Structurally intact (78-kDa) forms of maternal lactoferrin purified from urine of preterm infants fed human milk: identification of a trypsin-like proteolytic cleavage event in vivo that does not result in fragment dissociation.
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Candidacidal activities of human lactoferrin peptides derived from the N terminusBiological role of lactoferrinThe survival of ingested lactoferrin in the gastrointestinal tract of adult mice.Lactoferrin--a novel bone growth factorHuman lactoferrin and peptides derived from a surface-exposed helical region reduce experimental Escherichia coli urinary tract infection in mice.Breast milk lactoferrin regulates gene expression by binding bacterial DNA CpG motifs but not genomic DNA promoters in model intestinal cells.Lactoferrin and necrotizing enterocolitis.Lactoferrin: an iron-binding antimicrobial protein against Escherichia coli infection.Production and characterization of chimeric transferrins for the determination of the binding domains for bacterial transferrin receptors.Human lactoferrin and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant bacteria.Regulation of human mononuclear phagocyte migration by cell surface-binding proteins for advanced glycation end products.Glycosylated and unglycosylated human lactoferrins both bind iron and show identical affinities towards human lysozyme and bacterial lipopolysaccharide, but differ in their susceptibilities towards tryptic proteolysis.N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNAStructural and functional insights into Aeropyrum pernix OppA, a member of a novel archaeal OppA subfamilyLactoferrin inhibits hepatitis C virus viremia in patients with chronic hepatitis C: a pilot study.Concentration of Lactoferrin in Human Milk and Its Variation during Lactation in Different Chinese Populations
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P2860
Structurally intact (78-kDa) forms of maternal lactoferrin purified from urine of preterm infants fed human milk: identification of a trypsin-like proteolytic cleavage event in vivo that does not result in fragment dissociation.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on April 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Structurally intact (78-kDa) f ...... sult in fragment dissociation.
@en
Structurally intact
@nl
type
label
Structurally intact (78-kDa) f ...... sult in fragment dissociation.
@en
Structurally intact
@nl
prefLabel
Structurally intact (78-kDa) f ...... sult in fragment dissociation.
@en
Structurally intact
@nl
P2093
P2860
P356
P1476
Structurally intact (78-kDa) f ...... sult in fragment dissociation.
@en
P2093
P2860
P304
P356
10.1073/PNAS.88.8.2994
P407
P577
1991-04-01T00:00:00Z