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Pesquisa : D08.811.277.352.100.680.750.937.750.100.500 [Categoria DeCS]
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  1 / 6 MEDLINE  
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[PMID]:23370290
[Au] Autor:Yagami T; Yamamoto Y; Kohma H; Nakamura T; Takasu N; Okamura N
[Ad] Endereço:Faculty of Pharmaceutical Sciences, Himeji Dokkyo University, 2-1, kami-ohno 7-Chome, Himeji, Hyogo 670-8524, Japan. yagami@himeji-du.ac.jp
[Ti] Título:L-type voltage-dependent calcium channel is involved in the snake venom group IA secretory phospholipase A2-induced neuronal apoptosis.
[So] Source:Neurotoxicology;35:146-53, 2013 Mar.
[Is] ISSN:1872-9711
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Snake venom group IA secretory phospholipase A2 (sPLA2-IA) is known as a neurotoxin. Snake venom sPLA2s are neurotoxic in vivo and in vitro, causing synergistic neurotoxicity to cortical cultures when applied with toxic concentrations of glutamate. However, it has not yet been cleared sufficiently how sPLA2-IA exerts neurotoxicity. Here, we found sPLA2-IA induced neuronal cell death in a concentration-dependent manner. This death was a delayed response requiring a latent time for 6h. sPLA2-IA-induced neuronal cell death was accompanied with apoptotic blebbing, condensed chromatin, and fragmented DNA, exhibiting apoptotic features. NMDA receptor blockers suppressed the neurotoxicity of sPLA2-IA, but an AMPA receptor blocker did not. Interestingly, L-type voltage-dependent Ca(2+) channel (L-VDCC) blocker significantly protected neurons from the sPLA2-IA-induced apoptosis. On the other hand, neither N-VDCC blockers nor P/Q-VDCC blocker did. In conclusion, we demonstrated that sPLA2-IA induced neuronal cell death via apoptosis. Furthermore, the present study suggests that not only NMDA receptor but also L-VDCC contributed to the neurotoxicity of snake venom sPLA2-IA.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Canais de Cálcio Tipo L/efeitos dos fármacos
Córtex Cerebral/efeitos dos fármacos
Venenos Elapídicos/toxicidade
Fosfolipases A2 do Grupo IA/toxicidade
Neurônios/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Bloqueadores dos Canais de Cálcio/farmacologia
Canais de Cálcio Tipo L/metabolismo
Células Cultivadas
Córtex Cerebral/embriologia
Córtex Cerebral/metabolismo
Córtex Cerebral/ultraestrutura
Montagem e Desmontagem da Cromatina/efeitos dos fármacos
Fragmentação do DNA
Relação Dose-Resposta a Droga
Venenos Elapídicos/enzimologia
Antagonistas de Aminoácidos Excitatórios/farmacologia
Neurônios/metabolismo
Neurônios/ultraestrutura
Fármacos Neuroprotetores/farmacologia
Ratos
Ratos Sprague-Dawley
Receptores de N-Metil-D-Aspartato/efeitos dos fármacos
Receptores de N-Metil-D-Aspartato/metabolismo
Transdução de Sinais/efeitos dos fármacos
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcium Channel Blockers); 0 (Calcium Channels, L-Type); 0 (Elapid Venoms); 0 (Excitatory Amino Acid Antagonists); 0 (Neuroprotective Agents); 0 (Receptors, N-Methyl-D-Aspartate); EC 3.1.1.4 (Group IA Phospholipases A2)
[Em] Mês de entrada:1309
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130202
[St] Status:MEDLINE


  2 / 6 MEDLINE  
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[PMID]:22037357
[Au] Autor:Hite RD; Grier BL; Waite BM; Veldhuizen RA; Possmayer F; Yao LJ; Seeds MC
[Ad] Endereço:Section Head-Pulmonary, Critical Care, Allergy and Immunologic Diseases, Wake Forest University School of Medicine, 1 Medical Ctr. Blvd., Winston-Salem, NC 27157-1054, USA. dhite@wfubmc.edu
[Ti] Título:Surfactant protein B inhibits secretory phospholipase A2 hydrolysis of surfactant phospholipids.
[So] Source:Am J Physiol Lung Cell Mol Physiol;302(2):L257-65, 2012 Jan 15.
[Is] ISSN:1522-1504
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hydrolysis of surfactant phospholipids (PL) by secretory phospholipases A(2) (sPLA(2)) contributes to surfactant damage in inflammatory airway diseases such as acute lung injury/acute respiratory distress syndrome. We and others have reported that each sPLA(2) exhibits specificity in hydrolyzing different PLs in pulmonary surfactant and that the presence of hydrophilic surfactant protein A (SP-A) alters sPLA(2)-mediated hydrolysis. This report tests the hypothesis that hydrophobic SP-B also inhibits sPLA(2)-mediated surfactant hydrolysis. Three surfactant preparations were used containing varied amounts of SP-B and radiolabeled tracers of phosphatidylcholine (PC) or phosphatidylglycerol (PG): 1) washed ovine surfactant (OS) (pre- and postorganic extraction) compared with Survanta (protein poor), 2) Survanta supplemented with purified bovine SP-B (1-5%, wt/wt), and 3) a mixture of dipalmitoylphosphatidylcholine (DPPC), 1-palmitoyl-2-oleoyl-phosphatidylcholine (POPC), and 1-palmitoyl-2-oleoyl-phosphatidylglycerol (POPG) (DPPC:POPC:POPG, 40:40:20) prepared as vesicles and monomolecular films in the presence or absence of SP-B. Hydrolysis of PG and PC by Group IB sPLA(2) (PLA2G1A) was significantly lower in the extracted OS, which contains SP-B, compared with Survanta (P = 0.005), which is SP-B poor. Hydrolysis of PG and PC in nonextracted OS, which contains all SPs, was lower than both Survanta and extracted OS. When Survanta was supplemented with 1% SP-B, PG and PC hydrolysis by PLA2G1B was significantly lower (P < 0.001) than in Survanta alone. When supplemented into pure lipid vesicles and monomolecular films composed of PG and PC mixtures, SP-B also inhibited hydrolysis by both PLA2G1B and Group IIA sPLA2 (PLA2G2A). In films, PLA2G1B hydrolyzed surfactant PL monolayers at surface pressures ≤30 mN/m (P < 0.01), and SP-B lowered the surface pressure range at which hydrolysis can occur. These results suggest the hydrophobic SP, SP-B, protects alveolar surfactant PL from hydrolysis mediated by multiple sPLA(2) in both vesicles (alveolar subphase) and monomolecular films (air-liquid interface).
[Mh] Termos MeSH primário: Fosfolipases A2 do Grupo IA/metabolismo
Fosfolipases A2 do Grupo IB/metabolismo
Fosfolipídeos/metabolismo
Proteína B Associada a Surfactante Pulmonar/metabolismo
Surfactantes Pulmonares/metabolismo
[Mh] Termos MeSH secundário: Lesão Pulmonar Aguda/metabolismo
Lesão Pulmonar Aguda/patologia
Animais
Bovinos
Hidrólise
Interações Hidrofóbicas e Hidrofílicas
Fosfatidilcolinas/metabolismo
Fosfatidilgliceróis/metabolismo
Proteína A Associada a Surfactante Pulmonar/metabolismo
Surfactantes Pulmonares/química
Síndrome do Desconforto Respiratório do Adulto/patologia
Ovinos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Phosphatidylcholines); 0 (Phosphatidylglycerols); 0 (Phospholipids); 0 (Pulmonary Surfactant-Associated Protein A); 0 (Pulmonary Surfactant-Associated Protein B); 0 (Pulmonary Surfactants); EC 3.1.1.4 (Group IA Phospholipases A2); EC 3.1.1.4 (Group IB Phospholipases A2)
[Em] Mês de entrada:1202
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:111101
[St] Status:MEDLINE
[do] DOI:10.1152/ajplung.00054.2011


  3 / 6 MEDLINE  
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[PMID]:19439980
[Au] Autor:Triggiani M; Granata F; Petraroli A; Loffredo S; Frattini A; Staiano RI; Monaco G; Marone G
[Ad] Endereço:Department of Clinical Immunology and Allergy and Center for Basic and Clinical Immunology Research (CISI), University of Naples Federico II, Naples, Italy. triggian@unina.it
[Ti] Título:Inhibition of secretory phospholipase A2-induced cytokine production in human lung macrophages by budesonide.
[So] Source:Int Arch Allergy Immunol;150(2):144-55, 2009.
[Is] ISSN:1423-0097
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Secretory phospholipases A(2) (sPLA(2)) are an emerging class of mediators of inflammation. These enzymes are released in vivo in patients with systemic inflammatory diseases and allergic disorders. sPLA(2)s may activate inflammatory cells by both enzymatic and nonenzymatic mechanisms. The aim of this study was to evaluate the effect of the inhaled glucocorticoid budesonide on sPLA(2)-induced activation of primary human macrophages. METHODS: Macrophages isolated from human lung tissue were preincubated (3-18 h) with budesonide (1-1,000 nM) before stimulation with 2 distinct sPLA(2)s (group IA and group X). At the end of incubation the release of TNF-alpha, IL-6 and IL-8 was assessed by ELISA. Specific mRNA for these products was determined by quantitative RT-PCR. Activation of mitogen-activated kinases ERK 1/2 and p38 was assessed by Western blot. RESULTS: Budesonide inhibited the release of TNF-alpha, IL-6 and IL-8 from sPLA(2)-stimulated macrophages in a concentration-dependent manner. The inhibitory effect of budesonide was due to a reduction of gene expression and was complete after 18 h of preincubation. Budesonide had no effect on sPLA(2)-induced arachidonic acid mobilization and exocytosis, assessed as beta-glucuronidase release. Suppression of cytokine/chemokine production by budesonide was associated with inhibition of sPLA(2)-induced ERK 1/2 and p38 activation. CONCLUSIONS: Budesonide inhibits the production of proinflammatory cytokines/chemokines from human lung macrophages activated by sPLA(2). Budesonide represents the first example of a drug able to block the nonenzymatic effects of sPLA(2) on human inflammatory cells and, therefore, may provide a useful therapeutic options for diseases associated with enhanced release of sPLA(2)s in vivo.
[Mh] Termos MeSH primário: Budesonida/farmacologia
Citocinas/biossíntese
Macrófagos Alveolares/efeitos dos fármacos
Macrófagos Alveolares/metabolismo
Fosfolipases A2 Secretórias/farmacologia
[Mh] Termos MeSH secundário: Ácido Araquidônico/metabolismo
Cicloeximida/farmacologia
Citocinas/genética
Dactinomicina/farmacologia
Expressão Gênica/efeitos dos fármacos
Expressão Gênica/genética
Glucuronidase/metabolismo
Fosfolipases A2 do Grupo IA/farmacologia
Fosfolipases A2 do Grupo X/farmacologia
Seres Humanos
Interleucina-6/genética
Interleucina-6/metabolismo
Interleucina-8/genética
Interleucina-8/metabolismo
Proteína Quinase 1 Ativada por Mitógeno/antagonistas & inibidores
Proteína Quinase 1 Ativada por Mitógeno/metabolismo
Proteína Quinase 3 Ativada por Mitógeno/antagonistas & inibidores
Proteína Quinase 3 Ativada por Mitógeno/metabolismo
Fosforilação/efeitos dos fármacos
Inibidores de Proteínas Quinases/farmacologia
Transdução de Sinais/efeitos dos fármacos
Transdução de Sinais/fisiologia
Fator de Necrose Tumoral alfa/genética
Fator de Necrose Tumoral alfa/metabolismo
Proteínas Quinases p38 Ativadas por Mitógeno/antagonistas & inibidores
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytokines); 0 (IL6 protein, human); 0 (Interleukin-6); 0 (Interleukin-8); 0 (Protein Kinase Inhibitors); 0 (Tumor Necrosis Factor-alpha); 1CC1JFE158 (Dactinomycin); 27YG812J1I (Arachidonic Acid); 51333-22-3 (Budesonide); 98600C0908 (Cycloheximide); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); EC 3.1.1.4 (Group IA Phospholipases A2); EC 3.1.1.4 (Group X Phospholipases A2); EC 3.1.1.4 (Phospholipases A2, Secretory); EC 3.2.1.31 (Glucuronidase)
[Em] Mês de entrada:0910
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090515
[St] Status:MEDLINE
[do] DOI:10.1159/000218117


  4 / 6 MEDLINE  
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[PMID]:18931897
[Au] Autor:Burke JE; Dennis EA
[Ad] Endereço:Department of Chemistry and Biochemistry, School of Medicine, University of California, La Jolla, San Diego, CA 92093-0601, USA.
[Ti] Título:Phospholipase A2 biochemistry.
[So] Source:Cardiovasc Drugs Ther;23(1):49-59, 2009 Feb.
[Is] ISSN:1573-7241
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The phospholipase A(2) (PLA(2)) superfamily consists of many different groups of enzymes that catalyze the hydrolysis of the sn-2 ester bond in a variety of different phospholipids. The products of this reaction, a free fatty acid, and lysophospholipid have many different important physiological roles. There are five main types of PLA(2): the secreted sPLA(2)'s, the cytosolic cPLA(2)'s, the Ca(2+)independent iPLA(2)'s, the PAF acetylhydrolases, and the lysosomal PLA(2)'s. This review focuses on the superfamily of PLA(2) enzymes, and then uses three specific examples of these enzymes to examine the differing biochemistry of the three main types of these enzymes. These three examples are the GIA cobra venom PLA(2), the GIVA cytosolic cPLA(2), and the GVIA Ca(2+)-independent iPLA(2).
[Mh] Termos MeSH primário: Ácidos Graxos não Esterificados/metabolismo
Lisofosfolipídeos/metabolismo
Fosfolipases A2/metabolismo
[Mh] Termos MeSH secundário: Animais
Venenos Elapídicos/enzimologia
Fosfolipases A2 do Grupo IA/metabolismo
Fosfolipases A2 do Grupo IV/metabolismo
Fosfolipases A2 do Grupo VI/metabolismo
Seres Humanos
Isoenzimas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
0 (Elapid Venoms); 0 (Fatty Acids, Nonesterified); 0 (Isoenzymes); 0 (Lysophospholipids); EC 3.1.1.4 (Group IA Phospholipases A2); EC 3.1.1.4 (Group IV Phospholipases A2); EC 3.1.1.4 (Group VI Phospholipases A2); EC 3.1.1.4 (Phospholipases A2)
[Em] Mês de entrada:0903
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:081022
[St] Status:MEDLINE
[do] DOI:10.1007/s10557-008-6132-9


  5 / 6 MEDLINE  
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[PMID]:18500818
[Au] Autor:Burke JE; Karbarz MJ; Deems RA; Li S; Woods VL; Dennis EA
[Ad] Endereço:Department of Chemistry and Biochemistry, School of Medicine, University of California at San Diego, La Jolla, California 92093-0601, USA.
[Ti] Título:Interaction of group IA phospholipase A2 with metal ions and phospholipid vesicles probed with deuterium exchange mass spectrometry.
[So] Source:Biochemistry;47(24):6451-9, 2008 Jun 17.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Deuterium exchange mass spectrometric evaluation of the cobra venom (Naja naja naja) group IA phospholipase A 2 (GIA PLA 2) was carried out in the presence of metal ions Ca (2+) and Ba (2+) and phospholipid vesicles. Novel conditions for digesting highly disulfide bonded proteins and a methodology for studying protein-lipid interactions using deuterium exchange have been developed. The enzyme exhibits unexpectedly slow rates of exchange in the two large alpha-helices of residues 43-53 and 89-101, which suggests that these alpha-helices are highly rigidified by the four disulfide bonds in this region. The binding of Ca (2+) or Ba (2+) ions decreased the deuterium exchange rates for five regions of the protein (residues 24-27, 29-40, 43-53, 103-110, and 111-114). The magnitude of the changes was the same for both ions with the exception of regions of residues 24-27 and 103-110 which showed greater changes for Ca (2+). The crystal structure of the N. naja naja GIA PLA 2 contains a single Ca (2+) bound in the catalytic site, but the crystal structures of related PLA 2s contain a second Ca (2+) binding site. The deuterium exchange studies reported here clearly show that in solution the GIA PLA 2 does in fact bind two Ca (2+) ions. With dimyristoylphosphatidylcholine (DMPC) phospholipid vesicles with 100 microM Ca (2+) present at 0 degrees C, significant areas on the i-face of the enzyme showed decreases in the rate of exchange. These areas included regions of residues 3-8, 18-21, and 56-64 which include Tyr-3, Trp-61, Tyr-63, and Phe-64 proposed to penetrate the membrane surface. These regions also contained Phe-5 and Trp-19, proposed to bind the fatty acyl tails of substrate.
[Mh] Termos MeSH primário: Bário/química
Cálcio/química
Venenos Elapídicos/enzimologia
Fosfolipases A2 do Grupo IA/química
Fosfolipídeos/química
Espectrometria de Massas em Tandem
Lipossomas Unilamelares/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Bário/metabolismo
Cálcio/metabolismo
Cátions Bivalentes/metabolismo
Medição da Troca de Deutério
Fosfolipases A2 do Grupo IA/metabolismo
Dados de Sequência Molecular
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/metabolismo
Mapeamento de Peptídeos
Fosfolipídeos/metabolismo
Ligação Proteica
Espectrometria de Massas em Tandem/métodos
Lipossomas Unilamelares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Cations, Divalent); 0 (Elapid Venoms); 0 (Peptide Fragments); 0 (Phospholipids); 0 (Unilamellar Liposomes); 24GP945V5T (Barium); EC 3.1.1.4 (Group IA Phospholipases A2); SY7Q814VUP (Calcium)
[Em] Mês de entrada:0807
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:080527
[St] Status:MEDLINE
[do] DOI:10.1021/bi8000962


  6 / 6 MEDLINE  
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[PMID]:10700385
[Au] Autor:Singh SB; Armugam A; Kini RM; Jeyaseelan K
[Ad] Endereço:Department of Biochemistry, National University of Singapore, 10 Medical Drive, Singapore, 119260.
[Ti] Título:Phospholipase A(2) with platelet aggregation inhibitor activity from Austrelaps superbus venom: protein purification and cDNA cloning.
[So] Source:Arch Biochem Biophys;375(2):289-303, 2000 Mar 15.
[Is] ISSN:0003-9861
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Four phospholipase A(2) (PLA(2)) enzymes (Superbins a, b, c, and d) with varying platelet aggregation inhibitor activities have been purified from Austrelaps superbus by a combination of gel filtration, ion-exchange, and reversed-phase high-pressure liquid chromatography. Purity and homogeneity of the superbins have been confirmed by high-performance capillary zone electrophoresis and mass spectrometry. The electron spray ionization mass spectrometry data showed that their molecular masses range from 13,140 to 13,236 Da. Each of the proteins has been found to be basic and exhibit varying degrees of PLA(2) activity. They also displayed different platelet aggregation inhibitory activities. Superbin a was found to possess the most potent inhibitory activity with an IC(50) of 9.0 nM, whereas Superbin d was found to be least effective with an IC(50) of 3.0 microM. Superbins b and c were moderately effective with IC(50) values of 0.05 and 0.5 microM, respectively. The amino-terminal sequencing confirmed the identity of these superbins. cDNA cloning resulted in the identification of 17 more PLA(2) isoforms in A. superbus venom. It has also provided complete information on the precursor PLA(2). The precursor PLA(2) contained a 27-amino-acid signal peptide and 117- to 125-amino-acid PLA(2) (molecular mass ranging from 13,000 to 14,000 Da). Two of these PLA(2) enzymes resembled more closely (87%) Superbin a in structure. Two unique PLA(2) enzymes containing an extra pancreatic loop also have been identified among the isoforms.
[Mh] Termos MeSH primário: Agkistrodon/genética
Venenos Elapídicos/enzimologia
Isoenzimas/genética
Isoenzimas/isolamento & purificação
Fosfolipases A/genética
Fosfolipases A/isolamento & purificação
Inibidores da Agregação de Plaquetas/isolamento & purificação
Inibidores da Agregação de Plaquetas/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Austrália
Sequência de Bases
Plaquetas/efeitos dos fármacos
Plaquetas/fisiologia
Clonagem Molecular
Sequência Consenso/genética
DNA Complementar/genética
Venenos Elapídicos/genética
Fosfolipases A2 do Grupo IA
Seres Humanos
Concentração Inibidora 50
Ponto Isoelétrico
Isoenzimas/química
Isoenzimas/metabolismo
Espectrometria de Massas
Dados de Sequência Molecular
Peso Molecular
Fosfolipases A/química
Fosfolipases A/metabolismo
Agregação Plaquetária/efeitos dos fármacos
Inibidores da Agregação de Plaquetas/química
Inibidores da Agregação de Plaquetas/farmacologia
Precursores de Proteínas/química
Precursores de Proteínas/genética
Precursores de Proteínas/isolamento & purificação
Precursores de Proteínas/metabolismo
Sinais Direcionadores de Proteínas/química
Sinais Direcionadores de Proteínas/genética
Proteínas de Répteis
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Complementary); 0 (Elapid Venoms); 0 (Isoenzymes); 0 (Platelet Aggregation Inhibitors); 0 (Protein Precursors); 0 (Protein Sorting Signals); 0 (Reptilian Proteins); EC 3.1.1.32 (Phospholipases A); EC 3.1.1.4 (Group IA Phospholipases A2); EC 3.1.1.4 (superbin)
[Em] Mês de entrada:0004
[Cu] Atualização por classe:161124
[Lr] Data última revisão:
161124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:000304
[St] Status:MEDLINE



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