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The carbohydrate-active enzymes database (CAZy) in 2013
Open accessAbstract
The Carbohydrate-Active Enzymes database (CAZy; http://www.cazy.org) provides online and continuously updated access to a sequence-based family classification linking the sequence to the specificity and 3D structure of the enzymes that assemble, modify and breakdown oligo- and polysaccharides. Functional and 3D structural information is added and curated on a regular basis based on the available literature. In addition to the use of the database by enzymologists seeking curated information on CAZymes, the dissemination of a stable nomenclature for these enzymes is probably a major contribution of CAZy. The past few years have seen the expansion of the CAZy classification scheme to new families, the development of subfamilies in several families and the power of CAZy for the analysis of genomes and metagenomes. This article outlines the changes that have occurred in CAZy during the past 5 years and presents our novel effort to display the resolution and the carbohydrate ligands in crystallographic complexes of CAZymes.
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Citations
Cites
New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
Henrissat, B., & Bairoch, A. (1993) · Biochemical Journal · doi:10.1042/bj2930781 · Cited by 1,974
Self-citationComplex Carbohydrate Utilization by the Healthy Human Microbiome
Cantarel, B. L., Lombard, V., & Henrissat, B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0028742 · Cited by 378
Self-citationThe convergence of carbohydrate active gene repertoires in human gut microbes
Lozupone, C. A., Hamady, M., Cantarel, B. L., Coutinho, P. M., Henrissat, B., Gordon, J. I., & Knight, R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807339105 · Cited by 139
Self-citation
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Dynamics and Stabilization of the Human Gut Microbiome during the First Year of Life
Bäckhed, F., Roswall, J., Peng, Y., Feng, Q., Jia, H., Kovatcheva-Datchary, P., Li, Y., Xia, Y., Xie, H., Zhong, H., et al. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.04.004 · Cited by 3,315
Varki, A. (2017) · Glycobiology · doi:10.1093/glycob/cww086 · Cited by 2,635
The carbohydrate-active enzyme database: functions and literature
Drula, E., Garron, M.-L., Dogan, S., Lombard, V., Henrissat, B., & Terrapon, N. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkab1045 · Cited by 2,439
Self-citationGut bacteria selectively promoted by dietary fibers alleviate type 2 diabetes
Zhao, L., Zhang, F., Ding, X., Wu, G., Lam, Y. Y., Wang, X., Fu, H., Xue, X., Lu, C., Ma, J., et al. (2018) · Science · doi:10.1126/science.aao5774 · Cited by 2,304
Dietary fiber and prebiotics and the gastrointestinal microbiota
Holscher, H. D. (2017) · Gut Microbes · doi:10.1080/19490976.2017.1290756 · Cited by 1,808
Diet-induced extinctions in the gut microbiota compound over generations
Sonnenburg, E. D., Smits, S. A., Tikhonov, M., Higginbottom, S. K., Wingreen, N. S., & Sonnenburg, J. L. (2016) · Nature · doi:10.1038/nature16504 · Cited by 1,730
An insight into gut microbiota and its functionalities
Adak, A., & Khan, M. R. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2943-4 · Cited by 1,485
The Fungal Cell Wall: Structure, Biosynthesis, and Function
Gow, N. A. R., Latge, J.-P., & Munro, C. A. (2017) · Microbiology Spectrum · doi:10.1128/microbiolspec.funk-0035-2016 · Cited by 1,423
A unified catalog of 204,938 reference genomes from the human gut microbiome
Almeida, A., Nayfach, S., Boland, M., Strozzi, F., Beracochea, M., Shi, Z. J., Pollard, K. S., Sakharova, E., Parks, D. H., Hugenholtz, P., et al. (2021) · Nature Biotechnology · doi:10.1038/s41587-020-0603-3 · Cited by 1,367
Lignin degradation: microorganisms, enzymes involved, genomes analysis and evolution
Janusz, G., Pawlik, A., Sulej, J., Świderska-Burek, U., Jarosz-Wilkołazka, A., & Paszczyński, A. (2017) · FEMS Microbiology Reviews · doi:10.1093/femsre/fux049 · Cited by 984
American Gut: an Open Platform for Citizen-Science Microbiome Research
McDonalda, D., Hyde, E., Debelius, J. W., Morton, J. T., Gonzalez, A., Ackermann, G., Aksenov, A. A., Behsaz, B., Brennan, C., Chen, Y., et al. (2018) · doi:10.1101/277970 · Cited by 878
US immigration westernizes the human gut microbiome
Vangay, P., Johnson, A. J., Ward, T. L., Al-Ghalith, G. A., Shields-Cutler, R. R., Hillmann, B. M., Lucas, S. K., Beura, L. K., Thompson, E. A., Till, L. M., et al. (2018) · Cell · doi:10.1016/j.cell.2018.10.029 · Cited by 794
Dietary fibre modulates the gut microbiota
Cronin, P., Joyce, S. A., O’Toole, P. W., & O’Connor, E. M. (2021) · Nutrients · doi:10.3390/nu13051655 · Cited by 658
Carbohydrate-active enzymes (CAZymes) in the gut microbiome
Wardman, J. F., Bains, R. K., Rahfeld, P., & Withers, S. G. (2022) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00712-1 · Cited by 597
Cultivation and sequencing of rumen microbiome members from the Hungate1000 Collection
Hungate1000 project collaborators, Seshadri, R., Leahy, S. C., Attwood, G. T., Teh, K. H., Lambie, S. C., Cookson, A. L., Eloe-Fadrosh, E. A., Pavlopoulos, G. A., Hadjithomas, M., et al. (2018) · Nature Biotechnology · doi:10.1038/nbt.4110 · Cited by 624
Self-citationCurrent challenges and best-practice protocols for microbiome analysis
Bharti, R., & Grimm, D. G. (2021) · Briefings in Bioinformatics · doi:10.1093/bib/bbz155 · Cited by 592
Polysaccharide Utilization Loci: Fueling Microbial Communities
Grondin, J. M., Tamura, K., Déjean, G., Abbott, D. W., & Brumer, H. (2017) · Journal of Bacteriology · doi:10.1128/jb.00860-16 · Cited by 554
Assembly of 913 microbial genomes from metagenomic sequencing of the cow rumen
Stewart, R. D., Auffret, M. D., Warr, A., Wiser, A. H., Press, M. O., Langford, K. W., Liachko, I., Snelling, T. J., Dewhurst, R. J., Walker, A. W., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03317-6 · Cited by 559
Tett, A., Huang, K. D., Asnicar, F., Fehlner-Peach, H., Pasolli, E., Karcher, N., Armanini, F., Manghi, P., Bonham, K., Zolfo, M., et al. (2019) · Cell Host & Microbe · doi:10.1016/j.chom.2019.08.018 · Cited by 476
Nondigestible carbohydrates, butyrate, and butyrate-producing bacteria
Fu, X., Liu, Z., Zhu, C., Mou, H., & Kong, Q. (2019) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2018.1542587 · Cited by 497
Fight them or feed them: How the intestinal mucus layer manages the gut microbiota
Schroeder, B. O. (2019) · Gastroenterology report · doi:10.1093/gastro/goy052 · Cited by 464
Strain-Level Analysis of Mother-to-Child Bacterial Transmission during the First Few Months of Life
Yassour, M., Jason, E., Hogstrom, L. J., Arthur, T. D., Tripathi, S., Siljander, H., Selvenius, J., Oikarinen, S., Hyöty, H., Virtanen, S. M., et al. (2018) · Cell Host & Microbe · doi:10.1016/j.chom.2018.06.007 · Cited by 455
Modulation of the human gut microbiota by dietary fibres occurs at the species level
Chung, W. S. F., Walker, A. W., Louis, P., Parkhill, J., Vermeiren, J., Bosscher, D., Duncan, S. H., & Flint, H. J. (2016) · BMC Biology · doi:10.1186/s12915-015-0224-3 · Cited by 409
Polysaccharide Production by Lactic Acid Bacteria: From Genes to Industrial Applications
Zeidan, A. A., Poulsen, V. K., Janzen, T., Buldo, P., Derkx, P. M. F., Øregaard, G., & Neves, A. R. (2017) · FEMS Microbiology Reviews · doi:10.1093/femsre/fux017 · Cited by 326
Characterizing the mucin-degrading capacity of the human gut microbiota
Glover, J. S., Ticer, T. D., & Engevik, M. A. (2022) · Scientific Reports · doi:10.1038/s41598-022-11819-z · Cited by 307
The reductive glycine pathway allows autotrophic growth of Desulfovibrio desulfuricans
Sánchez-Andrea, I., Guedes, I. A., Hornung, B., Boeren, S., Lawson, C. E., Sousa, D. Z., Bar-Even, A., Claassens, N. J., & Stams, A. J. M. (2020) · Nature Communications · doi:10.1038/s41467-020-18906-7 · Cited by 306
Early-branching gut fungi possess a large, comprehensive array of biomass-degrading enzymes
Solomon, K. V., Haitjema, C. H., Henske, J. K., Gilmore, S. P., Borges-Rivera, D., Lipzen, A., Brewer, H. M., Purvine, S. O., Wright, A. T., Theodorou, M. K., et al. (2016) · Science · doi:10.1126/science.aad1431 · Cited by 302
An atlas of β-glucuronidases in the human intestinal microbiome
Pollet, R. M., D'Agostino, E. H., Walton, W. G., Xu, Y., Little, M. S., Biernat, K. A., Pellock, S. J., Patterson, L. M., Creekmore, B. C., Isenberg, H. N., et al. (2017) · Structure · doi:10.1016/j.str.2017.05.003 · Cited by 289
Bifidobacteria exhibit social behavior through carbohydrate resource sharing in the gut
Milani, C., Lugli, G. A., Duranti, S., Turroni, F., Mancabelli, L., Ferrario, C., Mangifesta, M., Hevia, A., Viappiani, A., Scholz, M., et al. (2015) · Scientific Reports · doi:10.1038/srep15782 · Cited by 284
Hacquard, S., Kracher, B., Hiruma, K., Münch, P. C., Garrido-Oter, R., Thon, M. R., Weimann, A., Damm, U., Dallery, J.-F., Hainaut, M., et al. (2016) · Nature Communications · doi:10.1038/ncomms11362 · Cited by 278
Self-citationGlycan Utilization and Cross-Feeding Activities by Bifidobacteria
Turroni, F., Milani, C., Duranti, S., Mahony, J., van Sinderen, D., & Ventura, M. (2018) · Trends in Microbiology · doi:10.1016/j.tim.2017.10.001 · Cited by 263
Martens, E. C., Kelly, A. G., Tauzin, A. S., & Brumer, H. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.06.022 · Cited by 235
Fungal chitinases: function, regulation, and potential roles in plant/pathogen interactions
Langner, T., & Göhre, V. (2016) · Current Genetics · doi:10.1007/s00294-015-0530-x · Cited by 225
Leveraging diet to engineer the gut microbiome
Wolter, M., Grant, E. T., Boudaud, M., Steimle, A., Pereira, G. V., Martens, E. C., & Desai, M. S. (2021) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-021-00512-7 · Cited by 211
The BRENDA enzyme information system–From a database to an expert system
Schomburg, I., Jeske, L., Ulbrich, M., Placzek, S., Chang, A., & Schomburg, D. (2017) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2017.04.020 · Cited by 222
Beresford-Jones, B. S., Forster, S. C., Stares, M. D., Notley, G., Viciani, E., Browne, H. P., Boehmler, D. J., Soderholm, A. T., Kumar, N., Vervier, K., et al. (2022) · Cell Host & Microbe · doi:10.1016/j.chom.2021.12.003 · Cited by 194
Oliver, A., Chase, A. B., Weihe, C., Orchanian, S. B., Riedel, S. F., Hendrickson, C. L., Lay, M., Sewall, J. M., Martiny, J. B. H., & Whiteson, K. (2021) · mSystems · doi:10.1128/msystems.00115-21 · Cited by 171
Emerging Roles of β-Glucanases in Plant Development and Adaptative Responses
Perrot, T., Pauly, M., & Ramírez, V. (2022) · Plants · doi:10.3390/plants11091119 · Cited by 172
Leth, M. L., Ejby, M., Workman, C., Ewald, D. A., Pedersen, S. S., Sternberg, C., Bahl, M. I., Licht, T. R., Aachmann, F. L., Westereng, B., et al. (2018) · Nature Microbiology · doi:10.1038/s41564-018-0132-8 · Cited by 167
Svartström, O., Alneberg, J., Terrapon, N., Lombard, V., de Bruijn, I., Malmsten, J., Dalin, A.-M., EL Muller, E., Shah, P., Wilmes, P., et al. (2017) · The ISME Journal · doi:10.1038/ismej.2017.108 · Cited by 161
Self-citationTools of the crook-infection strategies of fungal plant pathogens
Rodriguez‐Moreno, L., Ebert, M. K., Bolton, M. D., & Thomma, B. P. H. J. (2018) · The Plant Journal · doi:10.1111/tpj.13810 · Cited by 130
Danne, C., Ryzhakov, G., Martínez-López, M., Ilott, N. E., Franchini, F., Cuskin, F., Lowe, E. C., Bullers, S. J., Arthur, J. S. C., & Powrie, F. (2017) · Cell Host & Microbe · doi:10.1016/j.chom.2017.11.002 · Cited by 120
Shotgun Metagenomics of a Water Kefir Fermentation Ecosystem Reveals a Novel Oenococcus Species
Verce, M., De Vuyst, L., & Weckx, S. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.00479 · Cited by 121
Karcher, N., Pasolli, E., Asnicar, F., Huang, K. D., Tett, A., Manara, S., Armanini, F., Bain, D., Duncan, S. H., Louis, P., et al. (2020) · Genome Biology · doi:10.1186/s13059-020-02042-y · Cited by 116
Bouchon, D., Zimmer, M., & Dittmer, J. (2016) · Frontiers in Microbiology · doi:10.3389/fmicb.2016.01472 · Cited by 110
Lenardon, M. D., Sood, P., Dorfmueller, H. C., Brown, A. J. P., & Gow, N. A. R. (2020) · The Cell Surface · doi:10.1016/j.tcsw.2020.100047 · Cited by 110
Mango anthracnose disease: the current situation and direction for future research
Dofuor, A. K., Quartey, N. K.-A., Osabutey, A. F., Antwi-Agyakwa, A. K., Asante, K., Boateng, B. O., Ablormeti, F. K., Lutuf, H., Osei-Owusu, J., Osei, J. H. N., et al. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1168203 · Cited by 103
“Specifically, to penetrate the plant host, pathogenic fungi may secrete cell wall-degrading carbohydrate-active enzymes such as glycoside hydrolases, glycosyltransferases, polysaccharide lyases, carbohydrate esterases, and redox enzymes (Lombard et al., 2014).”
BackgroundSubstrate dependent in vitro antifungal activity of Bacillus sp strain AR2
Singh, A. K., Rautela, R., & Cameotra, S. S. (2014) · Microbial Cell Factories · doi:10.1186/1475-2859-13-67 · Cited by 97
Deo, D., Davray, D., & Kulkarni, R. (2019) · Microorganisms · doi:10.3390/microorganisms7100444 · Cited by 90
Jia, F.-F., Zhang, L.-J., Pang, X.-H., Gu, X.-X., Abdelazez, A., Liang, Y., Sun, S.-R., & Meng, X.-C. (2017) · Genomics · doi:10.1016/j.ygeno.2017.06.008 · Cited by 82
Katoh, T., Ojima, M. N., Sakanaka, M., Ashida, H., Gotoh, A., & Katayama, T. (2020) · Microorganisms · doi:10.3390/microorganisms8040481 · Cited by 80
Surve, S., Shinde, D. B., & Kulkarni, R. (2022) · Scientific Reports · doi:10.1038/s41598-022-05850-3 · Cited by 74
Stokke, R., Dahle, H., Roalkvam, I., Wissuwa, J., Daae, F. L., Tooming‐Klunderud, A., Thorseth, I. H., Pedersen, R. B., & Steen, I. H. (2015) · Environmental Microbiology · doi:10.1111/1462-2920.12970 · Cited by 63
3D Structural Insights into β-Glucans and Their Binding Proteins
Manabe, N., & Yamaguchi, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22041578 · Cited by 57
Polymerization of the backbone of the pectic polysaccharide rhamnogalacturonan I
Amos, R. A., Atmodjo, M. A., Huang, C., Gao, Z., Venkat, A., Taujale, R., Kannan, N., Moremen, K. W., & Mohnen, D. (2022) · Nature Plants · doi:10.1038/s41477-022-01270-3 · Cited by 55
Cenci, U., Sibbald, S. J., Curtis, B. A., Kamikawa, R., Eme, L., Moog, D., Henrissat, B., Maréchal, E., Chabi, M., Djemiel, C., et al. (2018) · BMC Biology · doi:10.1186/s12915-018-0593-5 · Cited by 53
Self-citationKandasamy, S., Yoo, J., Yun, J., Lee, K.-H., Kang, H.-B., Kim, J.-E., Oh, M.-H., & Ham, J.-S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214494 · Cited by 51
Peng, S., Zheng, H., Herrero-Fresno, A., Olsen, J. E., Dalsgaard, A., & Ding, Z. (2021) · Science of The Total Environment · doi:10.1016/j.scitotenv.2021.148259 · Cited by 51
Al-Masaudi, S., El Kaoutari, A., Drula, E., Al-Mehdar, H., Redwan, E. M., Lombard, V., & Henrissat, B. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.00666 · Cited by 48
Self-citationComputational models in the service of X‐ray and cryo‐ electron microscopy structure determination
Kryshtafovych, A., Moult, J., Albrecht, R., Chang, G. A., Chao, K., Fraser, A., Greenfield, J., Hartmann, M. D., Herzberg, O., Josts, I., et al. (2021) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26223 · Cited by 45
Ioannou, A., Knol, J., & Belzer, C. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.631282 · Cited by 44
Ostrem Loss, E., Thompson, J., Cheung, P. L. K., Qian, Y., & Venturelli, O. S. (2023) · Nature Ecology & Evolution · doi:10.1038/s41559-022-01930-9 · Cited by 38
Lignocellulose degradation in isopods: new insights into the adaptation to terrestrial life
Bredon, M., Herran, B., Lheraud, B., Bertaux, J., Grève, P., Moumen, B., & Bouchon, D. (2019) · BMC Genomics · doi:10.1186/s12864-019-5825-8 · Cited by 36
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
Complete genome analysis of Bacillus velezensis TS5 and its potential as a probiotic strain in mice
Chen, B., Zhou, Y., Duan, L., Gong, X., Liu, X., Pan, K., Zeng, D., Ni, X., & Zeng, Y. (2023) · Frontiers in Microbiology · doi:10.3389/fmicb.2023.1322910 · Cited by 32
Bai, Z., Zhang, N., Jin, Y., Chen, L., Mao, Y., Sun, L., Fang, F., Liu, Y., Han, M., & Li, G. (2023) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2022.919701 · Cited by 29
Klis, F. M., & Brul, S. (2015) · Eukaryotic Cell · doi:10.1128/ec.00142-15 · Cited by 27
Kijner, S., Ennis, D., Shmorak, S., Florentin, A., & Yassour, M. (2024) · Nature Communications · doi:10.1038/s41467-023-44437-y · Cited by 25
Evolutionary development and co‐phylogeny of primate‐associated bifidobacteria
Lugli, G. A., Alessandri, G., Milani, C., Mancabelli, L., Ruiz, L., Fontana, F., Borragán, S., González, A., Turroni, F., Ossiprandi, M. C., et al. (2020) · Environmental Microbiology · doi:10.1111/1462-2920.15108 · Cited by 24
Ouwerkerk, J. P., Tytgat, H. L. P., Elzinga, J., Koehorst, J., Van den Abbeele, P., Henrissat, B., Gueimonde, M., Cani, P. D., Van de Wiele, T., Belzer, C., et al. (2022) · Microorganisms · doi:10.3390/microorganisms10081605 · Cited by 23
Self-citationReductive acetogenesis is a dominant process in the ruminant hindgut
Li, Q., Huo, J., Ni, G., Zhang, F., Zhang, S., Zhang, X., Wang, R., Jiao, J., Yu, Z., Pu, X., et al. (2025) · Microbiome · doi:10.1186/s40168-024-02018-1 · Cited by 22
Kováčová, K., Degani, G., Stratilová, E., Farkaš, V., & Popolo, L. (2015) · FEMS Yeast Research · doi:10.1093/femsyr/fou011 · Cited by 21
Comparative Genomic Analysis of Bifidobacterium bifidum Strains Isolated from Different Niches
Lu, W., Pei, Z., Zang, M., Lee, Y.-K., Zhao, J., Chen, W., Wang, H., & Zhang, H. (2021) · Genes · doi:10.3390/genes12101504 · Cited by 17
cazy_webscraper: local compilation and interrogation of comprehensive CAZyme datasets
Hobbs, E. E. M., Gloster, T. M., & Pritchard, L. (2023) · Microbial Genomics · doi:10.1099/mgen.0.001086 · Cited by 15
Varejão, N., De-Andrade, R. A., Almeida, R. V., Anobom, C. D., Foguel, D., & Reverter, D. (2018) · Structure · doi:10.1016/j.str.2017.12.004 · Cited by 14
Human Gut Metagenomes Encode Diverse GH156 Sialidases
Mann, E., Shekarriz, S., & Surette, M. G. (2022) · Applied and Environmental Microbiology · doi:10.1128/aem.01755-22 · Cited by 12
Agl24 is an ancient archaeal homolog of the eukaryotic N-glycan chitobiose synthesis enzymes
Meyer, B. H., Adam, P. S., Wagstaff, B. A., Kolyfetis, G. E., Probst, A. J., Albers, S. V., & Dorfmueller, H. C. (2022) · eLife · doi:10.7554/elife.67448 · Cited by 12
Protein language models uncover carbohydrate-active enzyme function in metagenomics
Thurimella, K., Mohamed, A. M. T., Li, C., Vatanen, T., Graham, D. B., Owens, R. M., La Rosa, S. L., Plichta, D. R., Bacallado, S., & Xavier, R. J. (2025) · BMC Bioinformatics · doi:10.1186/s12859-025-06286-y · Cited by 9
Akhtar, A., Lata, M., Sunsunwal, S., Yadav, A., LNU, K., Subramanian, S., & Ramya, T. N. C. (2023) · Communications Biology · doi:10.1038/s42003-023-04718-0 · Cited by 9
Saburi, W., Nihira, T., Nakai, H., Kitaoka, M., & Mori, H. (2022) · Scientific Reports · doi:10.1038/s41598-021-04421-2 · Cited by 7
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Thurimella, K., Mohamed, A. M. T., Graham, D. B., Owens, R. M., La Rosa, S. L., Plichta, D. R., Bacallado, S., & Xavier, R. J. (2023) · doi:10.1101/2023.10.23.563620 · Cited by 7
Matta, T., Agrawal, K., Datta, P., Kumari, L., Bishnoi, M., Chopra, K., & Kondepudi, K. K. (2026) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-025-10628-w · Cited by 4
Lu, W., Zha, B., Lyu, J., LingHu, C., Chen, J., Deng, S., Zhang, X., Li, L., & Wang, G. (2024) · Frontiers in Microbiology · doi:10.3389/fmicb.2024.1500886 · Cited by 4
Metadata
- Authors
- Lombard, V., Golaconda Ramulu, H., Drula, E., Coutinho, P. M., & Henrissat, B.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2013-11-21
- Volume
- 42
- Issue
- D1
- Pages
- D490-D495
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- OpenAlex
- W2122559203
- Cited by
- 6,333
- References
- 3
- FWCI
- 148.60
- Type
- journal article
- Language
- en
- Open access
- gold
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Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
