BIOPEP-UWM Database of Bioactive Peptides: Current Opportunities
Open accessAbstract
The BIOPEP-UWM™ database of bioactive peptides (formerly BIOPEP) has recently become a popular tool in the research on bioactive peptides, especially on these derived from foods and being constituents of diets that prevent development of chronic diseases. The database is continuously updated and modified. The addition of new peptides and the introduction of new information about the existing ones (e.g., chemical codes and references to other databases) is in progress. New opportunities include the possibility of annotating peptides containing D-enantiomers of amino acids, batch processing option, converting amino acid sequences into SMILES code, new quantitative parameters characterizing the presence of bioactive fragments in protein sequences, and finding proteinases that release particular peptides.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Libraries of bioactive peptide sequences obtained via proteolysis of food proteins are widely available in databases like BIOPEP-UWM and contain modules of in silico proteolysis, activity prediction, and structure-function analysis.
“Libraries of bioactive peptide sequences obtained via proteolysis of food proteins are widely available in databases like BIOPEP-UWM and contain modules of in silico proteolysis, activity prediction, and structure-function analysis [209].”
From Navigating the potential of algal peptides: health effects, market applications, and scientific challenges (2026) · cites this paper as [209]
The Introduction describes BIOPEP-UWM as a widely used database for bioactive peptides, especially those derived from food. Section 6 (Analysis; page not provided) describes simulated proteolysis and profiles of potential biological activity. It does not describe a dedicated structure–function analysis module, so that part of the claim is not supported. (LLM, conf=0.84)
Experimental — accuracy not yet measuredBiological informatics platforms based on machine learning and artificial intelligence have transformed peptide studies by allowing predictions of bioactivity, toxicity, physicochemical properties, and possible health impact within hours.
“Biological informatics platforms based on machine learning and artificial intelligence (AI) have transformed the field of peptide studies by allowing predictions of bioactivity, toxicity, physicochemical properties, and possible health impact within hours.”
From Navigating the potential of algal peptides: health effects, market applications, and scientific challenges (2026) · cites this paper as [209]
Section 4 (Peptide Information; page not provided) says software can predict physicochemical and biological properties of compounds, including food peptides. Section 6 (Analysis; page not provided) describes tools for assessing potential peptide bioactivity. The cited paper does not establish that these platforms use machine learning or AI, predict toxicity and health impacts, or produce those predictions within hours. (LLM, conf=0.87)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Open Babel: An open chemical toolbox
O'Boyle, N. M., Banck, M. S., James, C. A. J., Morley, C., Vandermeersch, T., & Hutchison, G. R. (2011) · Journal of Cheminformatics · doi:10.1186/1758-2946-3-33 · Cited by 10,705 · see citing works
DrugBank 5.0: a major update to the DrugBank database for 2018
Wishart, D. S., Feunang, Y. D., Guo, A. C., Lo, E. J., Marcu, A., Grant, J. R., Sajed, T., Johnson, D., Li, C., Sayeeda, Z., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gkx1037 · Cited by 8,404 · see citing works
Weininger, D. (1988) · Journal of Chemical Information and Computer Sciences · doi:10.1021/ci00057a005 · Cited by 7,436 · see citing works
INFOGEST static in vitro simulation of gastrointestinal food digestion
Brodkorb, A., Egger, L., Alminger, M., Alvito, P., Assunção, R., Ballance, S., Bohn, T., Bourlieu-Lacanal, C., Boutrou, R., Carrière, F., et al. (2019) · Nature Protocols · doi:10.1038/s41596-018-0119-1 · Cited by 5,199 · see citing works
HMDB 4.0: the human metabolome database for 2018
Wishart, D. S., Feunang, Y. D., Marcu, A., Guo, A. C., Liang, K., Vázquez-Fresno, R., Sajed, T., Johnson, D., Li, C., Karu, N., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gkx1089 · Cited by 3,438 · see citing works
PubChem 2019 update: improved access to chemical data
Kim, S., Chen, J., Cheng, T., Gindulyte, A., He, J., He, S., Li, Q., Shoemaker, B. A., Thiessen, P. A., Yu, B., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gky1033 · Cited by 3,249 · see citing works
ZINC 15 – Ligand Discovery for Everyone
Sterling, T., & Irwin, J. J. (2015) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.5b00559 · Cited by 3,224 · see citing works
APD3: the antimicrobial peptide database as a tool for research and education
Wang, G., Li, X., & Wang, Z. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1278 · Cited by 2,402 · see citing works
ChEMBL: towards direct deposition of bioassay data
Mendez, D., Gaulton, A., Bento, A. P., Chambers, J., De Veij, M., Félix, E., Magariños, M. P., Mosquera, J. F., Mutowo, P., Nowotka, M., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gky1075 · Cited by 2,372 · see citing works
New approach for understanding genome variations in KEGG
Kanehisa, M. I., Sato, Y., Furumichi, M., Morishima, K., & Tanabe, M. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky962 · Cited by 1,845 · see citing works
Rawlings, N. D., Barrett, A. J., Thomas, P. D., Huang, X., Bateman, A., & Finn, R. D. (2018) · Nucleic Acids Research · doi:10.1093/nar/gkx1134 · Cited by 1,749 · see citing works
Improved Method for Determining Food Protein Degree of Hydrolysis
Nielsen, P., Petersen, D., & Dambmann, C. (2001) · Journal of Food Science · doi:10.1111/j.1365-2621.2001.tb04614.x · Cited by 1,728 · see citing works
Gilson, M. K., Liu, T., Baitaluk, M., Nicola, G., Hwang, L., & Chong, J. P. C. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1072 · Cited by 1,632 · see citing works
The CompTox Chemistry Dashboard: a community data resource for environmental chemistry
Williams, A. J., Grulke, C., Edwards, J., McEachran, A. D., Mansouri, K., Baker, N., Patlewicz, G. Y., Shah, I., Wambaugh, J. F., Judson, R., et al. (2017) · Journal of Cheminformatics · doi:10.1186/s13321-017-0247-6 · Cited by 1,164 · see citing works
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 · see citing works
InChI, the IUPAC International Chemical Identifier
Heller, S. R., Mcnaught, A. D., Плетнев, И. В., Stein, S. E., & Tchekhovskoi, D. V. (2015) · Journal of Cheminformatics · doi:10.1186/s13321-015-0068-4 · Cited by 875 · see citing works
Waghu, F. H., Barai, R. S., Gurung, P., & Idicula-Thomas, S. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1051 · Cited by 715 · see citing works
Haug, K., Salek, R. M., Conesa, P., Hastings, J., de Matos, P., Rijnbeek, M. L., Mahendraker, T., Williams, M., Neumann, S., Rocca‐Serra, P., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1004 · Cited by 647 · see citing works
Flexible Sequence Similarity Searching with the FASTA3 Program Package
Pearson, W. R. (2003) · Humana Press eBooks · doi:10.1385/1-59259-192-2:185 · Cited by 601 · see citing works
BIOPEP Database and Other Programs for Processing Bioactive Peptide Sequences
Mińkiewicz, P., Dziuba, J., Iwaniak, A., Dziuba, M., & Darewicz, M. (2008) · Journal of AOAC International · doi:10.1093/jaoac/91.4.965 · Cited by 540 · see citing works
Self-citationNielsen, S. D.-H., Beverly, R. L., Qu, Y., & Dallas, D. C. (2017) · Food Chemistry · doi:10.1016/j.foodchem.2017.04.056 · Cited by 496 · see citing works
Open Targets Platform: new developments and updates two years on
Carvalho‐Silva, D., Pierleoni, A., Pignatelli, M., Ong, C. K., Fumis, L., Karamanis, N., Carmona, M., Faulconbridge, A., Hercules, A., McAuley, E., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky1133 · Cited by 449 · see citing works
CancerPPD: a database of anticancer peptides and proteins
Tyagi, A. K., Tuknait, A., Anand, P., Gupta, S., Sharma, M., Mathur, D. D., Joshi, A., Singh, S., Gautam, A., & Raghava, G. P. S. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku892 · Cited by 401 · see citing works
BRENDA in 2019: a European ELIXIR core data resource
Jeske, L., Placzek, S., Schomburg, I., Chang, A., & Schomburg, D. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky1048 · Cited by 385 · see citing works
Plasmin in milk and dairy products: an update
Bastian, E. D., & Brown, R. J. (1996) · International Dairy Journal · doi:10.1016/0958-6946(95)00021-6 · Cited by 312 · see citing works
Bioinformatics approaches, prospects and challenges of food bioactive peptide research
Udenigwe, C. C. (2014) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2014.02.004 · Cited by 299 · see citing works
Tu, M., Cheng, S., Lu, W., & Du, M. (2018) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2018.04.005 · Cited by 278 · see citing works
Seed Protein of Lentils: Current Status, Progress, and Food Applications
Khazaeı, H., Subedi, M., Nickerson, M. T., Martínez‐Villaluenga, C., Frı́as, J., & Vandenberg, A. (2019) · Foods · doi:10.3390/foods8090391 · Cited by 266 · see citing works
ExplorEnz: the primary source of the IUBMB enzyme list
McDonald, A. G., Boyce, S., & Tipton, K. F. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn582 · Cited by 250 · see citing works
Pirtskhalava, M., Gabrielian, A. E., Cruz, P., Griggs, H. L., Squires, R. B., Hurt, D. E., Grigolava, M., Chubinidze, M., Gogoladze, G., Vishnepolsky, B., et al. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1174 · Cited by 246 · see citing works
SATPdb: a database of structurally annotated therapeutic peptides
Singh, S., Chaudhary, K., Dhanda, S. K., Bhalla, S., Usmani, S. S., Gautam, A., Tuknait, A., Agrawal, P., Mathur, D. D., & Raghava, G. P. S. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1114 · Cited by 242 · see citing works
SureChEMBL: a large-scale, chemically annotated patent document database
Papadatos, G., Davies, M., Dedman, N., Chambers, J. K., Gaulton, A., Siddle, J., Koks, R., Irvine, S. A., Pettersson, J., Goncharoff, N., et al. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1253 · Cited by 233 · see citing works
BitterDB: taste ligands and receptors database in 2019
Dagan‐Wiener, A., Pizio, A. D., Nissim, I., Bahia, M. S., Dubovski, N., Margulis, E., & Niv, M. Y. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky974 · Cited by 227 · see citing works
AHTPDB: a comprehensive platform for analysis and presentation of antihypertensive peptides
Kumar, R., Chaudhary, K., Sharma, M., Nagpal, G., Chauhan, J. S., Singh, S., Gautam, A., & Raghava, G. P. S. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1141 · Cited by 211 · see citing works
Agyei, D., Tsopmo, A., & Udenigwe, C. C. (2018) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-018-0974-1 · Cited by 189 · see citing works
PepBank - a database of peptides based on sequence text mining and public peptide data sources.
Shtatland, T., Guettler, D., Kossodo, M., Pivovarov, M., & Weissleder, R. (2007) · BMC Bioinformatics · doi:10.1186/1471-2105-8-280 · Cited by 181 · see citing works
BIOPEP database of sensory peptides and amino acids
Iwaniak, A., Mińkiewicz, P., Darewicz, M., Sieniawski, K., & Starowicz, P. (2016) · Food Research International · doi:10.1016/j.foodres.2016.04.031 · Cited by 176 · see citing works
Self-citationNANPDB: A Resource for Natural Products from Northern African Sources
Ntie‐Kang, F., Telukunta, K. K., Döring, K., Simoben, C. V., Moumbock, A. F. A., Malange, Y. I., Njume, L. E., Yong, J. N., Sippl, W., & Günther, S. (2017) · Journal of Natural Products · doi:10.1021/acs.jnatprod.7b00283 · Cited by 176 · see citing works
Piovesana, S., Capriotti, A. L., Cavaliere, C., Barbera, G. L., Montone, C. M., Chiozzi, R. Z., & Laganà, A. (2018) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-018-0852-x · Cited by 176 · see citing works
Hemolytik: a database of experimentally determined hemolytic and non-hemolytic peptides
Gautam, A., Chaudhary, K., Singh, S., Joshi, A., Anand, P., Tuknait, A., Mathur, D. D., Varshney, G. C., & Raghava, G. P. S. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1008 · Cited by 169 · see citing works
Bradbury, A. F., & Smyth, D. G. (1991) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(91)90044-v · Cited by 169 · see citing works
NeuroPep: a comprehensive resource of neuropeptides
Wang, Y., Wang, M., Yin, S., Jang, R., Wang, J., Xue, Z., & Xu, T. (2015) · Database · doi:10.1093/database/bav038 · Cited by 163 · see citing works
PubChem chemical structure standardization
Hähnke, V. D., Kim, S., & Bolton, E. (2018) · Journal of Cheminformatics · doi:10.1186/s13321-018-0293-8 · Cited by 163 · see citing works
SwissSidechain: a molecular and structural database of non-natural sidechains
Gfeller, D., Michielin, O. A., & Zoete, V. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks991 · Cited by 140 · see citing works
CutDB: a proteolytic event database
Igarashi, Y., Eroshkin, A. M., Gramatikova, S. I., Gramatikoff, K., Zhang, Y., Smith, J. W., Osterman, A. L., & Godzik, A. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl813 · Cited by 131 · see citing works
MilkAMP: a comprehensive database of antimicrobial peptides of dairy origin
Théolier, J., Fliss, I., Jean, J., & Hammami, R. (2013) · Dairy Science and Technology · doi:10.1007/s13594-013-0153-2 · Cited by 123 · see citing works
Judson, R., Martin, M. T., Egeghy, P. P., Gangwal, S., Reif, D. M., Kothiya, P., Wolf, M. A., Cathey, T., Transue, T. R., Smith, D., et al. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13021805 · Cited by 118 · see citing works
The EROP-Moscow oligopeptide database
Zamyatnin, A. A. (2005) · Nucleic Acids Research · doi:10.1093/nar/gkj008 · Cited by 118 · see citing works
Lin, K. F., Zhang, L., Han, X., Xin, L., Meng, Z., Gong, P.-M., & Cheng, D. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2018.02.051 · Cited by 117 · see citing works
Database of biologically active peptide sequences
Dziuba, J., Mińkiewicz, P., Nałȩcz, D., & Iwaniak, A. (1999) · Food / Nahrung · doi:10.1002/(sici)1521-3803(19990601)43:3 · Cited by 114 · see citing works
Self-citationMińkiewicz, P., Dziuba, J., & Michalska, J. (2011) · Food Science and Technology International · doi:10.1177/1082013210368461 · Cited by 108 · see citing works
Iwaniak, A., Mińkiewicz, P., Darewicz, M., & Hrynkiewicz, M. (2016) · Food Research International · doi:10.1016/j.foodres.2016.08.010 · Cited by 104 · see citing works
Self-citationUdenigwe, C. C., Gong, M., & Wu, S. (2013) · Process Biochemistry · doi:10.1016/j.procbio.2013.08.013 · Cited by 101 · see citing works
The Construction of a Bioactive Peptide Database in Metazoa
Liu, F., Baggerman, G., Schoofs, L., & Wets, G. (2008) · Journal of Proteome Research · doi:10.1021/pr800037n · Cited by 95 · see citing works
Brainpeps: the blood–brain barrier peptide database
Dorpe, S. V., Bronselaer, A., Nielandt, J., Stalmans, S., Wynendaele, E., Audenaert, K., de Wiele, C. V., Burvenich, C., Peremans, K. Y., Hsuchou, H., et al. (2011) · Brain Structure and Function · doi:10.1007/s00429-011-0375-0 · Cited by 94 · see citing works
Computer-aided characteristics of proteins as potential precursors of bioactive peptides
Dziuba, J., Iwaniak, A., & Mińkiewicz, P. (2003) · Polimery · doi:10.14314/polimery.2003.050 · Cited by 90 · see citing works
Self-citationChemometrics and cheminformatics in the analysis of biologically active peptides from food sources
Iwaniak, A., Mińkiewicz, P., Darewicz, M., Protasiewicz, M., & Mogut, D. (2015) · Journal of Functional Foods · doi:10.1016/j.jff.2015.04.038 · Cited by 89 · see citing works
Self-citationGarcía‐Vaquero, M., Mora, L., & Hayes, M. (2019) · Marine Drugs · doi:10.3390/md17040204 · Cited by 82 · see citing works
Martini, S., Conte, A., & Tagliazucchi, D. (2019) · Journal of Proteomics · doi:10.1016/j.jprot.2019.103500 · Cited by 82 · see citing works
ChemIDplus-Super Source for Chemical and Drug Information
Tomasulo, P. (2002) · Medical Reference Services Quarterly · doi:10.1300/j115v21n01_04 · Cited by 81 · see citing works
Iwaniak, A., Darewicz, M., Mogut, D., & Mińkiewicz, P. (2019) · Journal of Functional Foods · doi:10.1016/j.jff.2019.103486 · Cited by 76 · see citing works
Self-citationBioPepDB: an integrated data platform for food-derived bioactive peptides
Li, Q., Zhang, C., Chen, H., Xue, J., Guo, X., Liang, M., & Chen, M. (2018) · International Journal of Food Sciences and Nutrition · doi:10.1080/09637486.2018.1446916 · Cited by 74 · see citing works
FeptideDB: A web application for new bioactive peptides from food protein
Panyayai, T., Ngamphiw, C., Tongsima, S., Mhuantong, W., Limsripraphan, W., Choowongkomon, K., & Sawatdichaikul, O. (2019) · Heliyon · doi:10.1016/j.heliyon.2019.e02076 · Cited by 69 · see citing works
Purification, characterization, and milk coagulating properties of ginger proteases
Huang, X., Chen, L. J., Luo, Y. B., Guo, H. Y., & Ren, F. (2011) · Journal of Dairy Science · doi:10.3168/jds.2010-4024 · Cited by 68 · see citing works
Peptides reproducibly released byin vivodigestion of beef meat and trout flesh in pigs
Bauchart, C., Morzel, M., Chambon, C., Mirand, P. P., Reynès, C., Buffière, C., & Rémond, D. (2007) · British Journal Of Nutrition · doi:10.1017/s0007114507761810 · Cited by 67 · see citing works
Ortiz‐Martínez, M., de Mejı́a, E. G., García‐Lara, S., Aguilar, O., López-Castillo, L. M., & Otero-Pappatheodorou, J. T. (2017) · Journal of Functional Foods · doi:10.1016/j.jff.2017.04.015 · Cited by 65 · see citing works
The relevance of dipeptides and tripeptides in the bioactivity and taste of dry-cured ham
Gallego, M., Mora, L., & Toldrá, F. (2019) · Food Production Processing and Nutrition · doi:10.1186/s43014-019-0002-7 · Cited by 63 · see citing works
Holton, T. A., Vijayakumar, V., & Khaldi, N. (2013) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2013.08.009 · Cited by 62 · see citing works
Lee, K. H., Hong, S. Y., Oh, J. E., Kwon, M. Y., Yoon, J. H., Lee, J. H., Lee, B. L., & Moon, H. M. (1998) · Biochemical Journal · doi:10.1042/bj3340099 · Cited by 60 · see citing works
Jakubczyk, A., Karaś, M., Złotek, U., Szymanowska, U., Baraniak, B., & Bochnak, J. (2019) · LWT · doi:10.1016/j.lwt.2019.02.009 · Cited by 60 · see citing works
Huang, B.-B., Lin, H.-C., & Chang, Y. (2015) · Journal of Functional Foods · doi:10.1016/j.jff.2015.09.065 · Cited by 58 · see citing works
Updating the research on the chemopreventive and therapeutic role of the peptide lunasin
Hsieh, C., Martínez‐Villaluenga, C., de Lumen, B. O., & Hernández‐Ledesma, B. (2017) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.8719 · Cited by 54 · see citing works
He, R., Malomo, S., Girgih, A., Ju, X.-R., & Aluko, R. (2013) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf400865m · Cited by 52 · see citing works
The Royal Society of Chemistry and the delivery of chemistry data repositories for the community
Williams, A. J., & Tkachenko, V. (2014) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-014-9784-5 · Cited by 52 · see citing works
Duffy, F. J., Verniere, M., Devocelle, M. C., Bernard, E., Shields, D. C., & Chubb, A. J. (2011) · Journal of Chemical Information and Modeling · doi:10.1021/ci100431r · Cited by 51 · see citing works
Siani, M. A., Weininger, D., & Blaney, J. M. (1994) · Journal of Chemical Information and Computer Sciences · doi:10.1021/ci00019a017 · Cited by 50 · see citing works
Engel, T. 1., Gasteiger, J. 1., & Wiley-VCH (2018) · Wiley eBooks · doi:10.1002/9783527806539 · Cited by 45 · see citing works
Bridging protein local structures and protein functions
Liu, Z., Wu, L., Wang, Y., Zhang, X., & Chen, L. (2008) · Amino Acids · doi:10.1007/s00726-008-0088-8 · Cited by 43 · see citing works
Juhász, A., Haraszi, R., & Maulis, C. (2015) · Database · doi:10.1093/database/bav100 · Cited by 43 · see citing works
Tapal, A., Vegarud, G. E., Sreedhara, A., & Tiku, P. K. (2019) · Food & Function · doi:10.1039/c8fo01933a · Cited by 42 · see citing works
Mojica, L., Luna‐Vital, D. A., & de Mejı́a, E. G. (2018) · Toxicology Reports · doi:10.1016/j.toxrep.2018.04.007 · Cited by 41 · see citing works
Yu, Z., Fan, Y., Zhao, W., Ding, L., Li, J., & Liu, J. (2018) · Journal of Food Science · doi:10.1111/1750-3841.14299 · Cited by 41 · see citing works
Ashok, A., Brijesha, N., & Aparna, H. S. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.07.009 · Cited by 39 · see citing works
Pinciroli, M., Aphalo, P., Nardo, A. E., Añón, M. C., & Quiroga, A. V. (2019) · Plant Foods for Human Nutrition · doi:10.1007/s11130-019-00754-6 · Cited by 36 · see citing works
Anekthanakul, K., Hongsthong, A., Senachak, J., & Ruengjitchatchawalya, M. (2018) · BMC Bioinformatics · doi:10.1186/s12859-018-2143-0 · Cited by 31 · see citing works
Common Amino Acid Subsequences in a Universal Proteome—Relevance for Food Science
Mińkiewicz, P., Darewicz, M., Iwaniak, A., Sokołowska, J., Starowicz, P., Bucholska, J., & Hrynkiewicz, M. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms160920748 · Cited by 30 · see citing works
Self-citationPreface for Volume 7: Natural and Artificial Flavoring Agents and Food Dyes
Grumezescu, A. M., & Holban, A. M. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-811518-3.00022-3 · Cited by 29 · see citing works
Annotation of Peptide Structures Using SMILES and Other Chemical Codes–Practical Solutions
Mińkiewicz, P., Iwaniak, A., & Darewicz, M. (2017) · Molecules · doi:10.3390/molecules22122075 · Cited by 27 · see citing works
Self-citationDziuba, M., Mińkiewicz, P., & Dąbek, M. (2014) · PubMed · Cited by 26 · see citing works
Mińkiewicz, P., Darewicz, M., Iwaniak, A., Bucholska, J., Starowicz, P., & Bialobrodzka, E. G. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17122039 · Cited by 25 · see citing works
Self-citationLarge-scale mapping of bioactive peptides in structural and sequence space
Nardo, A. E., Añón, M. C., & Parisi, G. D. (2018) · PLoS ONE · doi:10.1371/journal.pone.0191063 · Cited by 23 · see citing works
In Silico Analysis of Bioactive Peptides in Invasive Sea Grass Halophila stipulacea
Çavaş, Ç. K., Pérez‐Sánchez, H., Ozupek, N. M., & Çavaş, L. (2019) · Cells · doi:10.3390/cells8060557 · Cited by 22 · see citing works
Yu, D., Wang, C., Song, Y., Zhu, J., & Zhang, X. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20174159 · Cited by 21 · see citing works
Fragmentomics of natural peptide structures
Zamyatnin, A. A. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909130100 · Cited by 19 · see citing works
Chemoinformatics in Food Science
Peña‐Castillo, A., Méndez‐Lucio, O., Owen, J. R., Martínez‐Mayorga, K., & Medina‐Franco, J. L. (2018) · Wiley eBooks · doi:10.1002/9783527806539.ch10 · Cited by 19 · see citing works
Savitha, M. N., Siddesha, J. M., Suvilesh, K. N., Manjunath, Y., Kameshwar, V. H., D’Souza, C. J. M., Umashankara, M., & Vishwanath, B. S. (2018) · Peptides · doi:10.1016/j.peptides.2018.11.002 · Cited by 18 · see citing works
Structural properties of proteolytic-accessible bioactive fragments of selected animal proteins
Dziuba, J., Niklewicz, M., Iwaniak, A., Darewicz, M., & Mińkiewicz, P. (2005) · Polimery · doi:10.14314/polimery.2005.424 · Cited by 16 · see citing works
Self-citationMińkiewicz, P., Iwaniak, A., & Darewicz, M. (2015) · Journal of Chemical Education · doi:10.1021/ed5006739 · Cited by 15 · see citing works
Self-citationOnline Programs and Databases of Peptides and Proteolytic Enzymes – A Brief Update for 2007–2008
Mińkiewicz, P., Darewicz, M., Iwaniak, A., Michalska, J., & Dziuba, J. (2009) · University of Zagreb University Computing Centre (SRCE) · Cited by 12 · see citing works
Self-citationComputer-Aided Drug Design Studies in Food Chemistry
Scotti, L., Mendonça, F. J. B., Ishiki, H. M., Ribeiro, F. F., Duarte, M. C., Santana, G. S., Oliveira, T. B., Diniz, M. D. F. F. M., Quintans‐Júnior, L. J., & Scotti, L. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-811518-3.00009-0 · Cited by 11 · see citing works
In Silico Analysis of Peptide Potential Biological Functions
Калмыкова, С. Д., Arapidi, G. P., Urban, A. S., Osetrova, M., Gordeeva, V. D., Иванов, В. Т., & Govorun, V. M. (2018) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s106816201804009x · Cited by 11 · see citing works
Mińkiewicz, P., Turło, M., Iwaniak, A., & Darewicz, M. (2019) · Molecules · doi:10.3390/molecules24040789 · Cited by 6 · see citing works
Self-citation
Flagged first, then by citations
2 of the 104 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Molecular representations in AI-driven drug discovery: a review and practical guide
David, L., Thakkar, A., Mercado, R., & Engkvist, O. (2020) · Journal of Cheminformatics · doi:10.1186/s13321-020-00460-5 · Cited by 587 · see citing works
Limón, A. M. V., Aguilar-Toalá, J. E., & Liceaga, A. M. (2022) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c06110 · Cited by 534 · see citing works
Wen, C., Zhang, J., Zhang, H., Duan, Y., & Ma, H. (2020) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2020.09.019 · Cited by 462 · see citing works
A Global Review on Short Peptides: Frontiers and Perspectives
Apostolopoulos, V., Bojarska, J., Chai, T., Elnagdy, S. M., Kaczmarek, K., Matsoukas, J., New, R. R. C., Parang, K., Paredes‐López, O., Parhiz, H., et al. (2021) · Molecules · doi:10.3390/molecules26020430 · Cited by 441 · see citing works
Current Trends of Bioactive Peptides—New Sources and Therapeutic Effect
Jakubczyk, A., Karaś, M., Rybczyńska‐Tkaczyk, K., Zielińska, E., & Zieliński, D. (2020) · Foods · doi:10.3390/foods9070846 · Cited by 259 · see citing works
Charoenkwan, P., Yana, J., Nantasenamat, C., Hasan, M. M., & Shoombuatong, W. (2020) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.0c00707 · Cited by 193 · see citing works
Advances in the stability challenges of bioactive peptides and improvement strategies
Pei, J., Gao, X., Pan, D., Hua, Y., He, J., Liu, Z., & Dang, Y. (2022) · Current Research in Food Science · doi:10.1016/j.crfs.2022.10.031 · Cited by 189 · see citing works
Goshisht, M. K. (2024) · ACS Omega · doi:10.1021/acsomega.3c05913 · Cited by 169 · see citing works
Bioinformatics approaches to discovering food-derived bioactive peptides: Reviews and perspectives
Du, Z., Comer, J. R., & Li, Y. (2023) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2023.117051 · Cited by 161 · see citing works
In vivo bioactivities of food protein-derived peptides – a current review
Daroit, D. J., & Brandelli, A. (2021) · Current Opinion in Food Science · doi:10.1016/j.cofs.2021.01.002 · Cited by 158 · see citing works
Zhou, Y., Wu, W., Zhang, N., Soladoye, O. P., Zhang, Y., & Fu, Y. (2022) · Food Research International · doi:10.1016/j.foodres.2022.111842 · Cited by 150 · see citing works
Industrial production of spirulina as a protein source for bioactive peptide generation
Lafarga, T., Sánchez‐Zurano, A., Villaró, S., Morillas‐España, A., & Acién, F. G. (2021) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2021.07.018 · Cited by 139 · see citing works
Brewer’s Spent Grains: Possibilities of Valorization, a Review
Chetrariu, A., & Dabija, A. (2020) · Applied Sciences · doi:10.3390/app10165619 · Cited by 138 · see citing works
Du, Z., Ding, X., Xu, Y., & Li, Y. (2023) · Briefings in Bioinformatics · doi:10.1093/bib/bbad135 · Cited by 137 · see citing works
Tonolo, F., Fiorese, F., Moretto, L., Folda, A., Scalcon, V., Grinzato, A., Ferro, S., Arrigoni, G., Bindoli, A., Feller, E., et al. (2020) · Antioxidants · doi:10.3390/antiox9020117 · Cited by 133 · see citing works
Bielecka, M. M., Cichosz, G., & Czeczot, H. (2021) · International Dairy Journal · doi:10.1016/j.idairyj.2021.105208 · Cited by 132 · see citing works
Charoenkwan, P., Nantasenamat, C., Hasan, M. M., Moni, M. A., Manavalan, B., & Shoombuatong, W. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222313124 · Cited by 125 · see citing works
Bioactive peptides derived from fermented foods: Preparation and biological activities
Guo, Q., Chen, P., & Chen, X. (2023) · Journal of Functional Foods · doi:10.1016/j.jff.2023.105422 · Cited by 125 · see citing works
Piskov, S., Timchenko, L. D., Grimm, W., Rzhepakovsky, I. V., Avanesyan, S. S., Sizonenko, M., & Kurchenko, V. (2020) · Foods · doi:10.3390/foods9020160 · Cited by 121 · see citing works
Meat and plant-based meat analogs: Nutritional profile and in vitro digestion comparison
Yang, Y., Zheng, Y., Ma, W., Zhang, Y., Sun, C., & Fang, Y. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.108886 · Cited by 121 · see citing works
Mirzaei, M., Shavandi, A., Mirdamadi, S., Soleymanzadeh, N., Motahari, P., Mirdamadi, N., Moser, M., Subra, G., Alimoradi, H., & Goriely, S. (2021) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2021.10.008 · Cited by 119 · see citing works
Du, Z., & Li, Y. (2022) · Journal of Agriculture and Food Research · doi:10.1016/j.jafr.2022.100353 · Cited by 112 · see citing works
Barati, M., Javanmardi, F., Jazayeri, S. M. H. M., Jabbari, M., Rahmani, J., Barati, F., Nickho, H., Davoodi, S. H., Roshanravan, N., & Khaneghah, A. M. (2020) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12578 · Cited by 108 · see citing works
Charoenkwan, P., Kanthawong, S., Nantasenamat, C., Hasan, M. M., & Shoombuatong, W. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.0c00590 · Cited by 104 · see citing works
López‐Pedrouso, M., Borrajo, P., Pateiro, M., Lorenzo, J. M., & Franco, D. (2020) · Food Research International · doi:10.1016/j.foodres.2020.109389 · Cited by 103 · see citing works
Immunomodulatory peptides—A promising source for novel functional food production and drug discovery
Pavlićević, M., Marmiroli, N., & Maestri, E. (2021) · Peptides · doi:10.1016/j.peptides.2021.170696 · Cited by 102 · see citing works
Hashemi, Z. S., Zarei, M., Fath, M. K., Ganji, M., Farahani, M. S., Afsharnouri, F., Pourzardosht, N., Khalesi, B., Jahangiri, A., Rahbar, M. R., et al. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.669431 · Cited by 101 · see citing works
pLM4ACE: A protein language model based predictor for antihypertensive peptide screening
Du, Z., Ding, X., Hsu, W. W. Y., Munir, A., Xu, Y., & Li, Y. (2023) · Food Chemistry · doi:10.1016/j.foodchem.2023.137162 · Cited by 98 · see citing works
DFBP: a comprehensive database of food-derived bioactive peptides for peptidomics research
Qin, D., Bo, W., Zheng, X., Hao, Y., Li, B., Zheng, J., & Liang, G. (2022) · Bioinformatics · doi:10.1093/bioinformatics/btac323 · Cited by 96 · see citing works
Umami-MRNN: Deep learning-based prediction of umami peptide using RNN and MLP
Qi, L., Du, J., Sun, Y., Xiong, Y., Zhao, X., Pan, D., Zhi, Y., Dang, Y., & Gao, X. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.134935 · Cited by 96 · see citing works
Hall, F. G., Reddivari, L., & Liceaga, A. M. (2020) · Nutrients · doi:10.3390/nu12113588 · Cited by 94 · see citing works
Bioactive peptides generated in the processing of dry-cured ham
Toldrá, F., Gallego, M., Reig, M., Aristoy, M., & Mora, L. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.126689 · Cited by 93 · see citing works
Tonolo, F., Moretto, L., Grinzato, A., Fiorese, F., Folda, A., Scalcon, V., Ferro, S., Arrigoni, G., Bellamio, M., Feller, E., et al. (2020) · Antioxidants · doi:10.3390/antiox9121306 · Cited by 93 · see citing works
Natural Compounds with Antimicrobial Properties in Cosmetics
Rybczyńska‐Tkaczyk, K., Grenda, A., Jakubczyk, A., Kiersnowska, K., & Bik-Małodzińśka, M. (2023) · Pathogens · doi:10.3390/pathogens12020320 · Cited by 93 · see citing works
Bo, W., Chen, L., Qin, D., Geng, S., Li, J., Hu, M. Y., Li, B., & Liang, G. (2021) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2021.05.031 · Cited by 91 · see citing works
Lee, C. H., Hamdan, N., Nyakuma, B. B., Wong, S. L., Wong, K. Y., Tan, H., Jamaluddin, H., & Lee, T. H. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.139797 · Cited by 91 · see citing works
Kaczmarska, K. T., Taylor, M. C., Piyasiri, U., & Frank, D. C. (2021) · Foods · doi:10.3390/foods10040801 · Cited by 88 · see citing works
Cui, Z., Qi, C., Zhou, T., Yu, Y., Wang, Y., Zhang, Z., Zhang, Y., Wang, W., & Liu, Y. (2025) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.70068 · Cited by 88 · see citing works
Nielsen, S. D.-H., Jakobsen, L. M. A., Geiker, N. R. W., & Bertram, H. C. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.131919 · Cited by 87 · see citing works
Bioactive peptides of whey: obtaining, activity, mechanism of action, and further applications
Olvera-Rosales, L. B., Cruz-Guerrero, A. E., García-Garibay, J. M., Gómez‐Ruiz, L., Contreras‐López, E., Guzmán‐Rodríguez, F., & González-Olivares, L. G. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2079113 · Cited by 87 · see citing works
Milk-Derived Antimicrobial Peptides: Overview, Applications, and Future Perspectives
Singh, A., Duche, R. T., Wandhare, A. G., Kaur, J., Singh, B. P., Sihag, M. K., Singh, K. S., Sangwan, V., Talan, S., & Panwar, H. (2022) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-022-10004-y · Cited by 86 · see citing works
Xu, Y., Yang, Y., Ma, C., Bian, X., Liu, X.-F., Wang, Y., Chen, F., Wang, B., Zhang, G., & Zhang, N. (2023) · Food Research International · doi:10.1016/j.foodres.2023.113473 · Cited by 84 · see citing works
Zhang, M., Zhu, L., Wu, G., Liu, T., Qi, X., & Zhang, H. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2120454 · Cited by 80 · see citing works
Ren, L., Fan, J., Yang, Y., Liu, X.-F., Wang, B., Bian, X., Wang, D.-F., Xu, Y., Liu, B., Zhu, P.-Y., et al. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.135230 · Cited by 80 · see citing works
Shen, S. C.-Y., Khare, E., Lee, N., Saad, M. K., Kaplan, D. L., & Buehler, M. J. (2023) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00479 · Cited by 78 · see citing works
Bozkurt, F., Beki̇roğlu, H., Dogan, K., Karasu, S., & Sağdıç, O. (2021) · LWT · doi:10.1016/j.lwt.2021.111787 · Cited by 77 · see citing works
Applications and analysis of hydrolysates in animal cell culture
Ho, Y. Y., Lu, H., Lim, Z. F. S., Lim, H. W., Ho, Y. S., & Ng, S. K. (2021) · Bioresources and Bioprocessing · doi:10.1186/s40643-021-00443-w · Cited by 77 · see citing works
Yeşiltaş, B., García‐Moreno, P. J., Echers, S. G., Olsen, T. H., Jones, N. C., Hoffmann, S. V., Marcatili, P., Overgaard, M. T., Hansen, E. B., & Jacobsen, C. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.132699 · Cited by 77 · see citing works
Conventional and in silico approaches to select promising food-derived bioactive peptides: A review
Peredo-Lovillo, A. G., Hernández‐Mendoza, A., Vallejo‐Córdoba, B., & Romero‐Luna, H. E. (2021) · Food Chemistry X · doi:10.1016/j.fochx.2021.100183 · Cited by 76 · see citing works
Artificial intelligence in food bioactive peptides screening: Recent advances and future prospects
Chang, J. Y., Wang, H., Su, W., He, X., & Tan, M. (2024) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2024.104845 · Cited by 74 · see citing works
Fuentes, L., Richard, C., & Chen, L. (2021) · Journal of Functional Foods · doi:10.1016/j.jff.2021.104829 · Cited by 73 · see citing works
Rivero‐Pino, F., Millán-Linares, M. C., & la Paz, S. M. (2023) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2023.06.023 · Cited by 73 · see citing works
Tong, X., Lian, Z., Miao, L., Qi, B., Zhang, S., Li, Y., Wang, H., & Jiang, L. (2020) · LWT · doi:10.1016/j.lwt.2020.110151 · Cited by 72 · see citing works
Cui, L., Guo, Y., Lu, S., Zeng, X., He, J., Guo, Y., Pan, D., & Wu, Z. F. (2022) · Food Research International · doi:10.1016/j.foodres.2022.111339 · Cited by 72 · see citing works
Nolasco, A., Squillante, J., Velotto, S., D’Auria, G., Ferranti, P., Mamone, G., Errico, M. E., Avolio, R., Castaldo, R., Cirillo, T., et al. (2022) · Journal of Cleaner Production · doi:10.1016/j.jclepro.2022.133520 · Cited by 72 · see citing works
Guzmán-Lorite, M., Marina, M. L., & García, M. C. (2022) · Food Research International · doi:10.1016/j.foodres.2022.111862 · Cited by 72 · see citing works
Characteristics of Food Protein-Derived Antidiabetic Bioactive Peptides: A Literature Update
Nong, N. T. P., & Hsu, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179508 · Cited by 70 · see citing works
Бегунова, А. В., Savinova, О. S., Glazunova, O. A., Moiseenko, K. V., Рожкова, И. В., & Федорова, Т. В. (2020) · Foods · doi:10.3390/foods10010017 · Cited by 69 · see citing works
Urbizo-Reyes, U., Liceaga, A. M., Reddivari, L., Kim, K., & Anderson, J. M. (2021) · Journal of Functional Foods · doi:10.1016/j.jff.2021.104892 · Cited by 68 · see citing works
Applications of deep learning in understanding gene regulation
Li, Z., Gao, E., Zhou, J., Han, W., Xu, X., & Gao, X. (2023) · Cell Reports Methods · doi:10.1016/j.crmeth.2022.100384 · Cited by 68 · see citing works
Bu, Y., Liu, Y., Luan, H., Zhu, W., Li, X., & Li, J. (2021) · Food & Function · doi:10.1039/d0fo03326j · Cited by 67 · see citing works
Identification and molecular interactions of novel ACE inhibitory peptides from rapeseed protein
Duan, X., Dong, Y., Zhang, M., Li, Z., Bu, G., & Chen, F. (2023) · Food Chemistry · doi:10.1016/j.foodchem.2023.136085 · Cited by 67 · see citing works
Lertampaiporn, S., Vorapreeda, T., Hongsthong, A., & Thammarongtham, C. (2021) · Genes · doi:10.3390/genes12020137 · Cited by 66 · see citing works
Bioactive peptides in fermented foods and their application: a critical review
Chourasia, R., Phukon, L. C., Abedin, M. M., Padhi, S., Singh, S. P., & Kumar, A. (2022) · Systems Microbiology and Biomanufacturing · doi:10.1007/s43393-022-00125-4 · Cited by 65 · see citing works
Li, J., Liu, X., Li, W., Wu, D., Zhang, Z., Chen, W., & Yang, Y. (2023) · Food Chemistry · doi:10.1016/j.foodchem.2023.137057 · Cited by 65 · see citing works
In Silico and In Vitro Analysis of Multifunctionality of Animal Food-Derived Peptides
Amigo, L., Martínez‐Maqueda, D., & Hernández‐Ledesma, B. (2020) · Foods · doi:10.3390/foods9080991 · Cited by 64 · see citing works
Abedin, M. M., Chourasia, R., Phukon, L. C., Singh, S. P., & Rai, A. K. (2022) · Food Chemistry X · doi:10.1016/j.fochx.2022.100231 · Cited by 64 · see citing works
An, F., Cao, K., Ji, S., Wang, Y., Pan, G., Ma, Y., Zhao, Y., Wu, J., & Wu, R. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.134583 · Cited by 64 · see citing works
Gu, Y., Zhang, J., Niu, Y., Sun, B., Liu, Z., Mao, X., & Zhang, Y. (2024) · LWT · doi:10.1016/j.lwt.2024.115780 · Cited by 64 · see citing works
Potential of green and roasted coffee beans and spent coffee grounds to provide bioactive peptides
Ribeiro, E., Rocha, T. D. S., & Prudêncio, S. H. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.129061 · Cited by 64 · see citing works
Bautista-Expósito, S., Vandenberg, A., Peñas, E., Frı́as, J., & Martínez‐Villaluenga, C. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.754287 · Cited by 63 · see citing works
Shi, C., Liu, M., Zhao, H., Lv, Z., Liang, L., & Zhang, B. (2022) · Antioxidants · doi:10.3390/antiox11010127 · Cited by 63 · see citing works
Du, Z., Wang, D., & Li, Y. (2022) · ACS Omega · doi:10.1021/acsomega.2c03062 · Cited by 62 · see citing works
Mińkiewicz, P., Iwaniak, A., & Darewicz, M. (2022) · Applied Sciences · doi:10.3390/app12147204 · Cited by 61 · see citing works
Self-citationCorrêa, J. A. F., Nazareth, T. D. M., da Rocha, G. F., & Luciano, F. B. (2023) · Pathogens · doi:10.3390/pathogens12030477 · Cited by 61 · see citing works
Accelerating bioactive peptide discovery via mutual information-based meta-learning
He, W., Jiang, Y., Jin, J., Li, Z., Zhao, J., Manavalan, B., Su, R., Gao, X., & Wei, L. (2021) · Briefings in Bioinformatics · doi:10.1093/bib/bbab499 · Cited by 61 · see citing works
Screening of Novel Bioactive Peptides from Goat Casein: In Silico to In Vitro Validation
Coscueta, E. R., Batista, P., Gomes, J. E. G., da Silva, R., & Pintado, M. M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052439 · Cited by 60 · see citing works
Vincenzi, M., Mercurio, F. A., & Leone, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031798 · Cited by 60 · see citing works
Olalere, O. A., Yap, P., & Gan, C. (2023) · Journal of Proteins and Proteomics · doi:10.1007/s42485-023-00106-8 · Cited by 59 · see citing works
Gu, H., Gao, J., Shen, Q., Gao, D., Wang, Q., Tangyu, M., & Mao, X. (2020) · LWT · doi:10.1016/j.lwt.2020.110587 · Cited by 59 · see citing works
Xiao, C., Toldrá, F., Zhao, M., Zhou, F., Luo, D., Jia, R., & Mora, L. (2022) · Food Research International · doi:10.1016/j.foodres.2022.111253 · Cited by 58 · see citing works
Zhi, T., Li, X., Sadiq, F. A., Mao, K., Gao, J., Mi, S., Liu, X., Deng, W., Chitrakar, B., & Sang, Y. (2022) · LWT · doi:10.1016/j.lwt.2022.113636 · Cited by 58 · see citing works
Senadheera, T. R. L., Hossain, A., Dave, D., & Shahidi, F. (2022) · Marine Drugs · doi:10.3390/md20100610 · Cited by 58 · see citing works
Molecular Modelling in Bioactive Peptide Discovery and Characterisation
Agoni, C., Fernández-Díaz, R., Timmons, P. B., Adelfio, A., Gómez, H., & Shields, D. C. (2025) · Biomolecules · doi:10.3390/biom15040524 · Cited by 59 · see citing works
Arámburo-Gálvez, J. G., Arvizu-Flores, A. A., Cárdenas-Torres, F. I., Cabrera‐Chávez, F., Ramírez-Torres, G. I., Flores-Mendoza, L. K., Gastelum-Acosta, P. E., Figueroa-Salcido, O. G., & Ontiveros, N. (2022) · Foods · doi:10.3390/foods11111576 · Cited by 57 · see citing works
Rzhepakovsky, I. V., Areshidze, D. A., Avanesyan, S. S., Grimm, W., Filatova, N. V., Kalinin, A. V., Kochergin, S., Kozlova, M., Kurchenko, V. P., Sizonenko, M., et al. (2022) · Molecules · doi:10.3390/molecules27030762 · Cited by 56 · see citing works
Bioactive Peptides: An Understanding from Current Screening Methodology
Nong, N. T. P., & Hsu, J. (2022) · Processes · doi:10.3390/pr10061114 · Cited by 54 · see citing works
Zhang, Y., Dai, Z., Zhao, X., Chen, C., Li, S., Meng, Y., Suonan, Z., Sun, Y., Shen, Q., Wang, L., et al. (2022) · Food Chemistry · doi:10.1016/j.foodchem.2022.134690 · Cited by 54 · see citing works
Basri, N. I., Amin, A. M., & Ahmad, F. (2025) · Quality Assurance and Safety of Crops & Foods · doi:10.15586/qas.v17i1.1525 · Cited by 55 · see citing works
Effect of Gelatin Coating Enriched with Antioxidant Tomato By-Products on the Quality of Pork Meat
Gallego, M., Arnal, M., Talens, P., Toldrá, F., & Mora, L. (2020) · Polymers · doi:10.3390/polym12051032 · Cited by 54 · see citing works
Characteristics of Biopeptides Released In Silico from Collagens Using Quantitative Parameters
Iwaniak, A., Mińkiewicz, P., Pliszka, M., Mogut, D., & Darewicz, M. (2020) · Foods · doi:10.3390/foods9070965 · Cited by 54 · see citing works
Self-citationYap, P., & Gan, C. (2020) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2020.09.005 · Cited by 54 · see citing works
Tong, X., Cao, J., Sun, M., Liao, P., Dai, S., Cui, W., Cheng, X., Li, Y., Jiang, L., & Wang, H. (2021) · LWT · doi:10.1016/j.lwt.2021.111782 · Cited by 53 · see citing works
A structural explanation for protein digestibility changes in different food matrices
Chen, J., Gao, Q., Zhang, X., Bassey, A. P., Zeng, X., Zhou, G., & Xu, X. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.108281 · Cited by 53 · see citing works
Wang, F., Sangfuang, N., McCoubrey, L. E., Yadav, V., Elbadawi, M., Orlu, M., Gaisford, S., & Basit, A. W. (2023) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2023.122643 · Cited by 53 · see citing works
Chen, R., Liu, X., Xiang, J., Sun, W., & Tomasevic, I. B. (2023) · Meat Science · doi:10.1016/j.meatsci.2023.109261 · Cited by 53 · see citing works
Zhao, L., Zhang, M., Pan, F., Li, J., Dou, R., Wang, X., Wang, Y., He, Y., Wang, S., & Cai, S. (2021) · Current Research in Food Science · doi:10.1016/j.crfs.2021.08.008 · Cited by 52 · see citing works
MPMABP: A CNN and Bi-LSTM-Based Method for Predicting Multi-Activities of Bioactive Peptides
Li, Y., Li, X., Liu, Y., Yao, Y., & Huang, G. (2022) · Pharmaceuticals · doi:10.3390/ph15060707 · Cited by 52 · see citing works
Rational Discovery of Antimicrobial Peptides by Means of Artificial Intelligence
Puentes, P. R., Henao, M. C., Cifuentes, J., Muñoz-Camargo, C., Reyes, L. H., Cruz, J. C., & Arbeláez, P. (2022) · Membranes · doi:10.3390/membranes12070708 · Cited by 52 · see citing works
Ramírez, K., Pineda‐Hidalgo, K. V., & Rochín-Medina, J. J. (2020) · LWT · doi:10.1016/j.lwt.2020.110685 · Cited by 52 · see citing works
- Authors
- Minkiewicz, P., Iwaniak, A., & Darewicz, M.
- Affiliations
- Chair of Food Biochemistry, University of Warmia and Mazury in Olsztyn, Plac Cieszyński 1, 10-726 Olsztyn-Kortowo, Poland
- University of Warmia and Mazury in Olsztyn (PL)
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2019-11-27
- Volume
- 20
- Issue
- 23
- Pages
- 5978
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC6928608
- OpenAlex
- W2989775272
- Cited by
- 958
- References
- 104
- Citations by year
- 2026: 161 · 2025: 189 · 2024: 156 · 2023: 160 · 2022: 135 · 2021: 103 · 2020: 53 · 2019: 1
- FWCI
- 24.15
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- The project was financially supported by the Minister of Science and Higher Education in the range of the program entitled “Regional Initiative of Excellence” for the years 2019–2022, amount of funding 12,000,000 PLN (010/RID/2018/19)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Hydrolysis and Bioactive Peptides
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Keywords
- bioactive peptides, peptide database, food-derived peptides, chronic disease prevention, D-enantiomer, peptide annotation
- MeSH terms
- Amino Acid Sequence, Amino Acids, Animals, Humans, Peptide Hydrolases, Peptides, Databases, Factual
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review