ATP synthase: A molecular therapeutic drug target for antimicrobial and antitumor peptides

Current Medicinal Chemistry

Volumn 20, Issue 15, 2013, Pages 1956-1973

  Ahmad, Zulfiqar ^a   Okafor, Florence ^a   Azim, Sofiya ^b   Laughlin, Thomas F ^b  

^a ALABAMA A AND M UNIVERSITY   (United States)

^b EAST TENNESSEE STATE UNIVERSITY   (United States)

Author keywords

Antimicrobial peptides; Antitumor peptides; ATPase; E. coli ATP synthase; Enzyme inhibitors; F1Fo ATP synthase

Indexed keywords

4 CHLORO 7 NITROBENZOFURAZAN; ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALUMINUM FLUORIDE; ANGIOSTATIN; ANTIBIOTIC AGENT; ANTINEOPLASTIC AGENT; ANTIOBESITY AGENT; AUROVERTIN; BERYLLIUM FLUORIDE; DIARYLQUINOLINE; EFRAPEPTIN; EPICATECHIN; LEUCINOSTATIN DERIVATIVE; MORIN; OLIGOMYCIN; PEPTIDE DERIVATIVE; PHENOL DERIVATIVE; PICEATANNOL; POLYPEPTIDE ANTIBIOTIC AGENT; POLYPHENOL DERIVATIVE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE INHIBITOR; QUERCETIN; QUINOLINE DERIVATIVE; RESVERATROL; SCANDIUM FLUORIDE; SODIUM AZIDE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

ALZHEIMER DISEASE; ANGIOGENESIS; ANTIBACTERIAL ACTIVITY; ANTIINFLAMMATORY ACTIVITY; ANTIMALARIAL ACTIVITY; ANTIMICROBIAL ACTIVITY; ANTINEOPLASTIC ACTIVITY; APOPTOSIS; BACTERIAL INFECTION; BACTERIAL STRAIN; CANCER CELL; CATALYSIS; CELL PROLIFERATION; CELL TYPE; CYTOTOXICITY; DRUG BINDING SITE; DRUG INHIBITION; DRUG SYNTHESIS; ENZYME INHIBITION; ENZYME SUBSTRATE; ENZYME SYNTHESIS; ESCHERICHIA COLI; HUMAN; IMMUNOMODULATION; METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS; MITOCHONDRION; MOLECULARLY TARGETED THERAPY; NANOMOTOR; NONHUMAN; PROTEIN FUNCTION; REVIEW; STREPTOCOCCUS MUTANS; X RAY CRYSTALLOGRAPHY;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; ANIMALS; ANTI-INFECTIVE AGENTS; ANTINEOPLASTIC AGENTS; BACTERIA; BACTERIAL INFECTIONS; ENZYME INHIBITORS; FUNGI; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR TARGETED THERAPY; MYCOSES; NEOPLASMS; PEPTIDES; VIRUS DISEASES; VIRUSES;

EID: 84877982999     PISSN: 09298673     EISSN: 1875533X     Source Type: Journal    
DOI: 10.2174/0929867311320150003     Document Type: Review

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