2022
DOI: 10.1016/j.jprot.2022.104696
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BoMiProt 2.0: An update of the bovine milk protein database

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Cited by 5 publications
(3 citation statements)
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“…Several studies have focused on the cargo ingredients from milk exosomes. Analysis of the bovine milk protein database revealed that among different milk fractions, including whey, fat globule membranes, and exosomes, exosomes contained 684 exclusive proteins from an entire list of 6063 proteins [28]. Proteins can be post-translationally modified by glycosylation; some glycosylated proteins are associated with diseases and can serve as potential biomarkers.…”
Section: Source Of Milk Exosomesmentioning
confidence: 99%
“…Several studies have focused on the cargo ingredients from milk exosomes. Analysis of the bovine milk protein database revealed that among different milk fractions, including whey, fat globule membranes, and exosomes, exosomes contained 684 exclusive proteins from an entire list of 6063 proteins [28]. Proteins can be post-translationally modified by glycosylation; some glycosylated proteins are associated with diseases and can serve as potential biomarkers.…”
Section: Source Of Milk Exosomesmentioning
confidence: 99%
“…Bovine milk proteins databases BoMiProt (from 2020) [143] and upgraded BoMiProt 2.0 (from 2022) [144] are manually curated databases with over 10 642 proteins from whey, MFGM, and exosomes, including 1287 proteins with PTMs (http://www.bomiprot.org). Another protein atlas reporting of 4654 proteins from healthy cows found in 20 publications of milk proteomes has been compiled, in which the proteins are categorized based on milk fractions (skimmed milk, whey, MFGM, and exosomes), and according to five lactation stages [137].…”
Section: Databases Of Proteins Peptides and Ev-derived Proteins From ...mentioning
confidence: 99%
“…Given the importance of modifications of amino acid residues, contemporarily-developed computer programs take account of such modifications in protein sequences [1][2][3][4][5]. Databases annotating modified amino acid residues in proteins have recently been established as well [6][7][8]. Modifications of amino acid residues are also considered in records of peptide sequences in various databases [9][10][11][12][13][14][15][16][17][18] and during prediction of both structure [19] and physicochemical properties of peptides such as, for example, the isoelectric point [20].…”
Section: Introductionmentioning
confidence: 99%