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Trends in Pharmacological Sciences, ISSN 0165-6147, 2003, Volume 24, Issue 3, pp. 103 - 106
Journal Article
Journal Article
TOXICON, ISSN 0041-0101, 09/2018, Volume 151, pp. 1 - 4
Snake venom phospholipase A(2)(PLA(2)) has widely been reported to possess antibacterial effects, PLA(2) is the major component of cottonmouth snake venoms. We... 
MAJOR PHYSIOLOGICAL-ROLE | ESCHERICHIA-COLI | CELL WALL | PENETRATION | Phospholipase A | STRUCTURAL DETERMINANTS | Cottonmouth snake venom | AMINO-ACID-SEQUENCE | AGKISTRODON | PURIFICATION | Antibacterial activity | BOTHROPS-ASPER | PHARMACOLOGY & PHARMACY | TOXICOLOGY | PISCIVORUS
Journal Article
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS, ISSN 1388-1981, 06/2019, Volume 1864, Issue 6, pp. 789 - 802
Among all members of the secreted phospholipase A(2) (sPLA(2)) family, group IIA sPLA(2) (sPLA(2)-IIA) is possibly the most studied enzyme. Since its... 
ARACHIDONIC-ACID RELEASE | MAJOR PHYSIOLOGICAL-ROLE | GROUP-X | BIOCHEMISTRY & MOLECULAR BIOLOGY | Inflammation | FACTOR-KAPPA-B | MITOCHONDRIAL-DNA | HUMAN T-CELLS | CELL BIOLOGY | Secreted phospholipase A | Infectious diseases | BIOPHYSICS | SMOOTH-MUSCLE-CELLS | STAPHYLOCOCCUS-AUREUS | KRUPPEL-LIKE FACTOR-2 | Platelets | CELL-MEMBRANE HYDROLYSIS | Microbiome
Journal Article
Journal Article
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, ISSN 0003-9861, 03/2012, Volume 519, Issue 1, pp. 17 - 22
Suramin is a polysulphonated naphthylurea with inhibitory activity against the human secreted group IIA phospholipase A(2) (hsPLA2GIIA), and we have... 
MAJOR PHYSIOLOGICAL-ROLE | PLA inhibitor | ANALOGS | BIOCHEMISTRY & MOLECULAR BIOLOGY | PENETRATION | PHASE | ENZYME | BIOPHYSICS | Drug design | INHIBITORS | ELECTROSTATICS | Protein-drug binding | EXPRESSION | BACTERIAL-CELL WALL
Journal Article
BIOCHIMIE, ISSN 0300-9084, 01/2012, Volume 94, Issue 1, pp. 132 - 136
The Human Secreted Group IIA Phospholipase A(2) (hsPIA2GIIA) presents potent bactericidal activity, and is considered to contribute to the acute-phase immune... 
MAJOR PHYSIOLOGICAL-ROLE | VENOM | ACTIVATION | H48Q | BIOCHEMISTRY & MOLECULAR BIOLOGY | Active site mutant | ANTIBACTERIAL PROPERTIES | INCLUSION-BODIES | LYS49 | Membrane damage | PORCINE PANCREATIC PHOSPHOLIPASE-A2 | PURIFICATION | Ca2+-independent
Journal Article
Russian Journal of Genetics, ISSN 1022-7954, 02/2003, Volume 39, Issue 2, pp. 152 - 158
The data on the regulation of expression and on the biological role of the tumor necrosis factor and lymphotoxin in the author's laboratory, are briefly... 
Human Genetics | Biomedicine | DEPENDENT DIABETES-MELLITUS | TRANSCRIPTIONAL ACTIVATION | HUMAN GENOME | BETA-GENE | FACTOR TNF-ALPHA | GENETICS & HEREDITY | FACTOR-ALPHA GENE | TANDEM ARRANGEMENT | MAJOR HISTOCOMPATIBILITY COMPLEX | DEFICIENT MICE | EXPRESSION
Journal Article
Genetika, ISSN 0016-6758, 02/2003, Volume 39, Issue 2, p. 207
Journal Article
INVESTIGATIVE OPHTHALMOLOGY & VISUAL SCIENCE, ISSN 0146-0404, 09/2004, Volume 45, Issue 9, pp. 3161 - 3164
PURPOSE. Secretory phospholipase A(2) (sPLA(2)) is a potent antibacterial enzyme in tears and has been found to kill Staphylococcus aureus rapidly in vitro.... 
MAJOR PHYSIOLOGICAL-ROLE | WEARERS | PROTEIN | LACRIMAL GLANDS | CELL WALL | OPHTHALMOLOGY | PENETRATION | STAPHYLOCOCCUS-AUREUS | GROUP-IIA PHOSPHOLIPASE-A2 | HUMAN TEAR FLUID
Journal Article
BIOORGANIC CHEMISTRY, ISSN 0045-2068, 02/2009, Volume 37, Issue 1-3, pp. 41 - 45
Suramin is a polysulphonated napthylurea used as an antiprotozoal/anthelminitic drug, which also inhibits a broad range of enzymes. Suramin binding to... 
MAJOR PHYSIOLOGICAL-ROLE | GROUP-V | GROUP-X | BOTHROPSTOXIN-I | BIOCHEMISTRY & MOLECULAR BIOLOGY | Molecular dynamics | HYDROLYSIS | CHEMISTRY, ORGANIC | BACTERICIDAL PROPERTIES | PENETRATION | Isothermal titration calorimetry | INHIBITORS
Journal Article
BBA - Molecular and Cell Biology of Lipids, ISSN 1388-1981, 2006, Volume 1761, Issue 11, pp. 1270 - 1279
Journal Article
EUROPEAN JOURNAL OF LIPID SCIENCE AND TECHNOLOGY, ISSN 1438-7697, 03/2005, Volume 107, Issue 3, pp. 193 - 205
Phospholipases A(2) (PLA(2)) are an example of peripheral membrane proteins that must first bind to the phospholipid interface to allow phospholipid hydrolysis... 
ARACHIDONIC-ACID RELEASE | MAJOR PHYSIOLOGICAL-ROLE | GROUP-V | GROUP-X | FOOD SCIENCE & TECHNOLOGY | A C2 DOMAIN | apoptesis | HUMAN GROUP-IIA | HUMAN T-CELLS | NUTRITION & DIETETICS | inflammation | INTERFACIAL BINDING SURFACE | lipid signalling | antilacteral protein | WEIGHT GROUP IIA | membrane binding | BACTERIAL-CELL WALL
Journal Article