WebLogo: A Sequence Logo Generator: Figure 1

A somatic piRNA pathway in the Drosophila fat body ensures metabolic homeostasis and normal lifespan

Jones, B. C., Wood, J. G., Chang, C., Tam, A. D., Franklin, M. J., Siegel, E. R., & Helfand, S. L. (2016) · Nature Communications · doi:10.1038/ncomms13856 · Cited by 130

Acetate formation in the energy metabolism of parasitic helminths and protists

Tielens, A. G. M., van Grinsven, K. W. A., Henze, K., van Hellemond, J. J., & Martin, W. (2010) · International Journal for Parasitology · doi:10.1016/j.ijpara.2009.12.006 · Cited by 129

Candida glabrata environmental stress response involves Saccharomyces cerevisiae Msn2/4 orthologous transcription factors

Roetzer, A., Gregori, C., Jennings, A. M., Quintin, J., Ferrandon, D., Butler, G., Kuchler, K., Ammerer, G., & Schüller, C. (2008) · Molecular Microbiology · doi:10.1111/j.1365-2958.2008.06301.x · Cited by 124

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

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

(2021) · doi:10.1016/j.molcel.2021.07.031 · Cited by 120

Dynamic and scalable DNA-based information storage

Lin, K. N., Volkel, K., Tuck, J. M., & Keung, A. J. (2020) · Nature Communications · doi:10.1038/s41467-020-16797-2 · Cited by 117

A supramolecular assembly mediates lentiviral DNA integration

Ballandras-Colas, A., Maskell, D. P., Serrao, E., Locke, J., Swuec, P., Jónsson, S. R., Kotecha, A., Cook, N. J., Pye, V. E., Taylor, I. A., et al. (2017) · Science · doi:10.1126/science.aah7002 · Cited by 107

The roles of APOBEC-mediated RNA editing in SARS-CoV-2 mutations, replication and fitness

Kim, K., Calabrese, P., Wang, S., Qin, C., Rao, Y., Feng, P., & Chen, X. S. (2022) · Scientific Reports · doi:10.1038/s41598-022-19067-x · Cited by 115

Novel recognition motifs and biological functions of the RNA-binding protein HuD revealed by genome-wide identification of its targets

Bolognani, F., Contente-Cuomo, T., & Perrone-Bizzozero, N. I. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkp863 · Cited by 113

Zn-regulated GTPase metalloprotein activator 1 modulates vertebrate zinc homeostasis

Weiss, A., Murdoch, C. C., Edmonds, K. A., Jordan, M. R., Monteith, A. J., Perera, Y. R., Rodríguez Nassif, A. M., Petoletti, A. M., Beavers, W. N., Munneke, M. J., et al. (2022) · Cell · doi:10.1016/j.cell.2022.04.011 · Cited by 113

Transcription rate strongly affects splicing fidelity and cotranscriptionality in budding yeast

Aslanzadeh, V., Huang, Y., Sanguinetti, G., & Beggs, J. D. (2018) · Genome Research · doi:10.1101/gr.225615.117 · Cited by 109

The Calcineurin Signaling Network Evolves via Conserved Kinase-Phosphatase Modules that Transcend Substrate Identity

Goldman, A., Roy, J., Bodenmiller, B., Wanka, S., Landry, C. R., Aebersold, R., & Cyert, M. S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.05.012 · Cited by 109

Genome Data Mining and Soil Survey for the Novel Group 5 [NiFe]-Hydrogenase To Explore the Diversity and Ecological Importance of Presumptive High-Affinity H 2 -Oxidizing Bacteria

Constant, P., Chowdhury, S. P., Hesse, L., Pratscher, J., & Conrad, R. (2011) · Applied and Environmental Microbiology · doi:10.1128/aem.00673-11 · Cited by 105

Multiplexed relative and absolute quantitative immunopeptidomics reveals MHC I repertoire alterations induced by CDK4/6 inhibition

Stopfer, L. E., Mesfin, J. M., Joughin, B. A., Lauffenburger, D. A., & White, F. M. (2020) · Nature Communications · doi:10.1038/s41467-020-16588-9 · Cited by 109

β-Glucuronidases of opportunistic bacteria are the major contributors to xenobiotic-induced toxicity in the gut

Dashnyam, P., Mudududdla, R., Hsieh, T.-J., Lin, T.-C., Lin, H.-Y., Chen, P.-Y., Hsu, C.-Y., & Lin, C.-H. (2018) · Scientific Reports · doi:10.1038/s41598-018-34678-z · Cited by 108

Transcriptional regulation of Hepatic Stellate Cell activation in NASH

Marcher, A.-B., Bendixen, S. M., Terkelsen, M. K., Hohmann, S. S., Hansen, M. H., Larsen, B. D., Mandrup, S., Dimke, H., Detlefsen, S., & Ravnskjaer, K. (2019) · Scientific Reports · doi:10.1038/s41598-019-39112-6 · Cited by 95

Pushing the limits of de novo genome assembly for complex prokaryotic genomes harboring very long, near identical repeats

Schmid, M., Frei, D., Patrignani, A., Schlapbach, R., Frey, J. E., Remus-Emsermann, M. N. P., & Ahrens, C. H. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky726 · Cited by 92

Genome Analysis Reveals Interplay between 5′UTR Introns and Nuclear mRNA Export for Secretory and Mitochondrial Genes

Cenik, C., Chua, H. N., Zhang, H., Tarnawsky, S. P., Akef, A., Derti, A., Tasan, M., Moore, M. J., Palazzo, A. F., & Roth, F. P. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1001366 · Cited by 87

ATP synthase evolution on a cross-braced dated tree of life

Mahendrarajah, T. A., Moody, E. R. R., Schrempf, D., Szánthó, L. L., Dombrowski, N., Davín, A. A., Pisani, D., Donoghue, P. C. J., Szöllősi, G. J., Williams, T. A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42924-w · Cited by 86

Design of stimulus-responsive two-state hinge proteins

Praetorius, F., Leung, P. J. Y., Tessmer, M. H., Broerman, A., Demakis, C., Dishman, A. F., Pillai, A., Idris, A., Juergens, D., Dauparas, J., et al. (2023) · Science · doi:10.1126/science.adg7731 · Cited by 90

Phylogeny of Zebrafish, a “Model Species,” within Danio, a “Model Genus”

McCluskey, B. M., & Postlethwait, J. H. (2015) · Molecular Biology and Evolution · doi:10.1093/molbev/msu325 · Cited by 90

Genome-wide Analysis of Alternative Pre-mRNA Splicing and RNA-Binding Specificities of the Drosophila hnRNP A/B Family Members

Blanchette, M., Green, R. E., MacArthur, S., Brooks, A. N., Brenner, S. E., Eisen, M. B., & Rio, D. C. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.01.022 · Cited by 86

Perchlorate Reductase Is Distinguished by Active Site Aromatic Gate Residues

Youngblut, M. D., Tsai, C.-L., Clark, I. C., Carlson, H. K., Maglaqui, A. P., Gau-Pan, P. S., Redford, S. A., Wong, A., Tainer, J. A., & Coates, J. D. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.714618 · Cited by 88

Sequence signatures of two public antibody clonotypes that bind SARS-CoV-2 receptor binding domain

Tan, T. J. C., Yuan, M., Kuzelka, K., Padron, G. C., Beal, J. R., Chen, X., Wang, Y., Rivera-Cardona, J., Zhu, X., Stadtmueller, B. M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24123-7 · Cited by 75

A LAPF/phafin1-like protein regulates TORC1 and lysosomal membrane permeabilization in response to endoplasmic reticulum membrane stress

Kim, A., & Cunningham, K. W. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e15-08-0581 · Cited by 67

Arabidopsis mutant sk156 reveals complex regulation of SPL15 in a miR156-controlled gene network

Wei, S., Gruber, M. Y., Yu, B., Gao, M.-J., Khachatourians, G. G., Hegedus, D. D., Parkin, I. A., & Hannoufa, A. (2012) · BMC Plant Biology · doi:10.1186/1471-2229-12-169 · Cited by 73

Multiple determinants within iron-responsive elements dictate iron regulatory protein binding and regulatory hierarchy

Goforth, J. B., Anderson, S. A., Nizzi, C. P., & Eisenstein, R. S. (2010) · RNA · doi:10.1261/rna.1857210 · Cited by 71

Pervasive generation of oppositely oriented spacers during CRISPR adaptation

Shmakov, S., Savitskaya, E., Semenova, E., Logacheva, M. D., Datsenko, K. A., & Severinov, K. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku226 · Cited by 70

Genetic and structural basis for recognition of SARS-CoV-2 spike protein by a two-antibody cocktail

Dong, J., Zost, S. J., Greaney, A. J., Starr, T. N., Dingens, A. S., Chen, E. C., Chen, R. E., Case, J. B., Sutton, R. E., Gilchuk, P., et al. (2021) · doi:10.1101/2021.01.27.428529 · Cited by 55

Characterization and Repurposing of Type I and Type II CRISPR–Cas Systems in Bacteria

Hidalgo-Cantabrana, C., Goh, Y. J., & Barrangou, R. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.09.013 · Cited by 63

Key determinants of target DNA recognition by retroviral intasomes

Serrao, E., Ballandras-Colas, A., Cherepanov, P., Maertens, G. N., & Engelman, A. N. (2015) · Retrovirology · doi:10.1186/s12977-015-0167-3 · Cited by 62

Integrase residues that determine nucleotide preferences at sites of HIV-1 integration: implications for the mechanism of target DNA binding

Serrao, E., Krishnan, L., Shun, M.-C., Li, X., Cherepanov, P., Engelman, A., & Maertens, G. N. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku136 · Cited by 59

Electron bifurcation and fluoride efflux systems implicated in defluorination of perfluorinated unsaturated carboxylic acids by Acetobacterium spp

Yu, Y., Xu, F., Zhao, W., Thoma, C., Che, S., Richman, J. E., Jin, B., Zhu, Y., Xing, Y., Wackett, L., et al. (2024) · Science Advances · doi:10.1126/sciadv.ado2957 · Cited by 63

Cyclable Condensation and Hierarchical Assembly of Metastable Reflectin Proteins, the Drivers of Tunable Biophotonics

Levenson, R., Bracken, C., Bush, N., & Morse, D. E. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.686014 · Cited by 62

Transposon-encoded nucleases use guide RNAs to promote their selfish spread

Meers, C., Le, H. C., Pesari, S. R., Hoffmann, F. T., Walker, M. W. G., Gezelle, J., Tang, S., & Sternberg, S. H. (2023) · Nature · doi:10.1038/s41586-023-06597-1 · Cited by 60

Design of synthetic promoters for cyanobacteria with generative deep-learning model

Seo, E., Choi, Y.-N., Shin, Y. R., Kim, D., & Lee, J. W. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad451 · Cited by 61

Scalable empirical mixture models that account for across-site compositional heterogeneity

Schrempf, D., Lartillot, N., & Szöllősi, G. (2019) · doi:10.1101/794263 · Cited by 61

Comparisons of clustered regularly interspaced short palindromic repeats and viromes in human saliva reveal bacterial adaptations to salivary viruses

Pride, D. T., Salzman, J., & Relman, D. A. (2012) · Environmental Microbiology · doi:10.1111/j.1462-2920.2012.02775.x · Cited by 60

Structure and Function of the ABCD1 Variant Database: 20 Years, 940 Pathogenic Variants, and 3400 Cases of Adrenoleukodystrophy

Mallack, E. J., Gao, K., Engelen, M., & Kemp, S. (2022) · Cells · doi:10.3390/cells11020283 · Cited by 60

A Genome Scale Location Analysis of Human Staf/ZNF143-binding Sites Suggests a Widespread Role for Human Staf/ZNF143 in Mammalian Promoters

Myslinski, E., Gérard, M.-A., Krol, A., & Carbon, P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608507200 · Cited by 60

Evolutionary Histories of Type III Polyketide Synthases in Fungi

Navarro-Muñoz, J. C., & Collemare, J. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.03018 · Cited by 59

The FES Gene at the 15q26 Coronary-Artery-Disease Locus Inhibits Atherosclerosis

Karamanavi, E., McVey, D. G., van der Laan, S. W., Stanczyk, P. J., Morris, G. E., Wang, Y., Yang, W., Chan, K., Poston, R. N., Luo, J., et al. (2022) · Circulation Research · doi:10.1161/circresaha.122.321146 · Cited by 54

De novo gene synthesis by an antiviral reverse transcriptase

Tang, S., Conte, V., Zhang, D. J., Žedaveinytė, R., Lampe, G. D., Wiegand, T., Tang, L. C., Wang, M., Walker, M. W. G., George, J. T., et al. (2024) · Science · doi:10.1126/science.adq0876 · Cited by 58

Genome-wide analyses of PAM-relaxed Cas9 genome editors reveal substantial off-target effects by ABE8e in rice

Wu, Y., Ren, Q., Zhong, Z., Liu, G., Han, Y., Bao, Y., Liu, L., Xiang, S., Liu, S., Tang, X., et al. (2022) · Plant Biotechnology Journal · doi:10.1111/pbi.13838 · Cited by 56

Organization of lamprey variable lymphocyte receptor C locus and repertoire development

Das, S., Hirano, M., Aghaallaei, N., Bajoghli, B., Boehm, T., & Cooper, M. D. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1302500110 · Cited by 57

Functional Strain Redundancy and Persistent Phage Infection in Swiss Hard Cheese Starter Cultures

Somerville, V., Berthoud, H., Schmidt, R. S., Bachmann, H.-P., Meng, Y. H., Fuchsmann, P., von Ah, U., & Engel, P. (2022) · The ISME Journal · doi:10.1038/s41396-021-01071-0 · Cited by 55

DNA end sensing and cleavage by the Shedu anti-phage defense system

Loeff, L., Walter, A., Rosalen, G. T., & Jinek, M. (2025) · Cell · doi:10.1016/j.cell.2024.11.030 · Cited by 56

Cryo-EM reveals the architecture of placental malaria VAR2CSA and provides molecular insight into chondroitin sulfate binding

Wang, K., Dagil, R., Lavstsen, T., Misra, S. K., Spliid, C. B., Wang, Y., Gustavsson, T., Sandoval, D. R., Vidal-Calvo, E. E., Choudhary, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23254-1 · Cited by 52

Chemical Proteomics and Structural Biology Define EPHA2 Inhibition by Clinical Kinase Drugs

Heinzlmeir, S., Kudlinzki, D., Sreeramulu, S., Klaeger, S., Gande, S. L., Linhard, V., Wilhelm, M., Qiao, H., Helm, D., Ruprecht, B., et al. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00709 · Cited by 56

Aberrant methylmalonylation underlies methylmalonic acidemia and is attenuated by an engineered sirtuin

Head, P. E., Myung, S., Chen, Y., Schneller, J. L., Wang, C., Duncan, N., Hoffman, P., Chang, D., Gebremariam, A., Gucek, M., et al. (2022) · Science Translational Medicine · doi:10.1126/scitranslmed.abn4772 · Cited by 52

Design of Cyclic Peptides Targeting Protein–Protein Interactions Using AlphaFold

(2023) · doi:10.3390/ijms241713257 · Cited by 51

Genome annotation: from human genetics to biodiversity genomics

Guigó, R. (2023) · Cell Genomics · doi:10.1016/j.xgen.2023.100375 · Cited by 49

Endopeptidase Regulation as a Novel Function of the Zur-Dependent Zinc Starvation Response

Murphy, S. G., Alvarez, L., Adams, M. C., Liu, S., Chappie, J. S., Cava, F., & Dörr, T. (2019) · mBio · doi:10.1128/mbio.02620-18 · Cited by 46

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

Distinct gene clusters drive formation of ferrosome organelles in bacteria

Grant, C. R., Amor, M., Trujillo, H. A., Krishnapura, S., Iavarone, A. T., & Komeili, A. (2022) · Nature · doi:10.1038/s41586-022-04741-x · Cited by 45

Studies on the regulation of the human E1 subunit of the 2-oxoglutarate dehydrogenase complex, including the identification of a novel calcium-binding site

Armstrong, C. T., Anderson, J. L. R., & Denton, R. M. (2014) · Biochemical Journal · doi:10.1042/bj20131664 · Cited by 44

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

Mycobacterium tuberculosis VapC4 toxin engages small ORFs to initiate an integrated oxidative and copper stress response

Barth, V. C., Chauhan, U., Zeng, J., Su, X., Zheng, H., Husson, R. N., & Woychik, N. A. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2022136118 · Cited by 44

Recognition models to predict DNA-binding specificities of homeodomain proteins

Christensen, R. G., Enuameh, M. S., Noyes, M. B., Brodsky, M. H., Wolfe, S. A., & Stormo, G. D. (2012) · Bioinformatics · doi:10.1093/bioinformatics/bts202 · Cited by 42

Protein engineering by highly parallel screening of computationally designed variants

Sun, M. G. F., Seo, M.-H., Nim, S., Corbi-Verge, C., & Kim, P. M. (2016) · Science Advances · doi:10.1126/sciadv.1600692 · Cited by 41

The identification of response regulator‐specific binding sites reveals new roles of two‐component systems in Bacillus cereus and closely related low‐GC Gram‐positives

de Been, M., Bart, M. J., Abee, T., Siezen, R. J., & Francke, C. (2008) · Environmental Microbiology · doi:10.1111/j.1462-2920.2008.01700.x · Cited by 42

Cofactor Specificity of Glucose-6-Phosphate Dehydrogenase Isozymes in Pseudomonas putida Reveals a General Principle Underlying Glycolytic Strategies in Bacteria

Volke, D. C., Olavarría, K., & Nikel, P. I. (2021) · mSystems · doi:10.1128/msystems.00014-21 · Cited by 42

PTMScout, a Web Resource for Analysis of High Throughput Post-translational Proteomics Studies

Naegle, K. M., Gymrek, M., Joughin, B. A., Wagner, J. P., Welsch, R. E., Yaffe, M. B., Lauffenburger, D. A., & White, F. M. (2010) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m110.001206 · Cited by 41

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

Structural Insight into How Bacteria Prevent Interference between Multiple Divergent Type IV Secretion Systems

Gillespie, J. J., Phan, I. Q. H., Scheib, H., Subramanian, S., Edwards, T. E., Lehman, S. S., Piitulainen, H., Sayeedur Rahman, M., Rennoll-Bankert, K. E., Staker, B. L., et al. (2015) · mBio · doi:10.1128/mbio.01867-15 · Cited by 36

Transcriptional, post-transcriptional and chromatin-associated regulation of pri-miRNAs, pre-miRNAs and moRNAs

Nepal, C., Coolen, M., Hadzhiev, Y., Cussigh, D., Mydel, P., Steen, V. M., Carninci, P., Andersen, J. B., Bally-Cuif, L., Müller, F., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1354 · Cited by 35

The minor pilin PilV provides a conserved adhesion site throughout the antigenically variable meningococcal type IV pilus

Barnier, J.-P., Meyer, J., Kolappan, S., Bouzinba-Ségard, H., Gesbert, G., Jamet, A., Frapy, E., Schönherr-Hellec, S., Capel, E., Virion, Z., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2109364118 · Cited by 34

Insights into the CRISPR/Cas system of Gardnerella vaginalis

Pleckaityte, M., Zilnyte, M., & Zvirbliene, A. (2012) · BMC Microbiology · doi:10.1186/1471-2180-12-301 · Cited by 33

The transcriptome of Candida albicans mitochondria and the evolution of organellar transcription units in yeasts

Kolondra, A., Labedzka-Dmoch, K., Wenda, J. M., Drzewicka, K., & Golik, P. (2015) · BMC Genomics · doi:10.1186/s12864-015-2078-z · Cited by 33

Determination of the consensus DNA-binding sequence and a transcriptional activation domain for ESE-2

Choi, Y. S., & Sinha, S. (2006) · Biochemical Journal · doi:10.1042/bj20060375 · Cited by 32

Adhesin Als4112 promotes Candida auris skin colonization through interactions with keratinocytes and extracellular matrix proteins

Zhao, G., Lyu, J., Veniaminova, N. A., Zarnowski, R., Mattos, E., Johnson, C. J., Quintanilla, D., Hautau, H., Hold, L. A., Xu, B., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-60876-1 · Cited by 32

AB-Gen: Antibody Library Design with Generative Pre-Trained Transformer and Deep Reinforcement Learning

Xu, X., Xu, T., Zhou, J., Liao, X., Zhang, R., Wang, Y., Zhang, L., & Gao, X. (2023) · Genomics, Proteomics & Bioinformatics · doi:10.1016/j.gpb.2023.03.004 · Cited by 32

Discovery of cytosine deaminases enables base-resolution methylome mapping using a single enzyme

Vaisvila, R., Johnson, S. R., Yan, B., Dai, N., Bourkia, B. M., Chen, M., Corrêa, I. R., Yigit, E., & Sun, Z. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.01.027 · Cited by 32

Design of diverse, functional mitochondrial targeting sequences across eukaryotic organisms using variational autoencoder

Boob, A. G., Tan, S.-I., Zaidi, A., Singh, N., Xue, X., Zhou, S., Martin, T. A., Chen, L.-Q., & Zhao, H. (2025) · Nature Communications · doi:10.1038/s41467-025-59499-3 · Cited by 31

Large genomic differences between the morphologically indistinguishable diplomonads Spironucleus barkhanus and Spironucleus salmonicida

Roxström-Lindquist, K., Jerlström-Hultqvist, J., Jørgensen, A., Troell, K., Svärd, S. G., & Andersson, J. O. (2010) · BMC Genomics · doi:10.1186/1471-2164-11-258 · Cited by 29

Spi-1/PU.1 activates transcription through clustered DNA occupancy in erythroleukemia

Ridinger-Saison, M., Boeva, V., Rimmelé, P., Kulakovskiy, I., Gallais, I., Levavasseur, B., Paccard, C., Legoix-Né, P., Morlé, F., Nicolas, A., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks659 · Cited by 28

Structural screens identify candidate human homologs of insect chemoreceptors and cryptic Drosophila gustatory receptor-like proteins

(2023) · doi:10.7554/elife.85537 · Cited by 28

The RIX domain defines a class of polymorphic T6SS effectors and secreted adaptors

Kanarek, K., Fridman, C. M., Bosis, E., & Salomon, D. (2023) · Nature Communications · doi:10.1038/s41467-023-40659-2 · Cited by 27

α-Carboxysome Size Is Controlled by the Disordered Scaffold Protein CsoS2

Oltrogge, L. M., Chen, A. W., Chaijarasphong, T., Turnšek, J. B., & Savage, D. F. (2024) · Biochemistry · doi:10.1021/acs.biochem.3c00403 · Cited by 27

Phosphorylation of the retinoic acid receptor alpha induces a mechanical allosteric regulation and changes in internal dynamics

Chebaro, Y., Amal, I., Rochel, N., Rochette-Egly, C., Stote, R. H., & Dejaegere, A. (2013) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1003012 · Cited by 25

Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin

Carver, A., Yu, T.-Y., Yates, L. A., White, T., Wang, R., Lister, K., Jasin, M., & Zhang, X. (2025) · Science · doi:10.1126/science.adr7920 · Cited by 25

Cyanobacterial α-carboxysome carbonic anhydrase is allosterically regulated by the Rubisco substrate RuBP

Pulsford, S. B., Outram, M. A., Förster, B., Rhodes, T., Williams, S. J., Badger, M. R., Price, G. D., Jackson, C. J., & Long, B. M. (2024) · Science Advances · doi:10.1126/sciadv.adk7283 · 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

Structural insights into human TFIIIC promoter recognition

(2023) · doi:10.1126/sciadv.adh2019 · Cited by 23

Diversification of molecular pattern recognition in bacterial NLR-like proteins

(2024) · doi:10.1038/s41467-024-54214-0 · Cited by 23

Structure of the murine lysosomal multienzyme complex core

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