PMAP-37, a novel antibacterial peptide from pig myeloid cells. cDNA cloning, chemical synthesis and activity.
about
Activity of protegrins against yeast-phase Candida albicansStructure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surfaceAntiviral potential of cathelicidinsCathelicidins: family of antimicrobial peptides. A reviewAntimicrobial peptides as mediators of epithelial host defense.The role of protegrins and other elastase-activated polypeptides in the bactericidal properties of porcine inflammatory fluids.Structural and functional analysis of horse cathelicidin peptides.RL-37, an alpha-helical antimicrobial peptide of the rhesus monkey.Purification and properties of proline-rich antimicrobial peptides from sheep and goat leukocytesThe structure of porcine protegrin genes.The role of defensins in lung biology and therapy.Genome wide analysis of the antimicrobial peptides in Python bivittatus and characterization of cathelicidins with potent antimicrobial activity and low cytotoxicity.The porcine lung as a potential model for cystic fibrosisStructures of genes for two cathelin-associated antimicrobial peptides: prophenin-2 and PR-39.Heparan sulfate proteoglycan-dependent neutrophil chemotaxis toward PR-39 cathelicidin.Structure and organization of the human antimicrobial peptide LL-37 in phospholipid membranes: relevance to the molecular basis for its non-cell-selective activity.Defining the genetic relationship of protegrin-related sequences and the in vivo expression of protegrins.Antibacterial activity of secretolytin, a chromogranin B-derived peptide (614-626), is correlated with peptide structure.The cathelicidin family of antimicrobial peptide precursors: a component of the oxygen-independent defense mechanisms of neutrophils.Biological characterization of two novel cathelicidin-derived peptides and identification of structural requirements for their antimicrobial and cell lytic activities.Molecular analysis of the sheep cathelin family reveals a novel antimicrobial peptide.cDNA sequences of three sheep myeloid cathelicidins.Solution structure of a cathelicidin-derived antimicrobial peptide, CRAMP as determined by NMR spectroscopy.SMAP-29: a potent antibacterial and antifungal peptide from sheep leukocytesCathelicidins: Immunomodulatory Antimicrobials
P2860
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P2860
PMAP-37, a novel antibacterial peptide from pig myeloid cells. cDNA cloning, chemical synthesis and activity.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
PMAP-37, a novel antibacterial ...... emical synthesis and activity.
@en
PMAP-37, a novel antibacterial ...... emical synthesis and activity.
@nl
type
label
PMAP-37, a novel antibacterial ...... emical synthesis and activity.
@en
PMAP-37, a novel antibacterial ...... emical synthesis and activity.
@nl
prefLabel
PMAP-37, a novel antibacterial ...... emical synthesis and activity.
@en
PMAP-37, a novel antibacterial ...... emical synthesis and activity.
@nl
P2093
P2860
P1433
P1476
PMAP-37, a novel antibacterial ...... emical synthesis and activity.
@en
P2093
P2860
P304
P356
10.1111/J.1432-1033.1995.TB20344.X
P407
P577
1995-03-01T00:00:00Z