Excitement ahead: structure, function and mechanism of snake venom phospholipase A2 enzymes.
about
Inventing an arsenal: adaptive evolution and neofunctionalization of snake venom phospholipase A2 genesSpider genomes provide insight into composition and evolution of venom and silkEffects of Animal Venoms and Toxins on Hallmarks of CancerBee Venom Phospholipase A2: Yesterday's Enemy Becomes Today's FriendMVL-PLA2, a snake venom phospholipase A2, inhibits angiogenesis through an increase in microtubule dynamics and disorganization of focal adhesionsStructural and Functional Studies of a Bothropic Myotoxin Complexed to Rosmarinic Acid: New Insights into Lys49-PLA2 InhibitionSnake Venom Cytotoxins, Phospholipase A2s, and Zn(2+)-dependent Metalloproteinases: Mechanisms of Action and Pharmacological RelevanceMolecular evolution of vertebrate neurotrophins: co-option of the highly conserved nerve growth factor gene into the advanced snake venom arsenalfFull-Length Venom Protein cDNA Sequences from Venom-Derived mRNA: Exploring Compositional Variation and Adaptive Multigene EvolutionA catalog for the transcripts from the venomous structures of the caterpillar Lonomia obliqua: identification of the proteins potentially involved in the coagulation disorder and hemorrhagic syndromeCharacterization of a human coagulation factor Xa-binding site on Viperidae snake venom phospholipases A2 by affinity binding studies and molecular bioinformatics.The Deep Origin and Recent Loss of Venom Toxin Genes in Rattlesnakes.Role of accelerated segment switch in exons to alter targeting (ASSET) in the molecular evolution of snake venom proteinsCC-PLA2-1 and CC-PLA2-2, two Cerastes cerastes venom-derived phospholipases A2, inhibit angiogenesis both in vitro and in vivo.Neurotoxicity and other pharmacological activities of the snake venom phospholipase A2 OS2: the N-terminal region is more important than enzymatic activity.cDNA and deduced primary structure of basic phospholipase A2 with neurotoxic activity from the venom secretion of the Crotalus durissus collilineatus rattlesnake.Ascorbate ameliorates Echis coloratus venom-induced oxidative stress in human fibroblastsAntivenomic assessment of the immunological reactivity of EchiTAb-Plus-ICP, an antivenom for the treatment of snakebite envenoming in sub-Saharan AfricaA novel protein from the serum of Python sebae, structurally homologous with type-γ phospholipase A(2) inhibitor, displays antitumour activity.Sphingomyelinase D activity in model membranes: structural effects of in situ generation of ceramide-1-phosphateSynergism between basic Asp49 and Lys49 phospholipase A2 myotoxins of viperid snake venom in vitro and in vivo.Restriction and recruitment-gene duplication and the origin and evolution of snake venom toxins.Differential myotoxic and cytotoxic activities of pre-synaptic neurotoxins from Papuan taipan (Oxyuranus scutellatus) and Irian Jayan death adder (Acanthophis rugosus) venoms.Anticoagulant proteins from snake venoms: structure, function and mechanismPhTX-II a basic myotoxic phospholipase A₂ from Porthidium hyoprora snake venom, pharmacological characterization and amino acid sequence by mass spectrometry.Biochemical characterization and pharmacological properties of new basic PLA2 BrTX-I isolated from Bothrops roedingeri (Roedinger's Lancehead) Mertens, 1942, snake venom.A novel anti-inflammatory role for secretory phospholipase A2 in immune complex-mediated arthritis.The genesis of an exceptionally lethal venom in the timber rattlesnake (Crotalus horridus) revealed through comparative venom-gland transcriptomics.Phospholipase A2 isolated from the venom of Crotalus durissus terrificus inactivates dengue virus and other enveloped viruses by disrupting the viral envelope.Inhibition of nicotinic acetylcholine receptors, a novel facet in the pleiotropic activities of snake venom phospholipases A2.Purification of a phospholipase A(2) from Daboia russelii siamensis venom with anticancer effectsInteractions of pharmacologically active snake venom sPLA2 with different cell linesSnake venoms are integrated systems, but abundant venom proteins evolve more rapidly.Snake venoms and hemostasis.Purification, crystallization and preliminary X-ray diffraction analysis of an acidic phospholipase A2 with vasoconstrictor activity from Agkistrodon halys pallas venomBiological and Biochemical Potential of Sea Snake Venom and Characterization of Phospholipase A2 and Anticoagulation Activity.Crystallization and preliminary X-ray diffraction analysis of hemextin A: a unique anticoagulant protein from Hemachatus haemachatus venom.Snakebite nephropathy.Unmasking snake venom of Bothrops leucurus: purification and pharmacological and structural characterization of new PLA2 Bleu TX-IIIQuantifying Demyelination in NK venom treated nerve using its electric circuit model.
P2860
Q21283933-B473CE69-7B4D-410C-99EE-CD89650561E1Q22122091-68D5C706-9D66-4463-BA32-224D15C3F37EQ26740611-37758027-56C1-437B-B672-B31DB4BB7086Q26767063-9C52234E-79A2-45F5-9EBB-19A14510C861Q27331610-871E12A6-4B43-4AE0-912D-017CAA60FE70Q27676481-5040C72D-71F0-4903-A494-99E81FFDECC2Q28388091-A07D28A1-9F92-48D0-8B36-2C767EE1FE08Q28535488-111125CB-5799-4945-A23A-7E581103F757Q28550183-E7C90AD7-37BB-4C60-A408-6A31615DD4F4Q33219673-ECAABDC3-4D95-4D8B-8087-F827CAF60CB6Q33308925-D0739BE8-9611-4355-A998-9552AE0AD74DQ33363889-2F11616C-E4A7-4C4C-A214-C5145379BBD0Q33476005-9C6B2256-8C3F-46AD-B4DA-D4841ADC763AQ33530304-43363382-0E95-41F0-9D42-DC742D9CC710Q33552284-D72758B0-68DE-4CB0-92FE-B3EE79DAC3BBQ33558677-148C66C3-BB31-45EB-BEB3-DE03A9BF0A79Q33847486-F8D90AAA-C436-49F5-8499-02EED47AD764Q33880753-330199C5-2B31-4C99-8281-00AAC0996665Q33990746-53B4776E-81CC-4246-A951-16080E468471Q34257020-671E579D-3010-479C-9BF3-03846467767DQ34301758-E59DD93B-725F-4AEA-89FF-D0F56F9823BEQ34431665-72283C40-529D-4A60-8AE1-6A84DF50687CQ34546019-DE9CD3BC-3C73-4645-82AA-8301EC96F9B9Q34546151-A03193CF-6196-46EE-B686-2A453DBC19A4Q34584995-3E8B7F0F-6883-4194-A907-C959A1B22108Q34627326-697EA735-40CD-4616-B7E1-9E45A8E9209DQ34681820-E36D36F2-423E-4421-93A6-81613796E7A9Q34768642-786B1D70-CDD5-4079-9150-61EC062D13B5Q35406603-D909E4C5-422D-4D95-B19D-D6F96DB46F91Q35529782-D7E7E290-0192-44BB-B3FD-7A24B39175CBQ35535943-854DD3F0-1665-42DA-BD29-B396CE66CA1FQ35613461-7CB615F3-10F0-48E3-9FB0-8084A2D4CC6CQ35757966-9A97861B-3AC1-46DB-AC8C-294919C01125Q36230877-8F2851C8-5A8C-413B-9328-4342418BD1D5Q36448204-06D8C2EC-3A0B-4F02-9ED3-33CB8E8E0D4DQ36515769-5AF939B6-DD4F-437C-A317-DA117F72AFC1Q36585239-E13CC91F-8A83-4C24-B5E9-14679ECC351DQ36609884-9622298F-4128-46D3-8567-D410F0350D10Q36635439-27FB7A51-570C-4283-924E-7CC4116F6B92Q36638266-FDD2C6C8-0294-4742-B0BA-2BB397AB8329
P2860
Excitement ahead: structure, function and mechanism of snake venom phospholipase A2 enzymes.
description
2003 nî lūn-bûn
@nan
2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Excitement ahead: structure, f ...... enom phospholipase A2 enzymes.
@ast
Excitement ahead: structure, f ...... enom phospholipase A2 enzymes.
@en
Excitement ahead: structure, f ...... enom phospholipase A2 enzymes.
@nl
type
label
Excitement ahead: structure, f ...... enom phospholipase A2 enzymes.
@ast
Excitement ahead: structure, f ...... enom phospholipase A2 enzymes.
@en
Excitement ahead: structure, f ...... enom phospholipase A2 enzymes.
@nl
prefLabel
Excitement ahead: structure, f ...... enom phospholipase A2 enzymes.
@ast
Excitement ahead: structure, f ...... enom phospholipase A2 enzymes.
@en
Excitement ahead: structure, f ...... enom phospholipase A2 enzymes.
@nl
P1433
P1476
Excitement ahead: structure, f ...... enom phospholipase A2 enzymes.
@en
P304
P356
10.1016/J.TOXICON.2003.11.002
P50
P577
2003-12-01T00:00:00Z