UniProt: the Universal Protein Knowledgebase in 2023

Database resources of the National Center for Biotechnology Information: update

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AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models

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UniProt: the universal protein knowledgebase in 2021

The UniProt Consortium, Bateman, A., Martin, M.-J., Orchard, S., Magrane, M., Agivetova, R., Ahmad, S., Alpi, E., Bowler-Barnett, E. H., Britto, R., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1100 · Cited by 6,372

Database resources of the national center for biotechnology information

Sayers, E. W., Bolton, E. E., Brister, J. R., Canese, K., Chan, J., Comeau, D. C., Connor, R., Funk, K., Kelly, C., Kim, S., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1112 · Cited by 2,812

InterPro in 2022

Paysan‐Lafosse, T., Blum, M., Chuguransky, S., Grego, T., Pinto, B. L., Salazar, G. A., Bileschi, M. L., Bork, P., Bridge, A. J., Colwell, L. J., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac993 · Cited by 2,457

Ensembl 2022

Cunningham, F., Allen, J. E., Allen, J., Alvarez-Jarreta, J., Amode, M. R., Armean, I. M., Austine-Orimoloye, O., Azov, A. G., Barnes, I., Bennett, R., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1049 · Cited by 1,923

RCSB Protein Data Bank: powerful new tools for exploring 3D structures of biological macromolecules for basic and applied research and education in fundamental biology, biomedicine, biotechnology, bioengineering and energy sciences

Burley, S. K., Bhikadiya, C., Bi, C., Bittrich, S., Chen, L., Crichlow, G. V., Christie, C. H., Dalenberg, K., Di Costanzo, L., Duarte, J. M., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkaa1038 · Cited by 1,581

ChEBI in 2016: Improved services and an expanding collection of metabolites

Hastings, J., Owen, G., Dekker, A., Ennis, M., Kale, N., Muthukrishnan, V., Turner, S., Swainston, N., Mendes, P., & Steinbeck, C. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1031 · Cited by 1,083

Metabolomics: A New Tool to Reveal the Nature of Diabetic Kidney Disease

Huang, G., Li, M., Li, Y. J., & Mao, Y. (2022) · Laboratory Medicine · doi:10.1093/labmed/lmac041 · Cited by 933

BioLiP: a semi-manually curated database for biologically relevant ligand–protein interactions

Yang, J., Roy, A., & Zhang, Y. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks966 · Cited by 749

ForceGen: End-to-end de novo protein generation based on nonlinear mechanical unfolding responses using a language diffusion model

Ni, B., Kaplan, D. L., & Buehler, M. J. (2024) · Science Advances · doi:10.1126/sciadv.adl4000 · Cited by 51

GPSFun: geometry-aware protein sequence function predictions with language models

Yuan, Q., Tian, C., Song, Y., Ou, P., Zhu, M., Zhao, H., & Yang, Y. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae381 · Cited by 41

Autotrophic adaptive laboratory evolution of the acetogen Clostridium autoethanogenum delivers the gas-fermenting strain LAbrini with superior growth, products, and robustness

Ingelman, H., Heffernan, J. K., Harris, A., Brown, S. D., Shaikh, K. M., Saqib, A. Y., Pinheiro, M. J., de Lima, L. A., Martinez, K. R., González-García, R. A., et al. (2024) · New Biotechnology · doi:10.1016/j.nbt.2024.06.002 · Cited by 41

Assessing male reproductive toxicity of environmental pollutant di-ethylhexyl phthalate with network toxicology and molecular docking strategy

Hong, Y., Wang, Y., Wang, D., Yuan, Q., Yang, Z., & Deng, C. (2024) · Reproductive Toxicology · doi:10.1016/j.reprotox.2024.108749 · Cited by 41

A compendium of human gene functions derived from evolutionary modelling

Feuermann, M., Mi, H., Gaudet, P., Muruganujan, A., Lewis, S., Ebert, D., Mushayahama, T., Aleksander, S., Balhoff, J. P., Carbon, S., et al. (2025) · Nature · doi:10.1038/s41586-025-08592-0 · Cited by 45

Practical Applications of Language Models in Protein Sorting Prediction: SignalP 6.0, DeepLoc 2.1, and DeepLocPro 1.0

Nielsen, H. (2025) · Methods in molecular biology · doi:10.1007/978-1-0716-4623-6_10 · Cited by 48

AI-driven bioactive peptide discovery of next-generation metabolic biotherapeutics

Hamadou, M., & Mune, M. A. M. (2025) · Applied Food Research · doi:10.1016/j.afres.2025.101291 · Cited by 47

Novel evolved Yarrowia lipolytica strains for enhanced growth and lipid content under high concentrations of crude glycerol

Tsirigka, A., Theodosiou, E., Patsios, S. I., Tsoureki, A., Andreadelli, A., Papa, E., Aggeli, A., Karabelas, A. J., & Makris, A. M. (2023) · Microbial Cell Factories · doi:10.1186/s12934-023-02072-8 · Cited by 40

Analysis of aptamer-target binding and molecular mechanisms by thermofluorimetric analysis and molecular dynamics simulation

Zhang, H., Lv, C., Li, Z., Jiang, S., Cai, D., Liu, S.-S., Wang, T., & Zhang, K.-H. (2023) · Frontiers in Chemistry · doi:10.3389/fchem.2023.1144347 · Cited by 39

Identifying Candidate Gene–Disease Associations via Graph Neural Networks

Cinaglia, P., & Cannataro, M. (2023) · Entropy · doi:10.3390/e25060909 · Cited by 39

A Systematic Compilation of Human SH3 Domains: A Versatile Superfamily in Cellular Signaling

Mehrabipour, M., Jasemi, N. S. K., Dvorský, R., & Ahmadian, M. R. (2023) · Cells · doi:10.3390/cells12162054 · Cited by 40

Subclinical and clinical acute kidney injury share similar urinary peptide signatures and prognosis

Boutin, L., Latosińska, A., Mischak, H., Deniau, B., Asakage, A., Legrand, M. M., Gayat, É., Mebazaa, A., Chadjichristos, C. E., & Dépret, F. (2023) · Intensive Care Medicine · doi:10.1007/s00134-023-07198-2 · Cited by 39

Environmental distribution and genomic characteristics of Solirubrobacter, with proposal of two novel species

Jiang, Z., Mou, T., Sun, Y. Q., Su, J., Yu, L., & Zhang, Y. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1267771 · Cited by 41

Genotype–phenotype associations in 1018 individuals with SCN1A‐related epilepsies

Gallagher, D., Pérez‐Palma, E., Brünger, T., Ghanty, I., Brilstra, E. H., Ceulemans, B., Chémaly, N., Lange, I., Depienne, C., Guerrini, R., et al. (2024) · Epilepsia · doi:10.1111/epi.17882 · Cited by 43

Annelid adult cell type diversity and their pluripotent cellular origins

Álvarez‐Campos, P., García-Castro, H., Emili, E., Pérez-Posada, A., del Olmo, I., Péron, S., Salamanca-Díaz, D. A., Mason, V., Metzger, B. M., Bely, A. E., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-47401-6 · Cited by 42

Directed evolution of LaccID for cell surface proximity labeling and electron microscopy

Lee, S.-Y., Roh, H., González-Pérez, D., Mackey, M. R., Hoces, D., McLaughlin, C. N., Lin, C., Adams, S., Nguyen, K. H., Keun-young Kim, A., et al. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-01973-6 · Cited by 46

RCSB Protein Data Bank: Delivering integrative structures alongside experimental structures and computed structure models

Vallat, B. K., Rose, Y., Piehl, D. W., Duarte, J. M., Bittrich, S., Bi, C., Segura, J., Zalevsky, A. O., Sekharan, M. R., Webb, B., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1187 · Cited by 39

MBROLE3: improved functional enrichment of chemical compounds for metabolomics data analysis

López-Ibáñez, J., Pazos, F., & Chagoyen, M. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad405 · Cited by 38

Proximity-labeling chemoproteomics defines the subcellular cysteinome and inflammation-responsive mitochondrial redoxome

Yan, T., Julio, A. R., Villanueva, M., Jones, A. E., Ball, A. B., Boatner, L. M., Turmon, A. C., Nguyễn, K. B., Yen, S. L., Desai, H. S., et al. (2023) · Cell chemical biology · doi:10.1016/j.chembiol.2023.06.008 · Cited by 37

CSF1R-related disorder: State of the art, challenges, and proposition of a new terminology

Dulski, J., Muthusamy, K., Lund, T. C., & Wszołek, Z. K. (2023) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2023.105894 · Cited by 39

Structural basis for the ligand recognition and signaling of free fatty acid receptors

Zhang, X., Guseinov, A.-A., Jenkins, L., Li, K., Tikhonova, I. G., Milligan, G., & Zhang, C. (2024) · Science Advances · doi:10.1126/sciadv.adj2384 · Cited by 40

Variety in the USP deubiquitinase catalytic mechanism

Keijzer, N., Priyanka, A., Bultsma, Y., Fish, A., Gersch, M., & Sixma, T. K. (2024) · Life Science Alliance · doi:10.26508/lsa.202302533 · Cited by 38

An immunogenetic basis for lung cancer risk

Krishna, C., Tervi, A. M., Saffern, M., Wilson, E. A., Yoo, S., Mars, N., Roudko, V., Cho, B. A., Jones, S. E., Vaninov, N., et al. (2024) · Science · doi:10.1126/science.adi3808 · Cited by 42

The antitumor effects of herbal medicine Triphala on oral cancer by inactivating PI3K/Akt signaling pathway: based on the network pharmacology, molecular docking, in vitro and in vivo experimental validation

Hu, S., Li, S., Xu, Y., Huang, X., Mai, Z., Chen, Y., Xiao, H., Ning, W., Gaus, S., Savković, V., et al. (2024) · Phytomedicine · doi:10.1016/j.phymed.2024.155488 · Cited by 38

Maternal gestational diabetes mellitus associates with altered gut microbiome composition and head circumference abnormalities in male offspring

Wang, S., Liu, Y., Tam, W. H., Ching, J. Y. L., Xu, W., Yan, S., Qin, B., Lin, L., Peng, Y., Zhu, J., et al. (2024) · Cell Host & Microbe · doi:10.1016/j.chom.2024.06.005 · Cited by 43

Andrographolide ameliorates sepsis-induced acute lung injury by promoting autophagy in alveolar macrophages via the RAGE/PI3K/AKT/mTOR pathway

Qin, Y., Li, W., Liu, J., Wang, F., Zhou, W., Xiao, L., Zhou, P., Wu, F., Chen, X., Xu, S., et al. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.112719 · Cited by 38

Role of protein kinase PLK1 in the epigenetic maintenance of centromeres

Conti, D., Esposito-Verza, A., Pesenti, M. E., Cmentowski, V., Vetter, I. R., Pan, D., & Musacchio, A. (2024) · Science · doi:10.1126/science.ado5178 · Cited by 42

CATH v4.4: major expansion of CATH by experimental and predicted structural data

Waman, V. P., Bordin, N., Lau, A. M., Kandathil, S., Wells, J., Miller, D., Velankar, S., Jones, D. T., Sillitoe, I., & Orengo, C. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae1087 · Cited by 48

Degradation of circular RNA by the ribonuclease DIS3

Tao, X., Zhai, S.-N., Liu, C., Huang, Y., Wei, J., Guo, Y., Liu, X.-Q., Li, X., Yang, L. C., & Chen, L.-L. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.01.012 · Cited by 40

Sperm sequencing reveals extensive positive selection in the male germline

Neville, M. D. C., Lawson, A. R. J., Sanghvi, R., Abascal, F., Pham, M. H., Cagan, A., Nicola, P. A., Bayzetinova, T., Baez‐Ortega, A., Roberts, K., et al. (2025) · Nature · doi:10.1038/s41586-025-09448-3 · Cited by 46

Immune regulation of poly unsaturated fatty acids and free fatty acid receptor 4

Duah, M., Zhang, K., Liang, Y., Ayarick, V. A., Xu, K., & Pan, B. (2022) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2022.109222 · Cited by 40

Creating new-to-nature carbon fixation: A guide

Schulz-Mirbach, H., Dronsella, B., He, H., & Erb, T. J. (2023) · Metabolic Engineering · doi:10.1016/j.ymben.2023.12.012 · Cited by 35

Repeated co-option of HMG-box genes for sex determination in brown algae and animals

Luthringer, R., Raphalen, M., Guerra, C., Colin, S., Martinho, C., Zheng, M., Hoshino, M., Badis, Y., Lipinska, A. P., Haas, F. B., et al. (2024) · Science · doi:10.1126/science.adk5466 · Cited by 35

Metaproteomic portrait of the healthy human gut microbiota

Tanca, A., Palomba, A., Fiorito, G., Abbondio, M., Pagnozzi, D., & Uzzau, S. (2024) · npj Biofilms and Microbiomes · doi:10.1038/s41522-024-00526-4 · Cited by 38

CaMKK2: bridging the gap between Ca2+ signaling and energy-sensing

McAloon, L. M., Muller, A. G., Nay, K., Lu, E. L., Smeuninx, B., Means, A. R., Febbraio, M. A., & Scott, J. W. (2024) · Essays in Biochemistry · doi:10.1042/ebc20240011 · Cited by 36

ESM-Ezy: a deep learning strategy for the mining of novel multicopper oxidases with superior properties

Qian, H., Wang, Y., Zhou, X.-B., Gu, T., Wang, H., Lyu, H., Li, Z., Li, X., Zhou, H., Guo, C.-C., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-58521-y · Cited by 35

AlphaFold2 enables accurate deorphanization of ligands to single-pass receptors

Banhos Danneskiold-Samsøe, N., Kavi, D., Jude, K. M., Nissen, S. B., Wat, L. W., Coassolo, L., Zhao, M., Santana-Oikawa, G. A., Broido, B. B., Garcia, K. C., et al. (2024) · Cell Systems · doi:10.1016/j.cels.2024.10.004 · Cited by 35

The ultra-high affinity transport proteins of ubiquitous marine bacteria

Clifton, B. E., Alcolombri, U., Uechi, G.-I., Jackson, C. J., & Laurino, P. (2024) · Nature · doi:10.1038/s41586-024-07924-w · Cited by 37

Improved structure-related prediction for insufficient homologous proteins using MSA enhancement and pre-trained language model

Meng, Q., Guo, F., & Tang, J. (2023) · Briefings in Bioinformatics · doi:10.1093/bib/bbad217 · Cited by 37

Outdoor airborne allergens: Characterization, behavior and monitoring in Europe

Grewling, Ł., Ribeiro, H., Antunes, C. M., Apangu, G., Çelenk, S., Costa, A., Eguíluz‐Gracia, I., Galveias, A., Roldán, N. G., Lika, M., et al. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.167042 · Cited by 38

How Ligands Interact with the Kinase Hinge

Zhao, Z., & Bourne, P. E. (2023) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.3c00212 · Cited by 39

iSanXoT: A standalone application for the integrative analysis of mass spectrometry-based quantitative proteomics data

Rodríguez, J. M., Jorge, I., Martínez‐Val, A., Barrero-Rodríguez, R., Magni, R., Núñez, E., Laguillo-Gómez, A., Devesa, C. A., López, J. A., Camafeita, E., et al. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.12.034 · Cited by 36

MetaCerberus: distributed highly parallelized HMM-based processing for robust functional annotation across the tree of life

Figueroa, J. L., Dhungel, E., Bellanger, M., Brouwer, C., & White, R. A., III (2024) · Bioinformatics · doi:10.1093/bioinformatics/btae119 · Cited by 36

An Active Site Tyr Residue Guides the Regioselectivity of Lysine Hydroxylation by Nonheme Iron Lysine-4-hydroxylase Enzymes through Proton-Coupled Electron Transfer

Cao, Y., Hay, S., & de Visser, S. P. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c14574 · Cited by 36

CXCL3: A key player in tumor microenvironment and inflammatory diseases

Bao, Y., Tong, C., & Xiong, X. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.122691 · Cited by 39

Structure‐aware deep learning model for peptide toxicity prediction

Ebrahimikondori, H., Sutherland, D., Yanai, A., Richter, A., Salehi, A., Li, C., Coombe, L., Kotkoff, M., Warren, R. L., & Birol, İ. (2024) · Protein Science · doi:10.1002/pro.5076 · Cited by 43

Ligand-induced conformational changes in the β1-adrenergic receptor revealed by hydrogen-deuterium exchange mass spectrometry

Toporowska, J., Kapoor, P., Musgaard, M., Gherbi, K., Sengmany, K., Qu, F., Soave, M., Yen, H., Hansen, K., Jazayeri, A., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-53161-0 · Cited by 36

35 Years of TFAM Research: Old Protein, New Puzzles

Kozhukhar, N., & ALEXEYEV, M. F. (2023) · Biology · doi:10.3390/biology12060823 · Cited by 41

The ESTHER database on alpha/beta hydrolase fold proteins - An overview of recent developments

Chatonnet, A., Perochon, M., Velluet, E., & Marchot, P. (2023) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2023.110671 · Cited by 37

Enhanced Bacterium–Phage Symbiosis in Attached Microbial Aggregates on a Membrane Surface Facing Elevated Hydraulic Stress

Tan, Y., Yu, P., Huang, D., Yuan, M., Yu, Z., Lü, H., Alvarez, P. J. J., & Zhu, L. (2023) · Environmental Science & Technology · doi:10.1021/acs.est.3c05452 · Cited by 35

Engineering the synthetic β-alanine pathway in Komagataella phaffii for conversion of methanol into 3-hydroxypropionic acid

Àvila-Cabré, S., Pérez‐Trujillo, M., Albiol, J., & Ferrer, P. (2023) · Microbial Cell Factories · doi:10.1186/s12934-023-02241-9 · Cited by 34

Twin defect-rich Pt ultrathin nanowire nanozymes alleviate inflammatory skin diseases by scavenging reactive oxygen species

Zhao, H., Zhao, H., Li, M., Tang, Y., Xiao, X., Cai, Y., He, F., Huang, H., Zhang, Y., & Li, J. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103055 · Cited by 35

DEGRONOPEDIA: a web server for proteome-wide inspection of degrons

Szulc, N. A., Stefaniak, F., Piechota, M., Soszyńska, A., Piórkowska, G., Cappannini, A., Bujnicki, J. M., Maniaci, C., & Pokrzywa, W. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae238 · Cited by 35

CyclicPepedia: a knowledge base of natural and synthetic cyclic peptides

Liu, L., Yang, L., Cao, S., Gao, Z., Yang, B., Zhang, G., Zhu, R., & Wu, D. (2024) · Briefings in Bioinformatics · doi:10.1093/bib/bbae190 · Cited by 35

Predicting intercellular communication based on metabolite-related ligand-receptor interactions with MRCLinkdb

Zhang, Y., Yang, Y., Ren, L., Zhan, M., Sun, T., Zou, Q., & Zhang, Y. (2024) · BMC Biology · doi:10.1186/s12915-024-01950-w · Cited by 36

PLM_Sol: predicting protein solubility by benchmarking multiple protein language models with the updated Escherichia coli protein solubility dataset

Zhang, X. J., Hu, X., Zhang, T., Yang, L., Liu, C., Xu, N., Wang, H., & Sun, W. (2024) · Briefings in Bioinformatics · doi:10.1093/bib/bbae404 · Cited by 38

RBPWorld for exploring functions and disease associations of RNA-binding proteins across species

Liao, J., Yang, B., Shi, C.-P., Deng, W.-X., Deng, J.-S., Cen, M., Zheng, B.-Q., Zhan, Z.-L., Liang, Q., Wang, J.-E., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae1028 · Cited by 36

Computer-aided drug discovery: From traditional simulation methods to language models and quantum computing

Pei, Z. (2024) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2024.102334 · Cited by 37

The IUPHAR/BPS Guide to PHARMACOLOGY in 2026

Harding, S. D., Armstrong, J. F., Faccenda, E., Southan, C., Alexander, S. P. H., Davenport, A. P., Spedding, M., & Davies, J. A. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1067 · Cited by 35

Epigenetics and Plant Hormone Dynamics: A Functional and Methodological Perspective

Rudolf, J., Tomovicova, L., Panzarova, K., Fajkus, J., Hejatko, J., & Skalak, J. (2024) · Journal of Experimental Botany · doi:10.1093/jxb/erae054 · Cited by 35

Multi-level advances in databases related to systems pharmacology in traditional Chinese medicine: a 60-year review

Fan, M., Jin, C., Li, D., Deng, Y., Lin, Y., Chen, Y., Ma, Y., & Wang, T. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1289901 · Cited by 33

PathDIP 5: improving coverage and making enrichment analysis more biologically meaningful

Pastrello, C., Kotlyar, M., Abovsky, M., Lu, R., & Jurišica, I. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad1027 · Cited by 34

The promises of large language models for protein design and modeling

Valentini, G., Malchiodi, D., Gliozzo, J., Mesiti, M., Soto-Gomez, M., Cabri, A., Reese, J., Casiraghi, E., & Robinson, P. N. (2023) · Frontiers in Bioinformatics · doi:10.3389/fbinf.2023.1304099 · Cited by 40

Evaluating the Effect of Gestational Exposure to Perfluorohexane Sulfonate on Placental Development in Mice Combining Alternative Splicing and Gene Expression Analyses

Zhang, Y., Lv, J., Fan, Y., Tao, L., Xu, J., Tang, W., Sun, N., Zhao, L., Xu, D., & Huang, Y. (2023) · Environmental Health Perspectives · doi:10.1289/ehp13217 · Cited by 34

Neuronal-specific TNFAIP1 ablation attenuates postoperative cognitive dysfunction via targeting SNAP25 for K48-linked ubiquitination

Wang, W., Gao, W., Gong, P., Song, W., Bu, X., Hou, J., Zhang, L., & Zhao, B. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01390-z · Cited by 34

AI approaches for the discovery and validation of drug targets

Wenteler, A., Cabrera, C., Wei, W., Neduva, V., & Barnes, M. R. (2024) · Cambridge Prisms Precision Medicine · doi:10.1017/pcm.2024.4 · Cited by 38

FTO in health and disease

Benák, D., Sevcikova, A., Holzerová, K., & Hlaváčková, M. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1500394 · Cited by 40

Cryo-electron tomography pipeline for plasma membranes

Sun, W. W., Michalak, D. J., Sochacki, K. A., Kunamaneni, P., Alfonzo-Méndez, M. A., Arnold, A. M., Strub, M.-P., Hinshaw, J. E., & Taraska, J. W. (2025) · Nature Communications · doi:10.1038/s41467-025-56045-z · Cited by 35

Analysis of Zika virus capsid-Aedes aegypti mosquito interactome reveals pro-viral host factors critical for establishing infection

Gestuveo, R. J., Royle, J., Donald, C. L., Lamont, D. J., Hutchinson, E. C., Merits, A., Kohl, A., & Varjak, M. (2021) · Nature Communications · doi:10.1038/s41467-021-22966-8 · Cited by 35

The 2023 Nucleic Acids Research Database Issue and the online molecular biology database collection

Rigden, D., & Fernández, X. M. (2023) · Nucleic Acids Res. · doi:10.1093/nar/gkac1186 · Cited by 27

Heat stress at the bicellular stage inhibits sperm cell development and transport into pollen tubes

Li, X., Bruckmann, A., Dresselhaus, T., & Begcy, K. (2024) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiae087 · Cited by 34

Mapping of multiple neurotransmitter receptor subtypes and distinct protein complexes to the connectome

Sanfilippo, P., Kim, A. J., Bhukel, A., Yoo, J., Mirshahidi, P. S., Pandey, V., Bevir, H., Yuen, A., Mirshahidi, P. S., Guo, P., et al. (2024) · Neuron · doi:10.1016/j.neuron.2023.12.014 · Cited by 36

Comparative evaluation of AlphaFold2 and disorder predictors for prediction of intrinsic disorder, disorder content and fully disordered proteins

Zhao, B., Ghadermarzi, S., & Kurgan, L. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.06.001 · Cited by 33

Alkaliphilic/Alkali-Tolerant Fungi: Molecular, Biochemical, and Biotechnological Aspects

Fernández‐López, M. G., Batista‐García, R. A., & Aréchiga‐Carvajal, E. T. (2023) · Journal of Fungi · doi:10.3390/jof9060652 · Cited by 33

Genotype and clinical characteristics of patients with Wolfram syndrome and WFS1-related disorders

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