Results 201 to 210 of about 42,582 (271)
Computational insights and insecticidal activity of black gram defensin proteins against bruchids (Callosobruchus maculatus). [PDF]
Sci RepDayma J +6 more
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Protective Effects of Recombinant <i>Lactobacillus paracasei</i> Expressing Porcine β-Defensin 2 Against DSS-Induced Colitis in a Murine Model. [PDF]
Animals (Basel)Chen Y +5 more
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A multifunctional fungal defensin bladesin loaded-hydrogel for accelerated infectious wound healing. [PDF]
Int J Pharm XChen Y, Yu Y, Shen B.
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α-Defensin Accuracy to Diagnose Periprosthetic Joint Infection—Best Available Test?
Journal of Arthroplasty, 2016CARLOS Higuera +2 more
exaly +2 more sources
Pharmacology & Therapeutics, 1994
Defensins are widely distributed and abundant 3-4 kDa antimicrobial peptides that are variable cationic and contain six disulfide-paired cysteines. Three structurally distinct peptide families have been identified: 'classical' defensins, beta-defensins and insect defensins.
T, Ganz, R I, Lehrer
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Defensins are widely distributed and abundant 3-4 kDa antimicrobial peptides that are variable cationic and contain six disulfide-paired cysteines. Three structurally distinct peptide families have been identified: 'classical' defensins, beta-defensins and insect defensins.
T, Ganz, R I, Lehrer
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Planta, 2002
Plant defensins are small, basic peptides that have a characteristic three-dimensional folding pattern that is stabilized by eight disulfide-linked cysteines. They are termed plant defensins because they are structurally related to defensins found in other types of organism, including humans.
Bart P H J, Thomma +2 more
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Plant defensins are small, basic peptides that have a characteristic three-dimensional folding pattern that is stabilized by eight disulfide-linked cysteines. They are termed plant defensins because they are structurally related to defensins found in other types of organism, including humans.
Bart P H J, Thomma +2 more
openaire +2 more sources
Journal of Molecular Medicine, 2005
Antimicrobial peptides are small, cationic, amphiphilic peptides of 12-50 amino acids with microbicidal activity against both bacteria and fungi. The eukaryotic antimicrobial peptides may be divided into four distinct groups according to their structural features: cysteine-free alpha-helices, extended cysteine-free alpha-helices with a predominance of ...
Josef Johann, Schneider +4 more
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Antimicrobial peptides are small, cationic, amphiphilic peptides of 12-50 amino acids with microbicidal activity against both bacteria and fungi. The eukaryotic antimicrobial peptides may be divided into four distinct groups according to their structural features: cysteine-free alpha-helices, extended cysteine-free alpha-helices with a predominance of ...
Josef Johann, Schneider +4 more
openaire +2 more sources
Defensinpred: Defensin and Defensin Types Prediction Server
Protein & Peptide Letters, 2012Defensins are considered to play an important role in the innate immune system of virtually all life forms, from insects and plants to amphibians and mammals. They are classified into alpha, beta and theta-defensins. Fast and accurate computational prediction of defensin and defensin types will help in annotating unidentified defensin novel peptides ...
S Ramya, Kumari +3 more
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Nature Reviews Microbiology, 2004
Defensins are endogenous, cysteine-rich antimicrobial peptides that contribute to host defence against bacterial, fungal and viral infections. There are three subfamilies of defensins in primates: alpha-defensins are most common in neutrophils and Paneth cells of the small intestine; beta-defensins protect the skin and the mucous membranes of the ...
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Defensins are endogenous, cysteine-rich antimicrobial peptides that contribute to host defence against bacterial, fungal and viral infections. There are three subfamilies of defensins in primates: alpha-defensins are most common in neutrophils and Paneth cells of the small intestine; beta-defensins protect the skin and the mucous membranes of the ...
openaire +2 more sources