Jalview Version 2—a multiple sequence alignment editor and analysis workbench

Antibody variable sequences have a pronounced effect on cellular transport and plasma half-life

Grevys, A., Frick, R., Mester, S., Flem-Karlsen, K., Nilsen, J., Foss, S., Sand, K. M. K., Emrich, T., Fischer, J. A. A., Greiff, V., et al. (2022) · iScience · doi:10.1016/j.isci.2022.103746 · Cited by 51

Structure of Anabaena flos-aquae gas vesicles revealed by cryo-ET

Dutka, P., Metskas, L. A., Hurt, R. C., Salahshoor, H., Wang, T.-Y., Malounda, D., Lu, G. J., Chou, T.-F., Shapiro, M. G., & Jensen, G. J. (2023) · Structure · doi:10.1016/j.str.2023.03.011 · Cited by 51

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

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

The Evolutionary Conserved γ-Core Motif Influences the Anti-Candida Activity of the Penicillium chrysogenum Antifungal Protein PAF

Sonderegger, C., Váradi, G., Galgóczy, L., Kocsubé, S., Posch, W., Borics, A., Dubrac, S., Tóth, G. K., Wilflingseder, D., & Marx, F. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01655 · Cited by 48

DIP/Dpr interactions and the evolutionary design of specificity in protein families

Sergeeva, A. P., Katsamba, P. S., Cosmanescu, F., Brewer, J. J., Ahlsen, G., Mannepalli, S., Shapiro, L., & Honig, B. (2020) · Nature Communications · doi:10.1038/s41467-020-15981-8 · Cited by 38

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

Conoid extrusion regulates glideosome assembly to control motility and invasion in Apicomplexa

Dos Santos Pacheco, N., Brusini, L., Haase, R., Tosetti, N., Maco, B., Brochet, M., Vadas, O., & Soldati-Favre, D. (2022) · Nature Microbiology · doi:10.1038/s41564-022-01212-x · 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

Antibacterial T6SS effectors with a VRR-Nuc domain are structure-specific nucleases

Hespanhol, J. T., Sanchez-Limache, D. E., Nicastro, G. G., Mead, L., Llontop, E. E., Chagas-Santos, G., Farah, C. S., de Souza, R. F., Galhardo, R. D. S., Lovering, A. L., et al. (2022) · eLife · doi:10.7554/elife.82437 · Cited by 45

Pyruvate kinase variant of fission yeast tunes carbon metabolism, cell regulation, growth and stress resistance

Kamrad, S., Grossbach, J., Rodríguez‐López, M., Mülleder, M., Townsend, S., Cappelletti, V., Stojanovski, G., Correia‐Melo, C., Picotti, P., Beyer, A., et al. (2020) · Molecular Systems Biology · doi:10.15252/msb.20199270 · Cited by 40

The Iron Deficiency-Regulated Small Protein Effector FEP3/IRON MAN1 Modulates Interaction of BRUTUS-LIKE1 With bHLH Subgroup IVc and POPEYE Transcription Factors

Lichtblau, D. M., Schwarz, B., Baby, D., Endres, C., Sieberg, C., & Bauer, P. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.930049 · Cited by 43

Regulatory sites in the Mon1–Ccz1 complex control Rab5 to Rab7 transition and endosome maturation

Borchers, A.-C., Janz, M., Schäfer, J.-H., Moeller, A., Kümmel, D., Paululat, A., Ungermann, C., & Langemeyer, L. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2303750120 · Cited by 43

The structure of apolipoprotein B100 from human low-density lipoprotein

Berndsen, Z. T., & Cassidy, C. K. (2025) · Nature · doi:10.1038/s41586-024-08467-w · Cited by 43

Genome-encoded ABCF factors implicated in intrinsic antibiotic resistance in Gram-positive bacteria: VmlR2, Ard1 and CplR

Obana, N., Takada, H., Crowe-McAuliffe, C., Iwamoto, M., Egorov, A. A., Wu, K. J. Y., Chiba, S., Murina, V., Paternoga, H., Tresco, B. I. C., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad193 · Cited by 42

Structure of the human outer kinetochore KMN network complex

Yatskevich, S., Yang, J., Bellini, D., Zhang, Z., & Barford, D. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01249-y · Cited by 42

Lim homeobox genes in the Ctenophore Mnemiopsis leidyi: the evolution of neural cell type specification

Simmons, D. K., Pang, K., & Martindale, M. Q. (2012) · EvoDevo · doi:10.1186/2041-9139-3-2 · Cited by 38

Mechanism of ribosome-associated mRNA degradation during tubulin autoregulation

Höpfler, M., Absmeier, E., Peak-Chew, S.-Y., Vartholomaiou, E., Passmore, L. A., Gasic, I., & Hegde, R. S. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.05.020 · Cited by 41

Inhibition of HTLV-1 Infection by HIV-1 First- and Second-Generation Integrase Strand Transfer Inhibitors

Barski, M. S., Minnell, J. J., & Maertens, G. N. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01877 · Cited by 37

The structure of HiSiaQM defines the architecture of tripartite ATP-independent periplasmic (TRAP) transporters

Peter, M. F., Depping, P., Schneberger, N., Severi, E., Gatterdam, K., Tindall, S., Durand, A., Heinz, V., Koenig, P.-A., Geyer, M., et al. (2021) · doi:10.1101/2021.12.03.471092 · Cited by 38

Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter

Peter, M. F., Ruland, J. A., Depping, P., Schneberger, N., Severi, E., Moecking, J., Gatterdam, K., Tindall, S., Durand, A., Heinz, V., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31907-y · Cited by 38

A modified TurboID approach identifies tissue-specific centriolar components in C. elegans

Holzer, E., Rumpf-Kienzl, C., Falk, S., & Dammermann, A. (2022) · PLOS Genetics · doi:10.1371/journal.pgen.1010150 · Cited by 37

CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae

Weaver, S. J., Ortega, D. R., Sazinsky, M. H., Dalia, T. N., Dalia, A. B., & Jensen, G. J. (2020) · Nature Communications · doi:10.1038/s41467-020-18866-y · Cited by 37

PLK1-mediated phosphorylation cascade activates Mis18 complex to ensure centromere inheritance

Parashara, P., Medina-Pritchard, B., Abad, M. A., Sotelo-Parrilla, P., Thamkachy, R., Grundei, D., Zou, J., Spanos, C., Kumar, C. N., Basquin, C., et al. (2024) · Science · doi:10.1126/science.ado8270 · Cited by 36

Genome and metabolic network of “Candidatus Phaeomarinobacter ectocarpi” Ec32, a new candidate genus of Alphaproteobacteria frequently associated with brown algae

Dittami, S. M., Barbeyron, T., Boyen, C., Cambefort, J., Collet, G., Delage, L., Gobet, A., Groisillier, A., Leblanc, C., Michel, G., et al. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00241 · Cited by 35

Human MARF1 is an endoribonuclease that interacts with the DCP1:2 decapping complex and degrades target mRNAs

Nishimura, T., Fakim, H., Brandmann, T., Youn, J.-Y., Gingras, A.-C., Jinek, M., & Fabian, M. R. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky1011 · Cited by 31

Cryo-EM structure of the Smc5/6 holo-complex

Hallett, S. T., Campbell Harry, I., Schellenberger, P., Zhou, L., Cronin, N. B., Baxter, J., Etheridge, T. J., Murray, J. M., & Oliver, A. W. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac692 · Cited by 35

A MIR4646 associated methylation locus is hypomethylated in adolescent depression

Boström, A. E., Ciuculete, D.-M., Attwood, M., Krattinger, R., Nikontovic, L., Titova, O. E., Kullak-Ublick, G. A., Mwinyi, J., & Schiöth, H. B. (2017) · Journal of Affective Disorders · doi:10.1016/j.jad.2017.05.017 · Cited by 33

Structures of tweety homolog proteins TTYH2 and TTYH3 reveal a Ca2+-dependent switch from intra- to intermembrane dimerization

Li, B., Hoel, C. M., & Brohawn, S. G. (2021) · Nature Communications · doi:10.1038/s41467-021-27283-8 · Cited by 31

Stable kinetochore‐microtubule attachment requires loop‐dependent Ndc80‐Ndc80 binding

Polley, S., Müschenborn, H., Terbeck, M., De Antoni, A., Vetter, I. R., Dogterom, M., Musacchio, A., Volkov, V. A., & Huis in 't Veld, P. J. (2023) · The EMBO Journal · doi:10.15252/embj.2022112504 · Cited by 31

Discovery of EMRE in fungi resolves the true evolutionary history of the mitochondrial calcium uniporter

Pittis, A. A., Goh, V., Cebrian-Serrano, A., Wettmarshausen, J., Perocchi, F., & Gabaldón, T. (2020) · Nature Communications · doi:10.1038/s41467-020-17705-4 · Cited by 29

Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16INK4A

Göbl, C., Morris, V. K., van Dam, L., Visscher, M., Polderman, P. E., Hartlmüller, C., de Ruiter, H., Hora, M., Liesinger, L., Birner-Gruenberger, R., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2019.101316 · Cited by 29

Insights into the conservation and diversification of the molecular functions of YTHDF proteins

(2023) · doi:10.1371/journal.pgen.1010980 · Cited by 29

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

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

First nosocomial cluster of COVID-19 due to the Delta variant in a major acute care hospital in Singapore: investigations and outbreak response.

Lim, W.-Y., Tan, G. S. E., Htun, H. L., Phua, H. P., Kyaw, W. M., Guo, H., Cui, L., Mak, T. M., Poh, B. F., Wong, J. C. C., et al. (2022) · Journal of Hospital Infection · doi:10.1016/j.jhin.2021.12.011 · Cited by 26

A multiscale approach reveals the molecular architecture of the autoinhibited kinesin KIF5A

Carrington, G., Fatima, U., Caramujo, I., Lewis, T., Casas-Mao, D., & Peckham, M. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105713 · Cited by 26

The Sperm Protein Spaca6 is Essential for Fertilization in Zebrafish

Binner, M. I., Kogan, A., Panser, K., Schleiffer, A., Deneke, V. E., & Pauli, A. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.806982 · Cited by 25

Exonic knockout and knockin gene editing in hematopoietic stem and progenitor cells rescues RAG1 immunodeficiency

Castiello, M. C., Brandas, C., Ferrari, S., Porcellini, S., Sacchetti, N., Canarutto, D., Draghici, E., Merelli, I., Barcella, M., Pelosi, G., et al. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adh8162 · Cited by 25

Hypermethylation-associated downregulation of microRNA-4456 in hypersexual disorder with putative influence on oxytocin signalling: A DNA methylation analysis of miRNA genes

Boström, A. E., Chatzittofis, A., Ciuculete, D.-M., Flanagan, J. N., Krattinger, R., Bandstein, M., Mwinyi, J., Kullak-Ublick, G. A., Öberg, K. G., Arver, S., et al. (2020) · Epigenetics · doi:10.1080/15592294.2019.1656157 · Cited by 25

Vision-related convergent gene losses reveal SERPINE3’s unknown role in the eye

Indrischek, H., Hammer, J., Machate, A., Hecker, N., Kirilenko, B., Roscito, J., Hans, S., Norden, C., Brand, M., & Hiller, M. (2022) · eLife · doi:10.7554/elife.77999 · Cited by 21

Molecular profiling of sponge deflation reveals an ancient relaxant-inflammatory response

Ruperti, F., Becher, I., Stokkermans, A., Wang, L., Marschlich, N., Potel, C., Maus, E., Stein, F., Drotleff, B., Schippers, K. J., et al. (2024) · Current Biology · doi:10.1016/j.cub.2023.12.021 · Cited by 23

Amino Acid Substitutions in the Aryl Hydrocarbon Receptor Ligand Binding Domain Reveal YH439 As an Atypical AhR Activator

Whelan, F., Hao, N., Furness, S. G. B., Whitelaw, M. L., & Chapman-Smith, A. (2010) · Molecular Pharmacology · doi:10.1124/mol.109.062927 · Cited by 22

Conserved regulatory motifs in the juxtamembrane domain and kinase N-lobe revealed through deep mutational scanning of the MET receptor tyrosine kinase domain

Estevam, G. O., Linossi, E. M., Macdonald, C. B., Espinoza, C. A., Michaud, J. M., Coyote-Maestas, W., Collisson, E. A., Jura, N., & Fraser, J. S. (2024) · eLife · doi:10.7554/elife.91619 · Cited by 22

Deep embeddings to comprehend and visualize microbiome protein space

Odrzywolek, K., Karwowska, Z., Majta, J., Byrski, A., Milanowska-Zabel, K., & Kosciolek, T. (2022) · Scientific Reports · doi:10.1038/s41598-022-14055-7 · Cited by 22

Characterization of the membrane interactions of phospholipase Cγ reveals key features of the active enzyme

Le Huray, K. I. P., Bunney, T. D., Pinotsis, N., Kalli, A. C., & Katan, M. (2022) · Science Advances · doi:10.1126/sciadv.abp9688 · Cited by 21

RSL24D1 sustains steady-state ribosome biogenesis and pluripotency translational programs in embryonic stem cells

Durand, S., Bruelle, M., Bourdelais, F., Bennychen, B., Blin-Gonthier, J., Isaac, C., Huyghe, A., Martel, S., Seyve, A., Vanbelle, C., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36037-7 · Cited by 21

BRCA2 stabilises RAD51 and DMC1 nucleoprotein filaments through a conserved interaction mode

(2024) · doi:10.1038/s41467-024-52699-3 · Cited by 21

Evidence of microbial reductive dehalogenation in deep-sea cold seeps and its implications for biogeochemical cycles

Han, Y., Deng, Z., Peng, Y., Peng, J., Cao, L., Xu, Y., Yang, Y., Zhou, H., Zhang, C., Zhang, D., et al. (2025) · Microbiome · doi:10.1186/s40168-025-02147-1 · Cited by 21

Genotypic, proteomic, and phenotypic approaches to decipher the response to caspofungin and calcineurin inhibitors in clinical isolates of echinocandin-resistant Candida glabrata

Ceballos-Garzon, A., Monteoliva, L., Gil, C., Alvarez-Moreno, C., Vega-Vela, N. E., Engelthaler, D. M., Bowers, J., Le Pape, P., & Parra-Giraldo, C. M. (2022) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/dkab454 · Cited by 18

A comprehensive WGS-based pipeline for the identification of new candidate genes in inherited retinal dystrophies

González-del Pozo, M., Fernández-Suárez, E., Bravo-Gil, N., Méndez-Vidal, C., Martín-Sánchez, M., Rodríguez-de la Rúa, E., Ramos-Jiménez, M., Morillo-Sánchez, M. J., Borrego, S., & Antiñolo, G. (2022) · npj Genomic Medicine · doi:10.1038/s41525-022-00286-0 · Cited by 21

Structural and biophysical analysis of a Haemophilus influenzae tripartite ATP-independent periplasmic (TRAP) transporter

Currie, M. J., Davies, J. S., Scalise, M., Gulati, A., Wright, J. D., Newton-Vesty, M. C., Abeysekera, G. S., Subramanian, R., Wahlgren, W. Y., Friemann, R., et al. (2024) · eLife · doi:10.7554/elife.92307.3 · Cited by 20

Missense Variants Reveal Functional Insights Into the Human ARID Family of Gene Regulators

Deák, G., & Cook, A. G. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167529 · Cited by 20

Genome Mining and Characterization of Two Novel Lacticaseibacillus rhamnosus Probiotic Candidates with Bile Salt Hydrolase Activity

Agolino, G., Cristofolini, M., Vaccalluzzo, A., Tagliazucchi, D., Cattivelli, A., Pino, A., Caggia, C., Solieri, L., & Randazzo, C. L. (2025) · Biomolecules · doi:10.3390/biom15010086 · Cited by 19

The hGID GID4 E3 ubiquitin ligase complex targets ARHGAP11A to regulate cell migration

(2024) · doi:10.26508/lsa.202403046 · Cited by 19

Bioinformatics Analysis of Bacterial Annexins – Putative Ancestral Relatives of Eukaryotic Annexins

Kodavali, P. K., Dudkiewicz, M., Pikuła, S., & Pawłowski, K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0085428 · Cited by 18

MAP9/MAPH-9 supports axonemal microtubule doublets and modulates motor movement

Tran, M. V., Khuntsariya, D., Fetter, R. D., Ferguson, J. W., Wang, J. T., Long, A. F., Cote, L. E., Wellard, S. R., Vázquez-Martínez, N., Sallee, M. D., et al. (2024) · Developmental Cell · doi:10.1016/j.devcel.2023.12.001 · Cited by 18

Repeated duplications and losses shaped SMC complex evolution from archaeal ancestors to modern eukaryotes

van Hooff, J. J. E., Raas, M. W. D., Tromer, E. C., & Eme, L. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115855 · Cited by 18

Zebrafish Ski7 tunes RNA levels during the oocyte-to-embryo transition

Cabrera-Quio, L. E., Schleiffer, A., Mechtler, K., & Pauli, A. (2021) · PLOS Genetics · doi:10.1371/journal.pgen.1009390 · Cited by 18

Cryo-EM structures of apo-APC/C and APC/CCDH1:EMI1 complexes provide insights into APC/C regulation

Höfler, A., Yu, J., Yang, J., Zhang, Z., Chang, L., McLaughlin, S. H., Grime, G. W., Garman, E. F., Boland, A., & Barford, D. (2024) · Nature Communications · doi:10.1038/s41467-024-54398-5 · Cited by 18

Hsa-mir-548 family expression in human reproductive tissues

Rooda, I., Kaselt, B., Liivrand, M., Smolander, O.-P., Salumets, A., & Velthut-Meikas, A. (2021) · BMC Genomic Data · doi:10.1186/s12863-021-00997-w · Cited by 17

Docking Domain Engineering in a Modular Polyketide Synthase and Its Impact on Structure and Function

Buyachuihan, L., Zhao, Y., Schelhas, C., & Grininger, M. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.3c00074 · Cited by 15

Structural basis for triacylglyceride extraction from mycobacterial inner membrane by MFS transporter Rv1410

(2023) · doi:10.1038/s41467-023-42073-0 · Cited by 14

Structural and functional properties of the transporter SLC26A6 reveal mechanism of coupled anion exchange

Tippett, D. N., Breen, C., Butler, S. J., Sawicka, M., & Dutzler, R. (2023) · eLife · doi:10.7554/elife.87178 · Cited by 14

Discovery of broadly‐neutralizing antibodies against brown recluse spider and Gadim scorpion sphingomyelinases using consensus toxins as antigens

Rivera‐de‐Torre, E., Lampadariou, S., Møiniche, M., Bohn, M. F., Kazemi, S. M., & Laustsen, A. H. (2024) · Protein Science · doi:10.1002/pro.4901 · Cited by 13

The human MRS2 magnesium-binding domain is a regulatory feedback switch for channel activity

Uthayabalan, S., Vishnu, N., Madesh, M., & Stathopulos, P. B. (2023) · Life Science Alliance · doi:10.26508/lsa.202201742 · Cited by 13

Regulation of the phosphoinositide code by phosphorylation of membrane readers

Kervin, T. A., & Overduin, M. (2021) · Cells · doi:10.3390/cells10051205 · Cited by 13

Kinetoplastid kinetochore proteins KKT14–KKT15 are divergent Bub1/BubR1–Bub3 proteins

Ballmer, D., Carter, W., van Hooff, J. J. E., Tromer, E. C., Ishii, M., Ludzia, P., & Akiyoshi, B. (2024) · Open Biology · doi:10.1098/rsob.240025 · Cited by 13

Molecular insights into the activation of Mre11-Rad50 endonuclease activity by Sae2/CtIP

Nicolas, Y., Bret, H., Cannavo, E., Acharya, A., Cejka, P., Borde, V., & Guerois, R. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.05.019 · Cited by 12

Structural basis of RECQL5-induced RNA polymerase II transcription braking and subsequent reactivation

Zhang, L., Gordiyenko, Y., Morgan, T., Franco, C., Tufegdžić Vidaković, A., & Zhang, S. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01586-6 · Cited by 12

Structure of full-length ERGIC-53 in complex with MCFD2 for cargo transport

Watanabe, S., Kise, Y., Yonezawa, K., Inoue, M., Shimizu, N., Nureki, O., & Inaba, K. (2024) · Nature Communications · doi:10.1038/s41467-024-46747-1 · Cited by 12

Duplication and neofunctionalization of a horizontally transferred xyloglucanase as a facet of the Red Queen coevolutionary dynamic

Attah, V., Milner, D. S., Fang, Y., Yan, X., Leonard, G., Heitman, J., Talbot, N. J., & Richards, T. A. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2218927121 · Cited by 11

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

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

Molecular mechanism targeting condensin for chromosome condensation

(2024) · doi:10.1038/s44318-024-00336-6 · Cited by 10

PERK-mediated antioxidant response is key for pathogen persistence in ticks

Rosche, K. L., Hurtado, J., Fisk, E. A., Vosbigian, K. A., Warren, A. L., Sidak-Loftis, L. C., Wright, S. J., Ramirez-Zepp, E., Park, J. M., & Shaw, D. K. (2023) · mSphere · doi:10.1128/msphere.00321-23 · Cited by 10

Cysteine Rich Intestinal Protein 2 is a copper-responsive regulator of skeletal muscle differentiation and metal homeostasis

Verdejo-Torres, O., Klein, D. C., Novoa-Aponte, L., Carrazco-Carrillo, J., Bonilla-Pinto, D., Rivera, A., Bakhshian, A., Fitisemanu, F. M., Jiménez-González, M. L., Flinn, L., et al. (2024) · PLOS Genetics · doi:10.1371/journal.pgen.1011495 · Cited by 10

Queuosine biosynthetic enzyme, QueE moonlights as a cell division regulator

Adeleye, S. A., & Yadavalli, S. S. (2024) · PLOS Genetics · doi:10.1371/journal.pgen.1011287 · Cited by 10

Helical reconstruction of VP39 reveals principles for baculovirus nucleocapsid assembly

(2024) · doi:10.1038/s41467-023-44596-y · Cited by 10

Structural journey of an insecticidal protein against western corn rootworm

Marini, G., Poland, B., Leininger, C., Lukoyanova, N., Spielbauer, D., Barry, J. K., Altier, D., Lum, A., Scolaro, E., Ortega, C. P., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-39891-7 · Cited by 9

Structural Insight into Geranylgeranyl Diphosphate Synthase (GGDPS) for Cancer Therapy

Pham, A. C., Holstein, S. A., & Borgstahl, G. E. O. (2024) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-23-0358 · Cited by 9

Systematic identification of Salmonella T6SS effectors uncovers diverse new families and lipid-targeting activities

Nicastro, G. G., Sibinelli-Sousa, S., Hespanhol, J. T., Santos, T. W. C., Munoz, J. P., Santos, R. S., Perez-Sepulveda, B. M., Miyamoto, S., Aravind, L., de Souza, R. F., et al. (2026) · PLOS Biology · doi:10.1371/journal.pbio.3003680 · Cited by 9

WIV, a protein domain found in a wide number of arthropod viruses, which probably facilitates infection

Karlin, D. G. (2024) · Journal of General Virology · doi:10.1099/jgv.0.001948 · Cited by 8

A unified analysis of evolutionary and population constraint in protein domains highlights structural features and pathogenic sites

MacGowan, S. A., Madeira, F., Britto-Borges, T., & Barton, G. J. (2024) · Communications Biology · doi:10.1038/s42003-024-06117-5 · Cited by 8

The SH protein of mumps virus is a druggable pentameric viroporin

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