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

Evolutionary adaptation of plant annexins has diversified their molecular structures, interactions and functional roles

Clark, G. B., Morgan, R. O., Fernandez, M., & Roux, S. J. (2012) · New Phytologist · doi:10.1111/j.1469-8137.2012.04308.x · Cited by 150

Structural insights into integrin α 5 β 1 opening by fibronectin ligand

Schumacher, S., Dedden, D., Nunez, R. V., Matoba, K., Takagi, J., Biertümpfel, C., & Mizuno, N. (2021) · Science Advances · doi:10.1126/sciadv.abe9716 · Cited by 150

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

Structural basis for channel conduction in the pump-like channelrhodopsin ChRmine

Kishi, K. E., Kim, Y. S., Fukuda, M., Inoue, M., Kusakizako, T., Wang, P. Y., Ramakrishnan, C., Byrne, E. F. X., Thadhani, E., Paggi, J. M., et al. (2022) · Cell · doi:10.1016/j.cell.2022.01.007 · Cited by 149

Structure of the SecY channel during initiation of protein translocation

Park, E., Ménétret, J.-F., Gumbart, J. C., Ludtke, S. J., Li, W., Whynot, A., Rapoport, T. A., & Akey, C. W. (2014) · Nature · doi:10.1038/nature12720 · Cited by 148

The structure of human thyroglobulin

Coscia, F., Taler-Verčič, A., Chang, V. T., Sinn, L., O’Reilly, F. J., Izoré, T., Renko, M., Berger, I., Rappsilber, J., Turk, D., et al. (2020) · Nature · doi:10.1038/s41586-020-1995-4 · Cited by 147

Architecture of human Rag GTPase heterodimers and their complex with mTORC1

Anandapadamanaban, M., Masson, G. R., Perisic, O., Berndt, A., Kaufman, J., Johnson, C. M., Santhanam, B., Rogala, K. B., Sabatini, D. M., & Williams, R. L. (2019) · Science · doi:10.1126/science.aax3939 · Cited by 147

Physiological roles of ovotransferrin

Giansanti, F., Leboffe, L., Pitari, G., Ippoliti, R., & Antonini, G. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.08.004 · Cited by 145

A structural biology community assessment of AlphaFold 2 applications

Akdel, M., Pires, D. E. V., Porta Pardo, E., Jänes, J., Zalevsky, A. O., Mészáros, B., Bryant, P., Good, L. L., Laskowski, R. A., Pozzati, G., et al. (2021) · doi:10.1101/2021.09.26.461876 · Cited by 122

Inhibition of Fatty Acid Binding Proteins Elevates Brain Anandamide Levels and Produces Analgesia

Kaczocha, M., Rebecchi, M. J., Ralph, B. P., Teng, Y.-H. G., Berger, W. T., Galbavy, W., Elmes, M. W., Glaser, S. T., Wang, L., Rizzo, R. C., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094200 · Cited by 142

Novel AAV capsids for intravitreal gene therapy of photoreceptor disorders

Pavlou, M., Schön, C., Occelli, L. M., Rossi, A., Meumann, N., Boyd, R. F., Bartoe, J. T., Siedlecki, J., Gerhardt, M. J., Babutzka, S., et al. (2021) · EMBO Molecular Medicine · doi:10.15252/emmm.202013392 · Cited by 135

Inner lumen proteins stabilize doublet microtubules in cilia and flagella

Owa, M., Uchihashi, T., Yanagisawa, H.-A., Yamano, T., Iguchi, H., Fukuzawa, H., Wakabayashi, K.-I., Ando, T., & Kikkawa, M. (2019) · Nature Communications · doi:10.1038/s41467-019-09051-x · Cited by 140

Structural basis for retroviral integration into nucleosomes

Maskell, D. P., Renault, L., Serrao, E., Lesbats, P., Matadeen, R., Hare, S., Lindemann, D., Engelman, A. N., Costa, A., & Cherepanov, P. (2015) · Nature · doi:10.1038/nature14495 · Cited by 138

Stabilizing the Pro-Apoptotic BimBH3 Helix (BimSAHB) Does Not Necessarily Enhance Affinity or Biological Activity

Okamoto, T., Zobel, K., Fedorova, A., Quan, C., Yang, H., Fairbrother, W. J., Huang, D. C. S., Smith, B. J., Deshayes, K., & Czabotar, P. E. (2013) · ACS Chemical Biology · doi:10.1021/cb3005403 · Cited by 136

Asymmetric Molecular Architecture of the Human γ-Tubulin Ring Complex

Wieczorek, M., Urnavicius, L., Ti, S.-C., Molloy, K. R., Chait, B. T., & Kapoor, T. M. (2020) · Cell · doi:10.1016/j.cell.2019.12.007 · Cited by 136

Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2

Pádua, R. A. P., Sun, Y., Marko, I., Pitsawong, W., Stiller, J. B., Otten, R., & Kern, D. (2018) · Nature Communications · doi:10.1038/s41467-018-06814-w · Cited by 133

Cryo-EM structure of the agonist-bound Hsp90-XAP2-AHR cytosolic complex

Gruszczyk, J., Grandvuillemin, L., Lai-Kee-Him, J., Paloni, M., Savva, C. G., Germain, P., Grimaldi, M., Boulahtouf, A., Kwong, H.-S., Bous, J., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34773-w · Cited by 137

Understanding the challenges of protein flexibility in drug design.

Antunes, D. A., Devaurs, D., & Kavraki, L. E. (2015) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2015.1094458 · Cited by 131

The structural coverage of the human proteome before and after AlphaFold

Porta-Pardo, E., Ruiz-Serra, V., Valentini, S., & Valencia, A. (2022) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1009818 · Cited by 131

Proton transport and pH control in fungi

Kane, P. M. (2016) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-319-25304-6_3 · Cited by 131

Structural and functional insights into the mode of action of a universally conserved Obg GTPase.

Feng, B., Mandava, C. S., Guo, Q., Wang, J., Cao, W., Li, N., Zhang, Y., Zhang, Y., Wang, Z., Wu, J., et al. (2014) · PLoS Biology · doi:10.1371/journal.pbio.1001866 · Cited by 129

Plant-made polio type 3 stabilized VLPs-a candidate synthetic polio vaccine

Marsian, J., Fox, H., Bahar, M. W., Kotecha, A., Fry, E. E., Stuart, D. I., Macadam, A. J., Rowlands, D. J., & Lomonossoff, G. P. (2017) · Nature Communications · doi:10.1038/s41467-017-00090-w · Cited by 121

Nuclear and cytoplasmic huntingtin inclusions exhibit distinct biochemical composition, interactome and ultrastructural properties

Riguet, N., Mahul-Mellier, A.-L., Maharjan, N., Burtscher, J., Croisier, M., Knott, G., Hastings, J., Patin, A., Reiterer, V., Farhan, H., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26684-z · Cited by 118

Capsid antibodies to different adeno-associated virus serotypes bind common regions

Gurda, B. L., DiMattia, M. A., Miller, E. B., Bennett, A., McKenna, R., Weichert, W. S., Nelson, C. D., Chen, W.-J., Muzyczka, N., Olson, N. H., et al. (2013) · Journal of Virology · doi:10.1128/jvi.00622-13 · Cited by 127

Human germline heterozygous gain-of-function STAT6 variants cause severe allergic disease

Sharma, M., Leung, D., Momenilandi, M., Jones, L. C. W., Pacillo, L., James, A. E., Murrell, J. R., Delafontaine, S., Maimaris, J., Vaseghi-Shanjani, M., et al. (2023) · Journal of Experimental Medicine · doi:10.1084/jem.20221755 · Cited by 125

Genome-wide analysis and expression profiling of the DREB transcription factor gene family in Malus under abiotic stress

Zhao, T., Liang, D., Wang, P., Liu, J., & Ma, F. (2012) · Molecular Genetics and Genomics · doi:10.1007/s00438-012-0687-7 · Cited by 123

Interplay between hydrophilicity and surface barriers on water transport in zeolite membranes

Fasano, M., Humplik, T., Bevilacqua, A., Tsapatsis, M., Chiavazzo, E., Wang, E. N., & Asinari, P. (2016) · Nature Communications · doi:10.1038/ncomms12762 · Cited by 123

Structural basis for species-selective targeting of Hsp90 in a pathogenic fungus

Whitesell, L., Robbins, N., Huang, D. S., McLellan, C. A., Shekhar-Guturja, T., LeBlanc, E. V., Nation, C. S., Hui, R., Hutchinson, A., Collins, C., et al. (2019) · Nature Communications · doi:10.1038/s41467-018-08248-w · Cited by 124

XPA: A key scaffold for human nucleotide excision repair

Sugitani, N., Sivley, R. M., Perry, K. E., Capra, J. A., & Chazin, W. J. (2016) · DNA Repair · doi:10.1016/j.dnarep.2016.05.018 · Cited by 116

Machine learning modeling of family wide enzyme-substrate specificity screens

Goldman, S., Das, R., Yang, K. K., & Coley, C. W. (2022) · PLOS Computational Biology · doi:10.1371/journal.pcbi.1009853 · Cited by 120

Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme

Sui, X., Wang, K., Gluchowski, N. L., Elliott, S. D., Liao, M., Walther, T. C., & Farese, R. V. (2020) · Nature · doi:10.1038/s41586-020-2289-6 · Cited by 120

Structure of the human signal peptidase complex reveals the determinants for signal peptide cleavage

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Imaging proteins at the single-molecule level

Longchamp, J.-N., Rauschenbach, S., Abb, S., Escher, C., Latychevskaia, T., Kern, K., & Fink, H.-W. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1614519114 · Cited by 119

KRAS as a druggable target in NSCLC: Rising like a phoenix after decades of development failures

Friedlaender, A., Drilon, A., Weiss, G. J., Banna, G. L., & Addeo, A. (2020) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2020.101978 · Cited by 118

Conformational buffering underlies functional selection in intrinsically disordered protein regions

González-Foutel, N. S., Glavina, J., Borcherds, W. M., Safranchik, M., Barrera-Vilarmau, S., Sagar, A., Estaña, A., Barozet, A., Garrone, N. A., Fernandez-Ballester, G., et al. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00811-w · Cited by 118

Towards elucidating the stability, dynamics and architecture of the nucleosome remodeling and deacetylase complex by using quantitative interaction proteomics

Kloet, S. L., Baymaz, H. I., Makowski, M., Groenewold, V., Jansen, P. W. T. C., Berendsen, M., Niazi, H., Kops, G. J., & Vermeulen, M. (2015) · The FEBS Journal · doi:10.1111/febs.12972 · Cited by 107

SARS-CoV-2 RBD in vitro evolution follows contagious mutation spread, yet generates an able infection inhibitor

Zahradník, J., Marciano, S., Shemesh, M., Zoler, E., Chiaravalli, J., Meyer, B., Rudich, Y., Dym, O., Elad, N., & Schreiber, G. (2021) · doi:10.1101/2021.01.06.425392 · Cited by 458

Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon

Jomaa, A., Boehringer, D., Leibundgut, M., & Ban, N. (2016) · Nature Communications · doi:10.1038/ncomms10471 · Cited by 115

An Endoplasmic Reticulum (ER) Membrane Complex Composed of SPFH1 and SPFH2 Mediates the ER-associated Degradation of Inositol 1,4,5-Trisphosphate Receptors

Pearce, M. M. P., Wormer, D. B., Wilkens, S., & Wojcikiewicz, R. J. H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809801200 · Cited by 114

Hsp90: A New Player in DNA Repair?

Pennisi, R., Ascenzi, P., & Di Masi, A. (2015) · Biomolecules · doi:10.3390/biom5042589 · Cited by 112

The structure of human CST reveals a decameric assembly bound to telomeric DNA

Lim, C. J., Barbour, A. T., Zaug, A. J., Goodrich, K. J., McKay, A. E., Wuttke, D. S., & Cech, T. R. (2020) · Science · doi:10.1126/science.aaz9649 · Cited by 111

Heparin binding induces conformational changes in Adeno-associated virus serotype 2

Levy, H. C., Bowman, V. D., Govindasamy, L., McKenna, R., Nash, K., Warrington, K., Chen, W., Muzyczka, N., Yan, X., Baker, T. S., et al. (2009) · Journal of Structural Biology · doi:10.1016/j.jsb.2008.12.002 · Cited by 110

USP7-specific inhibitors target and modify the enzyme’s active site via distinct chemical mechanisms.

Pozhidaeva, A., Valles, G., Wang, F., Wu, J., Sterner, D. E., Nguyen, P., Weinstock, J., Kumar, K. G. S., Kanyo, J., Wright, D., et al. (2017) · Cell Chemical Biology · doi:10.1016/j.chembiol.2017.09.004 · Cited by 107

AlphaFold2 reveals commonalities and novelties in protein structure space for 21 model organisms

Bordin, N., Sillitoe, I., Nallapareddy, V., Rauer, C., Lam, S. D., Waman, V. P., Sen, N., Heinzinger, M., Littmann, M., Kim, S., et al. (2023) · Communications Biology · doi:10.1038/s42003-023-04488-9 · Cited by 103

Structure of the CLC-1 chloride channel from Homo sapiens

Park, E., & MacKinnon, R. (2018) · eLife · doi:10.7554/elife.36629 · Cited by 109

Machine learning consensus scoring improves performance across targets in structure-based virtual screening.

Ericksen, S. S., Wu, H., Zhang, H., Michael, L. A., Newton, M. A., Hoffmann, F. M., & Wildman, S. A. (2017) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.7b00153 · Cited by 107

Mechanisms of Channel Block in Calcium-Permeable AMPA Receptors

Twomey, E. C., Yelshanskaya, M. V., Vassilevski, A. A., & Sobolevsky, A. I. (2018) · Neuron · doi:10.1016/j.neuron.2018.07.027 · Cited by 106

Cryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assembly

Bharat, T. A. M., Castillo Menendez, L. R., Hagen, W. J. H., Lux, V., Igonet, S., Schorb, M., Schur, F. K. M., Kräusslich, H.-G., & Briggs, J. A. G. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401455111 · Cited by 107

Structural basis for strand-transfer inhibitor binding to HIV intasomes

Passos, D. O., Li, M., Jóźwik, I. K., Zhao, X. Z., Santos-Martins, D., Yang, R., Smith, S. J., Jeon, Y., Forli, S., Hughes, S. H., et al. (2020) · Science · doi:10.1126/science.aay8015 · Cited by 106

The SMC-family Wadjet complex protects bacteria from plasmid transformation by recognition and cleavage of closed-circular DNA

Deep, A., Gu, Y., Gao, Y.-Q., Ego, K. M., Herzik, M. A., Zhou, H., & Corbett, K. D. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.09.008 · Cited by 106

Characterization and structural basis of a lethal mouse-adapted SARS-CoV-2

Sun, S., Gu, H., Cao, L., Chen, Q., Ye, Q., Yang, G., Li, R.-T., Fan, H., Deng, Y.-Q., Song, X., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25903-x · Cited by 104

The role of protonation states in ligand-receptor recognition and binding.

Petukh, M., Stefl, S., & Alexov, E. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319230004 · Cited by 101

The Role of Ovotransferrin in Egg-White Antimicrobial Activity: A Review

Legros, J., Jan, S., Bonnassie, S., Gautier, M., Croguennec, T., Pezennec, S., Cochet, M.-F., Nau, F., Andrews, S. C., & Baron, F. (2021) · Foods · doi:10.3390/foods10040823 · Cited by 102

A structure of human Scap bound to Insig-2 suggests how their interaction is regulated by sterols

Yan, R., Cao, P., Song, W., Qian, H., Du, X., Coates, H. W., Zhao, X., Li, Y., Gao, S., Gong, X., et al. (2021) · Science · doi:10.1126/science.abb2224 · Cited by 100

Visualization of clustered protocadherin neuronal self-recognition complexes

Brasch, J., Goodman, K. M., Noble, A. J., Rapp, M., Mannepalli, S., Bahna, F., Dandey, V. P., Bepler, T., Berger, B., Maniatis, T., et al. (2019) · Nature · doi:10.1038/s41586-019-1089-3 · Cited by 99

Membrane-anchored HDCR nanowires drive hydrogen-powered CO2 fixation

Dietrich, H. M., Righetto, R. D., Kumar, A., Wietrzynski, W., Trischler, R., Schuller, S. K., Wagner, J., Schwarz, F. M., Engel, B. D., Müller, V., et al. (2022) · Nature · doi:10.1038/s41586-022-04971-z · Cited by 99

Cryo-EM structures of NPC1L1 reveal mechanisms of cholesterol transport and ezetimibe inhibition

Huang, C.-S., Yu, X., Fordstrom, P., Choi, K., Chung, B. C., Roh, S.-H., Chiu, W., Zhou, M., Min, X., & Wang, Z. (2020) · Science Advances · doi:10.1126/sciadv.abb1989 · Cited by 98

Structural insights into adeno-associated virus serotype 5

Govindasamy, L., DiMattia, M. A., Gurda, B. L., Halder, S., McKenna, R., Chiorini, J. A., Muzyczka, N., Zolotukhin, S., & Agbandje-McKenna, M. (2013) · Journal of Virology · doi:10.1128/jvi.00867-13 · Cited by 95

Pharmacotherapy Evolution in Alzheimer’s Disease: Current Framework and Relevant Directions

Miculas, D. C., Negru, P. A., Bungau, S. G., Behl, T., Hassan, S. S. U., & Tit, D. M. (2022) · Cells · doi:10.3390/cells12010131 · Cited by 96

Distribution and Redistribution of HIV-1 Nucleocapsid Protein in Immature, Mature, and Integrase-Inhibited Virions: a Role for Integrase in Maturation

Fontana, J., Jurado, K. A., Cheng, N., Ly, N. L., Fuchs, J. R., Gorelick, R. J., Engelman, A. N., & Steven, A. C. (2015) · Journal of Virology · doi:10.1128/jvi.01522-15 · Cited by 96

SuRVoS: Super-Region Volume Segmentation workbench

Luengo, I., Darrow, M. C., Spink, M. C., Sun, Y., Dai, W., He, C. Y., Chiu, W., Pridmore, T., Ashton, A. W., Duke, E. M. H., et al. (2017) · Journal of Structural Biology · doi:10.1016/j.jsb.2017.02.007 · Cited by 89

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

Structural and kinetic analysis of the COP9-Signalosome activation and the cullin-RING ubiquitin ligase deneddylation cycle

Mosadeghi, R., Reichermeier, K. M., Winkler, M., Schreiber, A., Reitsma, J. M., Zhang, Y., Stengel, F., Cao, J., Kim, M., Sweredoski, M. J., et al. (2016) · eLife · doi:10.7554/elife.12102 · Cited by 95

A structural mechanism for directing corepressor-selective inverse agonism of PPARγ

Brust, R., Shang, J., Fuhrmann, J., Mosure, S. A., Bass, J., Cano, A., Heidari, Z., Chrisman, I. M., Nemetchek, M. D., Blayo, A.-L., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07133-w · Cited by 94

The Impact of Inflammation-Induced Tumor Plasticity during Myeloid Transformation

Yeaton, A., Cayanan, G., Loghavi, S., Dolgalev, I., Leddin, E. M., Loo, C. E., Torabifard, H., Nicolet, D., Wang, J., Corrigan, K., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-1146 · Cited by 94

Characterization of the binding of MRTX1133 as an avenue for the discovery of potential KRASG12D inhibitors for cancer therapy

Issahaku, A. R., Mukelabai, N., Agoni, C., Rudrapal, M., Aldosari, S. M., Almalki, S. G., & Khan, J. (2022) · Scientific Reports · doi:10.1038/s41598-022-22668-1 · Cited by 93

Cholesterol binding does not predict activity of the steroidogenic acute regulatory protein, StAR

Baker, B. Y., Epand, R. F., Epand, R. M., & Miller, W. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611221200 · Cited by 89

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

Fusion protein strategies for cryo-EM study of G protein-coupled receptors

Zhang, K., Wu, H., Hoppe, N., Manglik, A., & Cheng, Y. (2022) · Nature Communications · doi:10.1038/s41467-022-32125-2 · Cited by 91

Determination of protein structure at 8.5 Å resolution using cryo-electron tomography and sub-tomogram averaging

Schur, F. K. M., Hagen, W. J. H., de Marco, A., & Briggs, J. A. G. (2013) · Journal of Structural Biology · doi:10.1016/j.jsb.2013.10.015 · Cited by 90

Metabolic control of BRISC-SHMT2 assembly regulates immune signalling

Walden, M., Tian, L., Ross, R. L., Sykora, U. M., Byrne, D. P., Hesketh, E. L., Masandi, S. K., Cassel, J., George, R., Ault, J. R., et al. (2019) · Nature · doi:10.1038/s41586-019-1232-1 · Cited by 85

Structure of PDE3A-SLFN12 complex reveals requirements for activation of SLFN12 RNase

Garvie, C. W., Wu, X., Papanastasiou, M., Lee, S., Fuller, J., Schnitzler, G. R., Horner, S. W., Baker, A., Zhang, T., Mullahoo, J. P., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24495-w · Cited by 85

Visualization of the HIV-1 Env glycan shield across scales

Berndsen, Z. T., Chakraborty, S., Wang, X., Cottrell, C. A., Torres, J. L., Diedrich, J. K., López, C. A., Yates, J. R., van Gils, M. J., Paulson, J. C., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2000260117 · Cited by 86

Structural Definition of a Neutralization-sensitive Epitope on the MERS-CoV S1-NTD

Wang, N., Rosen, O., Wang, L., Turner, H. L., Stevens, L. J., Corbett, K. S., Bowman, C. A., Pallesen, J., Shi, W., Zhang, Y., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.052 · Cited by 86

How Pol α-primase is targeted to replisomes to prime eukaryotic DNA replication

Jones, M. L., Aria, V., Baris, Y., & Yeeles, J. T. P. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.035 · Cited by 86

Structural basis of ion transport and inhibition in ferroportin

Pan, Y., Ren, Z., Gao, S., Shen, J., Wang, L., Xu, Z., Yu, Y., Bachina, P., Zhang, H., Fan, X., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19458-6 · Cited by 81

Intraflagellar transport dynein is autoinhibited by trapping of its mechanical and track-binding elements

Toropova, K., Mladenov, M., & Roberts, A. J. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3391 · Cited by 85

The Structures of Frataxin Oligomers Reveal the Mechanism for the Delivery and Detoxification of Iron

Karlberg, T., Schagerlöf, U., Gakh, O., Park, S., Ryde, U., Lindahl, M., Leath, K., Garman, E., Isaya, G., & Al-Karadaghi, S. (2006) · Structure · doi:10.1016/j.str.2006.08.010 · Cited by 85

The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state

Lee, K., Thwin, A. C., Nadel, C. M., Tse, E., Gates, S. N., Gestwicki, J. E., & Southworth, D. R. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.07.023 · Cited by 76

Structure of adeno-associated virus-2 in complex with neutralizing monoclonal antibody A20

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Perfluoroalkyl Substances (PFASs) Are Substrates of the Renal Human Organic Anion Transporter 4 (OAT4)

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