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

Genome-wide screen reveals Rab12 GTPase as a critical activator of Parkinson’s disease-linked LRRK2 kinase

Dhekne, H. S., Tonelli, F., Yeshaw, W. M., Chiang, C. Y., Limouse, C., Jaimon, E., Purlyte, E., Alessi, D. R., & Pfeffer, S. R. (2023) · eLife · doi:10.7554/elife.87098 · Cited by 76

Neutralizing and protective human monoclonal antibodies recognizing the N-terminal domain of the SARS-CoV-2 spike protein

Suryadevara, N., Shrihari, S., Gilchuk, P., VanBlargan, L. A., Binshtein, E., Zost, S. J., Nargi, R. S., Sutton, R. E., Winkler, E. S., Chen, E. C., et al. (2021) · doi:10.1101/2021.01.19.427324 · Cited by 361

Tetracenomycin X inhibits translation by binding within the ribosomal exit tunnel

Osterman, I. A., Wieland, M., Maviza, T. P., Lashkevich, K. A., Lukianov, D. A., Komarova, E. S., Zakalyukina, Y. V., Buschauer, R., Shiriaev, D. I., Leyn, S. A., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0578-x · Cited by 75

Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor

Noddings, C. M., Johnson, J. L., & Agard, D. A. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01128-y · Cited by 75

Structural basis for placental malaria mediated by Plasmodium falciparum VAR2CSA.

Ma, R., Lian, T., Huang, R., Renn, J. P., Petersen, J. D., Zimmerberg, J., Duffy, P. E., & Tolia, N. H. (2021) · Nature Microbiology · doi:10.1038/s41564-020-00858-9 · Cited by 72

A novel Cas family member, HEPL, regulates FAK and cell spreading

Singh, M. K., Dadke, D., Nicolas, E., Serebriiskii, I. G., Apostolou, S., Canutescu, A., Egleston, B. L., & Golemis, E. A. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-09-0953 · Cited by 74

Paralog dependency indirectly affects the robustness of human cells

Dandage, R., & Landry, C. R. (2019) · Molecular Systems Biology · doi:10.15252/msb.20198871 · Cited by 65

Life Beyond Kinases: Structure-Based Discovery of Sorafenib as Nanomolar Antagonist of 5-HT Receptors

Lin, X., Huang, X.-P., Chen, G., Whaley, R., Peng, S., Wang, Y., Zhang, G., Wang, S. X., Wang, S., Roth, B. L., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300338m · Cited by 73

AAV-ID: A Rapid and Robust Assay for Batch-to-Batch Consistency Evaluation of AAV Preparations

Pacouret, S., Bouzelha, M., Shelke, R., Andres-Mateos, E., Xiao, R., Maurer, A., Mevel, M., Turunen, H., Barungi, T., Penaud-Budloo, M., et al. (2017) · Molecular Therapy · doi:10.1016/j.ymthe.2017.04.001 · Cited by 69

Insight into the mechanisms of enhanced retinal transduction by the engineered AAV2 capsid variant -7m8

Khabou, H., Desrosiers, M., Winckler, C., Fouquet, S., Auregan, G., Bemelmans, A., Sahel, J., & Dalkara, D. (2016) · Biotechnology and Bioengineering · doi:10.1002/bit.26031 · Cited by 71

Specificity and Inhibitory Mechanism of Andrographolide and Its Analogues as Antiasthma Agents on NF-κB p50

Nguyen, V. S., Loh, X. Y., Wijaya, H., Wang, J., Lin, Q., Lam, Y., Wong, W.-S. F., & Mok, Y. K. (2015) · Journal of Natural Products · doi:10.1021/np5007179 · Cited by 66

A Structural Ensemble of a Tau-Microtubule Complex Reveals Regulatory Tau Phosphorylation and Acetylation Mechanisms

Brotzakis, Z. F., Lindstedt, P. R., Taylor, R. J., Rinauro, D. J., Gallagher, N. C. T., Bernardes, G. J. L., & Vendruscolo, M. (2021) · ACS Central Science · doi:10.1021/acscentsci.1c00585 · Cited by 70

Structure of an endogenous mycobacterial MCE lipid transporter

Chen, J., Fruhauf, A., Fan, C., Ponce, J., Ueberheide, B., Bhabha, G., & Ekiert, D. C. (2023) · Nature · doi:10.1038/s41586-023-06366-0 · Cited by 69

A cryo-ET survey of microtubules and intracellular compartments in mammalian axons

Foster, H. E., Ventura Santos, C., & Carter, A. P. (2022) · Journal of Cell Biology · doi:10.1083/jcb.202103154 · Cited by 69

Soluble TREM2 inhibits secondary nucleation of Aβ fibrillization and enhances cellular uptake of fibrillar Aβ

Belsare, K. D., Wu, H., Mondal, D., Bond, A., Castillo, E., Jin, J., Jo, H., Roush, A. E., Pilla, K. B., Sali, A., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2114486119 · Cited by 68

The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function.

Grossman, M., Tworowski, D., Dym, O., Lee, M.-H., Levy, Y., Murphy, G., & Sagi, I. (2010) · Biochemistry · doi:10.1021/bi902141x · Cited by 68

Structural basis for ATG9A recruitment to the ULK1 complex in mitophagy initiation

Ren, X., Nguyen, T. N., Lam, W. K., Buffalo, C. Z., Lazarou, M., Yokom, A. L., & Hurley, J. H. (2023) · Science Advances · doi:10.1126/sciadv.adg2997 · Cited by 68

Identification of Nicotinamide Mononucleotide Deamidase of the Bacterial Pyridine Nucleotide Cycle Reveals a Novel Broadly Conserved Amidohydrolase Family

Galeazzi, L., Bocci, P., Amici, A., Brunetti, L., Ruggieri, S., Romine, M., Reed, S., Osterman, A. L., Rodionov, D. A., Sorci, L., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.275818 · Cited by 67

Cryo-EM structure and resistance landscape of M. tuberculosis MmpL3: An emergent therapeutic target

Adams, O., Deme, J. C., Parker, J. L., Fowler, P. W., Lea, S. M., & Newstead, S. (2021) · Structure · doi:10.1016/j.str.2021.06.013 · Cited by 63

Albumin-binding adenoviruses circumvent pre-existing neutralizing antibodies upon systemic delivery

Rojas, L. A., Condezo, G. N., Moreno, R., Fajardo, C. A., Arias-Badia, M., San Martín, C., & Alemany, R. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.07.004 · Cited by 66

Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.

Jomaa, A., Fu, Y.-H. H., Boehringer, D., Leibundgut, M., Shan, S.-O., & Ban, N. (2017) · Nature Communications · doi:10.1038/ncomms15470 · Cited by 66

Synthetic Adeno-Associated Viral Vector Efficiently Targets Mouse and Nonhuman Primate Retina In Vivo

Carvalho, L. S., Xiao, R., Wassmer, S. J., Langsdorf, A., Zinn, E., Pacouret, S., Shah, S., Comander, J. I., Kim, L. A., Lim, L., et al. (2018) · Human Gene Therapy · doi:10.1089/hum.2017.154 · Cited by 63

MHJ_0461 is a multifunctional leucine aminopeptidase on the surface of Mycoplasma hyopneumoniae

Jarocki, V. M., Santos, J., Tacchi, J. L., Raymond, B. B. A., Deutscher, A. T., Jenkins, C., Padula, M. P., & Djordjevic, S. P. (2015) · Open Biology · doi:10.1098/rsob.140175 · Cited by 63

Comparative Structural Analysis of 20S Proteasome Ortholog Protein Complexes by Native Mass Spectrometry

Vimer, S., Ben-Nissan, G., Morgenstern, D., Kumar-Deshmukh, F., Polkinghorn, C., Quintyn, R. S., Vasil’ev, Y. V., Beckman, J. S., Elad, N., Wysocki, V. H., et al. (2020) · ACS Central Science · doi:10.1021/acscentsci.0c00080 · Cited by 63

Sorsby fundus dystrophy—A review of pathology and disease mechanisms

Christensen, D. R. G., Brown, F. E., Cree, A. J., Ratnayaka, J. A., & Lotery, A. J. (2017) · Experimental Eye Research · doi:10.1016/j.exer.2017.08.014 · Cited by 60

Imprinted antibody responses against SARS-CoV-2 Omicron sublineages

Park, Y.-J., Pinto, D., Walls, A. C., Liu, Z., De Marco, A., Benigni, F., Zatta, F., Silacci-Fregni, C., Bassi, J., Sprouse, K. R., et al. (2022) · doi:10.1101/2022.05.08.491108 · Cited by 251

In Silico Modeling and Scoring of PROTAC-Mediated Ternary Complex Poses

Liao, J., Nie, X., Unarta, I. C., Ericksen, S. S., & Tang, W. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c02155 · Cited by 62

Cortisone-reductase deficiency associated with heterozygous mutations in 11β-hydroxysteroid dehydrogenase type 1

Lawson, A. J., Walker, E. A., Lavery, G. G., Bujalska, I. J., Hughes, B., Arlt, W., Stewart, P. M., & Ride, J. P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014934108 · Cited by 61

PACRG and FAP20 form the inner junction of axonemal doublet microtubules and regulate ciliary motility

Dymek, E. E., Lin, J., Fu, G., Porter, M. E., Nicastro, D., & Smith, E. F. (2019) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-01-0063 · Cited by 61

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

Cryo-EM Determination of Eravacycline-Bound Structures of the Ribosome and the Multidrug Efflux Pump AdeJ of Acinetobacter baumannii

Zhang, Z., Morgan, C. E., Bonomo, R. A., & Yu, E. W. (2021) · mBio · doi:10.1128/mbio.01031-21 · Cited by 58

UM171 glues asymmetric CRL3–HDAC1/2 assembly to degrade CoREST corepressors

Yeo, M. J. R., Zhang, O., Xie, X., Nam, E., Payne, N. C., Gosavi, P. M., Kwok, H. S., Iram, I., Lee, C., Li, J., et al. (2025) · Nature · doi:10.1038/s41586-024-08532-4 · Cited by 58

METTL17 is an Fe-S cluster checkpoint for mitochondrial translation

Ast, T., Itoh, Y., Sadre, S., McCoy, J. G., Namkoong, G., Wengrod, J. C., Chicherin, I., Joshi, P. R., Kamenski, P., Suess, D. L. M., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2023.12.016 · Cited by 58

Rhodopsin–transducin heteropentamer: Three-dimensional structure and biochemical characterization

Jastrzebska, B., Ringler, P., Lodowski, D. T., Moiseenkova-Bell, V., Golczak, M., Müller, S. A., Palczewski, K., & Engel, A. (2011) · Journal of Structural Biology · doi:10.1016/j.jsb.2011.08.016 · Cited by 57

The Hyr1 protein from the fungus Candida albicans is a cross kingdom immunotherapeutic target for Acinetobacter bacterial infection

Uppuluri, P., Lin, L., Alqarihi, A., Luo, G., Youssef, E. G., Alkhazraji, S., Yount, N. Y., Ibrahim, B. A., Bolaris, M. A., Edwards, J. E., et al. (2018) · PLOS Pathogens · doi:10.1371/journal.ppat.1007056 · Cited by 57

Structural insights into the assembly of gp130 family cytokine signaling complexes

Zhou, Y., Stevis, P. E., Cao, J., Saotome, K., Wu, J., Glatman Zaretsky, A., Haxhinasto, S., Yancopoulos, G. D., Murphy, A. J., Sleeman, M. W., et al. (2023) · Science Advances · doi:10.1126/sciadv.ade4395 · Cited by 56

Structural insights into the iron nitrogenase complex

Schmidt, F. V., Schulz, L., Zarzycki, J., Prinz, S., Oehlmann, N. N., Erb, T. J., & Rebelein, J. G. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01124-2 · Cited by 56

Molecular Organization and ATP-Induced Conformational Changes of ABCA4, the Photoreceptor-Specific ABC Transporter

Tsybovsky, Y., Orban, T., Molday, R. S., Taylor, D., & Palczewski, K. (2013) · Structure · doi:10.1016/j.str.2013.03.001 · Cited by 53

Tetrahymena RIB72A and RIB72B are microtubule inner proteins in the ciliary doublet microtubules

Stoddard, D., Zhao, Y., Bayless, B. A., Gui, L., Louka, P., Dave, D., Suryawanshi, S., Tomasi, R. F.-X., Dupuis-Williams, P., Baroud, C. N., et al. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-06-0405 · Cited by 53

Substrate and product complexes reveal mechanisms of Hedgehog acylation by HHAT

Jiang, Y., Benz, T. L., & Long, S. B. (2021) · Science · doi:10.1126/science.abg4998 · Cited by 55

Structure and regulation of the nuclear exosome targeting complex guides RNA substrates to the exosome

Gerlach, P., Garland, W., Lingaraju, M., Salerno-Kochan, A., Bonneau, F., Basquin, J., Jensen, T. H., & Conti, E. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.04.011 · Cited by 55

The final step of 40S ribosomal subunit maturation is controlled by a dual key lock

Plassart, L., Shayan, R., Montellese, C., Rinaldi, D., Larburu, N., Pichereaux, C., Froment, C., Lebaron, S., O'Donohue, M.-F., Kutay, U., et al. (2021) · eLife · doi:10.7554/elife.61254 · Cited by 55

Csx28 is a membrane pore that enhances CRISPR-Cas13b–dependent antiphage defense

VanderWal, A. R., Park, J.-U., Polevoda, B., Nicosia, J. K., Molina Vargas, A. M., Kellogg, E. H., & O’Connell, M. R. (2023) · Science · doi:10.1126/science.abm1184 · Cited by 55

Robust scoring functions for protein-ligand interactions with quantum chemical charge models.

Wang, J.-C., Lin, J.-H., Chen, C.-M., Perryman, A. L., & Olson, A. J. (2011) · Journal of Chemical Information and Modeling · doi:10.1021/ci200220v · Cited by 54

Gold Nanoparticle Aggregates Functionalized with Cyclic RGD Peptides for Targeting and Imaging of Colorectal Cancer Cells

Biscaglia, F., Ripani, G., Rajendran, S., Benna, C., Mocellin, S., Bocchinfuso, G., Meneghetti, M., Palleschi, A., & Gobbo, M. (2019) · ACS Applied Nano Materials · doi:10.1021/acsanm.9b01392 · Cited by 54

Structural basis for regulation of the opposing (p)ppGpp synthetase and hydrolase within the stringent response Orchestrator Rel.

Pausch, P., Abdelshahid, M., Steinchen, W., Schäfer, H., Gratani, F. L., Freibert, S.-A., Wolz, C., Turgay, K., Wilson, D. N., & Bange, G. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108157 · Cited by 53

A Monoclonal Antibody to Cryptococcus neoformans Glucuronoxylomannan Manifests Hydrolytic Activity for Both Peptides and Polysaccharides

Bowen, A., Wear, M. P., Cordero, R. J. B., Oscarson, S., & Casadevall, A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.767582 · Cited by 51

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

Structures of Angptl3 and Angptl4, modulators of triglyceride levels and coronary artery disease

Biterova, E., Esmaeeli, M., Alanen, H. I., Saaranen, M., & Ruddock, L. W. (2018) · Scientific Reports · doi:10.1038/s41598-018-25237-7 · Cited by 53

DNA-measuring Wadjet SMC ATPases restrict smaller circular plasmids by DNA cleavage

Liu, H. W., Roisné-Hamelin, F., Beckert, B., Li, Y., Myasnikov, A., & Gruber, S. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.11.015 · Cited by 53

Structural organization of the retriever–CCC endosomal recycling complex

Boesch, D. J., Singla, A., Han, Y., Kramer, D. A., Liu, Q., Suzuki, K., Juneja, P., Zhao, X., Long, X., Medlyn, M. J., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01184-4 · Cited by 52

The Fab region of IgG impairs the internalization pathway of FcRn upon Fc engagement

Brinkhaus, M., Pannecoucke, E., van der Kooi, E. J., Bentlage, A. E. H., Derksen, N. I. L., Andries, J., Balbino, B., Sips, M., Ulrichts, P., Verheesen, P., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33764-1 · Cited by 51

Novel H6PDH mutations in two girls with premature adrenarche: ‘apparent’ and ‘true’ CRD can be differentiated by urinary steroid profiling

Lavery, G. G., Idkowiak, J., Sherlock, M., Bujalska, I., Ride, J. P., Saqib, K., Hartmann, M. F., Hughes, B., Wudy, S. A., De Schepper, J., et al. (2013) · European Journal of Endocrinology · doi:10.1530/eje-12-0628 · Cited by 50

Allosteric interactions prime androgen receptor dimerization and activation

Wasmuth, E. V., Broeck, A. V., LaClair, J. R., Hoover, E. A., Lawrence, K. E., Paknejad, N., Pappas, K., Matthies, D., Wang, B., Feng, W., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.03.035 · Cited by 50

Converging mechanism of UM171 and KBTBD4 neomorphic cancer mutations

Xie, X., Zhang, O., Yeo, M. J. R., Lee, C., Tao, R., Harry, S. A., Payne, N. C., Nam, E., Paul, L., Li, Y., et al. (2025) · Nature · doi:10.1038/s41586-024-08533-3 · Cited by 50

Pseudomonas aeruginosa FpvB Is a High-Affinity Transporter for Xenosiderophores Ferrichrome and Ferrioxamine B

Chan, D. C. K., & Burrows, L. L. (2023) · mBio · doi:10.1128/mbio.03149-22 · Cited by 50

Partially inserted nascent chain unzips the lateral gate of the Sec translocon.

Kater, L., Frieg, B., Berninghausen, O., Gohlke, H., Beckmann, R., & Kedrov, A. (2019) · The EMBO Reports · doi:10.15252/embr.201948191 · Cited by 43

ON selectivity in the Drosophila visual system is a multisynaptic process involving both glutamatergic and GABAergic inhibition

Molina-Obando, S., Vargas-Fique, J. F., Henning, M., Gür, B., Schladt, T. M., Akhtar, J., Berger, T. K., & Silies, M. (2019) · eLife · doi:10.7554/elife.49373 · Cited by 49

Clamping of DNA shuts the condensin neck gate

Lee, B.-G., Rhodes, J., & Löwe, J. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2120006119 · Cited by 49

Allergens of Blomia tropicalis: An Overview of Recombinant Molecules

Santos da Silva, E., Asam, C., Lackner, P., Hofer, H., Wallner, M., Silva Pinheiro, C., Alcântara-Neves, N. M., & Ferreira, F. (2017) · International Archives of Allergy and Immunology · doi:10.1159/000464325 · Cited by 48

Ctf18-RFC and DNA Pol ϵ form a stable leading strand polymerase/clamp loader complex required for normal and perturbed DNA replication

Stokes, K., Winczura, A., Song, B., De Piccoli, G., & Grabarczyk, D. B. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa541 · Cited by 48

Biallelic variants in PSMB1 encoding the proteasome subunit β6 cause impairment of proteasome function, microcephaly, intellectual disability, developmental delay and short stature

Ansar, M., Ebstein, F., Özkoç, H., Paracha, S. A., Iwaszkiewicz, J., Gesemann, M., Zoete, V., Ranza, E., Santoni, F. A., Sarwar, M. T., et al. (2020) · Human Molecular Genetics · doi:10.1093/hmg/ddaa032 · Cited by 44

A New Gene Family Diagnostic for Intracellular Biomineralization of Amorphous Ca Carbonates by Cyanobacteria

Benzerara, K., Duprat, E., Bitard-Feildel, T., Caumes, G., Cassier-Chauvat, C., Chauvat, F., Dezi, M., Diop, S. I., Gaschignard, G., Görgen, S., et al. (2022) · Genome Biology and Evolution · doi:10.1093/gbe/evac026 · Cited by 47

Nucleosome binding by the pioneer transcription factor OCT4

Echigoya, K., Koyama, M., Negishi, L., Takizawa, Y., Mizukami, Y., Shimabayashi, H., Kuroda, A., & Kurumizaka, H. (2020) · Scientific Reports · doi:10.1038/s41598-020-68850-1 · Cited by 47

Mechanism of glycogen synthase inactivation and interaction with glycogenin

Marr, L., Biswas, D., Daly, L. A., Browning, C., Vial, S. C. M., Maskell, D. P., Hudson, C., Bertrand, J. A., Pollard, J., Ranson, N. A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31109-6 · Cited by 47

High-resolution characterization of gene function using single-cell CRISPR tiling screen

Yang, L., Chan, A. K. N., Miyashita, K., Delaney, C. D., Wang, X., Li, H., Pokharel, S. P., Li, S., Li, M., Xu, X., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24324-0 · Cited by 45

A structural model of human ferroportin and of its iron binding site

Bonaccorsi di Patti, M. C., Polticelli, F., Cece, G., Cutone, A., Felici, F., Persichini, T., & Musci, G. (2014) · The FEBS Journal · doi:10.1111/febs.12825 · Cited by 44

α- and β-Tubulin Lattice of the Axonemal Microtubule Doublet and Binding Proteins Revealed by Single Particle Cryo-Electron Microscopy and Tomography

Maheshwari, A., Obbineni, J. M., Bui, K. H., Shibata, K., Toyoshima, Y. Y., & Ishikawa, T. (2015) · Structure · doi:10.1016/j.str.2015.06.017 · Cited by 47

On-the-fly QM/MM docking with attracting cavities.

Chaskar, P., Zoete, V., & Röhrig, U. F. (2017) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6b00406 · Cited by 46

Reciprocal best structure hits: using AlphaFold models to discover distant homologues

Monzon, V., Paysan-Lafosse, T., Wood, V., & Bateman, A. (2022) · Bioinformatics Advances · doi:10.1093/bioadv/vbac072 · Cited by 46

Modulating co-translational protein folding by rational design and ribosome engineering

Ahn, M., Włodarski, T., Mitropoulou, A., Chan, S. H. S., Sidhu, H., Plessa, E., Becker, T. A., Budisa, N., Waudby, C. A., Beckmann, R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31906-z · Cited by 45

High-resolution structural characterization of a new adeno-associated virus serotype 5 antibody epitope toward engineering antibody-resistant recombinant gene delivery vectors

Jose, A., Mietzsch, M., Smith, J. K., Kurian, J., Chipman, P., McKenna, R., Chiorini, J., & Agbandje-McKenna, M. (2019) · Journal of Virology · doi:10.1128/jvi.01394-18 · Cited by 44

Structure of the human heparan sulfate polymerase complex EXT1-EXT2

Leisico, F., Omeiri, J., Le Narvor, C., Beaudouin, J., Hons, M., Fenel, D., Schoehn, G., Couté, Y., Bonnaffé, D., Sadir, R., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34882-6 · Cited by 45

Structural and molecular basis of choline uptake into the brain by FLVCR2

Cater, R. J., Mukherjee, D., Gil-Iturbe, E., Erramilli, S. K., Chen, T., Koo, K., Santander, N., Reckers, A., Kloss, B., Gawda, T., et al. (2024) · Nature · doi:10.1038/s41586-024-07326-y · Cited by 45

Structure and function of virion RNA polymerase of a crAss-like phage

Drobysheva, A. V., Panafidina, S. A., Kolesnik, M. V., Klimuk, E. I., Minakhin, L., Yakunina, M. V., Borukhov, S., Nilsson, E., Holmfeldt, K., Yutin, N., et al. (2021) · Nature · doi:10.1038/s41586-020-2921-5 · Cited by 44

APOGEE 2: multi-layer machine-learning model for the interpretable prediction of mitochondrial missense variants

Bianco, S. D., Parca, L., Petrizzelli, F., Biagini, T., Giovannetti, A., Liorni, N., Napoli, A., Carella, M., Procaccio, V., Lott, M. T., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40797-7 · Cited by 44

Siderophore-mediated iron acquisition by Klebsiella pneumoniae

Kumar, A., Chakravorty, S., Yang, T., Russo, T. A., Newton, S. M., & Klebba, P. E. (2024) · Journal of Bacteriology · doi:10.1128/jb.00024-24 · Cited by 42

Dravet syndrome-associated mutations in GABRA1,GABRB2 and GABRG2 define the genetic landscape of defects of GABAA receptors

Hernandez, C. C., Tian, X., Hu, N., Shen, W., Catron, M. A., Yang, Y., Chen, J., Jiang, Y., Zhang, Y., & Macdonald, R. L. (2021) · Brain Communications · doi:10.1093/braincomms/fcab033 · Cited by 43

Structure of a P element transposase–DNA complex reveals unusual DNA structures and GTP-DNA contacts

Ghanim, G. E., Kellogg, E. H., Nogales, E., & Rio, D. C. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0319-6 · Cited by 37

Functional analysis of human cytochrome P450 21A2 variants involved in congenital adrenal hyperplasia

Wang, C., Pallan, P. S., Zhang, W., Lei, L., Yoshimoto, F. K., Waterman, M. R., Egli, M., & Guengerich, F. P. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.792465 · 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

Anesthetics target interfacial transmembrane sites in nicotinic acetylcholine receptors

Forman, S. A., Chiara, D. C., & Miller, K. W. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.10.002 · Cited by 42

Functional and structural characterization of a dense core secretory granule sorting domain from the PC1/3 protease

Dikeakos, J. D., Di Lello, P., Lacombe, M.-J., Ghirlando, R., Legault, P., Reudelhuber, T. L., & Omichinski, J. G. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809576106 · Cited by 40

An ensemble of flexible conformations underlies mechanotransduction by the cadherin–catenin adhesion complex

Bush, M., Alhanshali, B. M., Qian, S., Stanley, C. B., Heller, W. T., Matsui, T., Weiss, T. M., Nicholl, I. D., Walz, T., Callaway, D. J. E., et al. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911489116 · Cited by 42

Retroviral integration into nucleosomes through DNA looping and sliding along the histone octamer

Wilson, M. D., Renault, L., Maskell, D. P., Ghoneim, M., Pye, V. E., Nans, A., Rueda, D. S., Cherepanov, P., & Costa, A. (2019) · Nature Communications · doi:10.1038/s41467-019-12007-w · Cited by 42

Filling Adeno-Associated Virus Capsids: Estimating Success by Cryo-Electron Microscopy

Subramanian, S., Maurer, A. C., Bator, C. M., Makhov, A. M., Conway, J. F., Turner, K. B., Marden, J. H., Vandenberghe, L. H., & Hafenstein, S. L. (2019) · Human Gene Therapy · doi:10.1089/hum.2019.041 · Cited by 40

Surface-Binding to Cardiolipin Nanodomains Triggers Cytochrome c Pro-apoptotic Peroxidase Activity via Localized Dynamics

Li, M., Mandal, A., Tyurin, V. A., DeLucia, M., Ahn, J., Kagan, V. E., & van der Wel, P. C. A. (2019) · Structure · doi:10.1016/j.str.2019.02.007 · Cited by 41

The Hydration Effect and Selectivity of Alkali Metal Ions on Poly(ethylene glycol) Models in Cyclic and Linear Topology

Poudel, L., Podgornik, R., & Ching, W.-Y. (2017) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.7b04061 · Cited by 41

Genetic and phenotypic assessment of the antimicrobial activity of three potential probiotic lactobacilli against human enteropathogenic bacteria

Kiousi, D. E., Efstathiou, C., Tzampazlis, V., Plessas, S., Panopoulou, M., Koffa, M., & Galanis, A. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2023.1127256 · Cited by 41

A ZnS4 Structural Zinc Site in the Helicobacter pylori Ferric Uptake Regulator

Vitale, S., Fauquant, C., Lascoux, D., Schauer, K., Saint-Pierre, C., & Michaud-Soret, I. (2009) · Biochemistry · doi:10.1021/bi9004396 · Cited by 40

MOSPD2 is an endoplasmic reticulum–lipid droplet tether functioning in LD homeostasis

Zouiouich, M., Di Mattia, T., Martinet, A., Eichler, J., Wendling, C., Tomishige, N., Grandgirard, E., Fuggetta, N., Fromental-Ramain, C., Mizzon, G., et al. (2022) · Journal of Cell Biology · doi:10.1083/jcb.202110044 · Cited by 40

Molecular basis of Wnt biogenesis, secretion, and Wnt7-specific signaling

Qi, X., Hu, Q., Elghobashi-Meinhardt, N., Long, T., Chen, H., & Li, X. (2023) · Cell · doi:10.1016/j.cell.2023.09.021 · Cited by 40

Structure of the RZZ complex and molecular basis of Spindly‐driven corona assembly at human kinetochores

(2022) · doi:10.15252/embj.2021110411 · Cited by 40

A G-protein-coupled chemoattractant receptor recognizes lipopolysaccharide for bacterial phagocytosis

Pan, M., Neilson, M. P., Grunfeld, A. M., Cruz, P., Wen, X., Insall, R. H., & Jin, T. (2018) · PLOS Biology · doi:10.1371/journal.pbio.2005754 · Cited by 36

An adeno-associated virus variant enabling efficient ocular-directed gene delivery across species

Luo, S., Jiang, H., Li, Q., Qin, Y., Yang, S., Li, J., Xu, L., Gou, Y., Zhang, Y., Liu, F., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-48221-4 · Cited by 39

Structural basis of the bacterial flagellar motor rotational switching

(2024) · doi:10.1038/s41422-024-01017-z · Cited by 39

The PfRCR complex bridges malaria parasite and erythrocyte during invasion

Farrell, B., Alam, N., Hart, M. N., Jamwal, A., Ragotte, R. J., Walters-Morgan, H., Draper, S. J., Knuepfer, E., & Higgins, M. K. (2024) · Nature · doi:10.1038/s41586-023-06856-1 · Cited by 39

New precision medicine avenues to the prevention of Alzheimer’s disease from insights into the structure and function of γ-secretases

De Strooper, B., & Karran, E. (2024) · The EMBO Journal · doi:10.1038/s44318-024-00057-w · Cited by 36

Design and linkage optimization of ursane-thalidomide-based PROTACs and identification of their targeted-degradation properties to MDM2 protein

Qi, Z., Yang, G., Deng, T., Wang, J., Zhou, H., Popov, S. A., Shults, E. E., & Wang, C. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104901 · Cited by 39

Impaired SorLA maturation and trafficking as a new mechanism for SORL1 missense variants in Alzheimer disease

Rovelet-Lecrux, A., Feuillette, S., Miguel, L., Schramm, C., Pernet, S., Quenez, O., Ségalas-Milazzo, I., Guilhaudis, L., Rousseau, S., Riou, G., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01294-4 · Cited by 38