin ligase component DDA1 regulates transcription-coupled repair dynamics

Llerena Schiffmacher, D. A., Lee, S.-H., Kliza, K. W., Theil, A. F., Akita, M., Helfricht, A., Bezstarosti, K., Gonzalo-Hansen, C., van Attikum, H., Verlaan-de Vries, M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-50584-7 · Cited by 19

Markov modeling reveals novel intracellular modulation of the human TREK-2 selectivity filter

Harrigan, M. P., McKiernan, K. A., Shanmugasundaram, V., Denny, R. A., & Pande, V. S. (2017) · Scientific Reports · doi:10.1038/s41598-017-00256-y · Cited by 19

Computational analysis of antimicrobial peptides targeting key receptors in infection-related cardiovascular diseases: molecular docking and dynamics insights

Dermawan, D., & Alotaiq, N. (2025) · Scientific Reports · doi:10.1038/s41598-025-93683-1 · Cited by 19

Isolation of cross-reactive monoclonal antibodies against divergent human coronaviruses that delineate a conserved and vulnerable site on the spike protein

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