Outer membrane protein I of pseudomonas aeruginosa is a target of cationic antimicrobial peptide/protein

Journal of Biological Chemistry

Volumn 285, Issue 12, 2010, Pages 8985-8994

  Lin, Yu Min ^a,b   Wu, Shih Jung ^a,c   Chang, Ting Wei ^a,d   Wang, Chiu Feng ^a   Suen, Ching Shu ^a   Hwang, Ming Jing ^a   Chang, Margaret Dah Tsyr ^b   Chen, Yuan Tsong ^a,c   Liao, You Di ^a,d  

^a INSTITUTE OF BIOMEDICAL SCIENCES   (Taiwan)

^b NATIONAL TSING HUA UNIVERSITY   (Taiwan)

^c NATIONAL TAIWAN UNIVERSITY   (Taiwan)

^d NATIONAL YANG MING UNIVERSITY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

ANTI-MICROBIAL ACTIVITY; BACTERIAL INFECTIONS; BACTERIAL MEMBRANES; C TERMINUS; CELL WALLS; CYTOSOLS; INNATE DEFENSE; LIPOPOLYSACCHARIDES; LYSINE RESIDUES; OUTER MEMBRANE PROTEIN; P.AERUGINOSA; PSEUDOMONAS AERUGINOSA;

AMINO ACIDS; BACTERIA; BACTERIOLOGY; BINDING ENERGY; BIOLOGICAL MEMBRANES;

PROTEINS;

OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN I; POLYPEPTIDE ANTIBIOTIC AGENT; RIBONUCLEASE; RIBONUCLEASE 7; UNCLASSIFIED DRUG; ANTIMICROBIAL CATIONIC PEPTIDE; CROSS LINKING REAGENT; LIPOPOLYSACCHARIDE; LIPOPROTEIN; POLYMER;

AMINO TERMINAL SEQUENCE; ANTIMICROBIAL ACTIVITY; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ESCHERICHIA COLI; INTERNALIZATION; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN MODIFICATION; PROTEIN PURIFICATION; PSEUDOMONAS AERUGINOSA; BIOLOGICAL MODEL; CELL MEMBRANE; CELL WALL; CHEMISTRY; CYTOSOL; HUMAN; METABOLISM; MOLECULAR CLONING; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE;

BACTERIA (MICROORGANISMS); PSEUDOMONAS AERUGINOSA;

ANTIMICROBIAL CATIONIC PEPTIDES; CELL MEMBRANE; CELL WALL; CLONING, MOLECULAR; CROSS-LINKING REAGENTS; CYTOSOL; ESCHERICHIA COLI; HUMANS; LIPOPOLYSACCHARIDES; LIPOPROTEINS; MODELS, BIOLOGICAL; POLYMERS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PSEUDOMONAS AERUGINOSA;

EID: 77950563502     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.078725     Document Type: Article

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