Results 21 to 30 of about 2,019 (200)
The many dimeric faces of Lys49 PLA<sub>2</sub>-like proteins: Conformational plasticity and membrane binding drive functional dimer states. [PDF]
Protein SciAbstract Lys49 secreted phospholipase A2‐like proteins (sPLA2s) are major myotoxins in viperid snake venoms, causing rapid muscle damage in envenomation. Beyond their clinical relevance, these small non‐catalytic proteins provide a model to study how quaternary structure and conformational dynamics enable catalysis‐independent membrane disruption ...
Lima DCA +4 more
europepmc +2 more sources
Mechanism of inhibition of Ca2+-ATPase by myotoxin a [PDF]
Biochemical Journal, 1995 The peptide DCRQKWKCCKKGSG [myotoxin-(29-42)], corresponding to residues 29-42 of myotoxin a, inhibits the activity of the Ca(2+)-ATPase of skeletal muscle sarcoplasmic reticulum, with a Kd value of 19.4 microM at pH 7.5, in 100 mM KCl. The peptide YKQCHKKGGHCFPKEK, corresponding to residues 1-16 of myotoxin a, is a less potent inhibitor. Inhibition by
K J, Baker, J M, East, A G, Lee
openaire +2 more sources
Scientific Reports, 2021 Viperid snake venoms contain a unique family of cytotoxic proteins, the Lys49 PLA2 homologs, which are devoid of enzymatic activity but disrupt the integrity of cell membranes.
Alfredo Jesús López-Dávila +7 more
doaj +1 more source
Role of enzymatic activity in muscle damage and cytotoxicity induced by Bothrops asper Asp49 phospholipase A2 myotoxins: are there additional effector mechanisms involved? [PDF]
PeerJ, 2014 Viperid venoms often contain mixtures of Asp49 and Lys49 PLA2 myotoxin isoforms, relevant to development of myonecrosis. Given their difference in catalytic activity, mechanistic studies on each type require highly purified samples.
Diana Mora-Obando +4 more
doaj +2 more sources
Engineering Antivenom: Research Progress and Future Directions in Snakebite Envenoming Therapy. [PDF]
Ann N Y Acad SciSnakebite envenoming therapy is evolving from plasma‐derived antivenoms toward rationally engineered therapeutics. Advances in toxicovenomics, structural biology, antibody engineering, computational protein design, recombinant expression, small‐molecule inhibitors, and diagnostics are enabling toxin‐centric development of safer, more effective, and ...
Laustsen AH.
europepmc +2 more sources
Toxins, 2014 A monomeric basic PLA2 (PhTX-II) of 14149.08 Da molecular weight was purified to homogeneity from Porthidium hyoprora venom. Amino acid sequence by in tandem mass spectrometry revealed that PhTX-II belongs to Asp49 PLA2 enzyme class and displays ...
Salomón Huancahuire-Vega +2 more
doaj +1 more source
Autocatalytic Acylation of Phospholipase-like Myotoxins
Biochemistry, 1995 Several snake venoms contain a phospholipase A2 in which position 49 in the active site is occupied by a lysine or a serine instead of the aspartate residue normally found. Although these proteins do not bind Ca2+ and are devoid of catalytic activity, they are still highly specific myotoxins and have recently been shown to induce membrane leakage by a ...
PEDERSEN, JENS ZACHO +5 more
openaire +5 more sources
A myotoxin secreted by some piscivorousConusspecies [PDF]
British Journal of Pharmacology, 1972 Summary. Toxins isolated from the venom apparatus ofConus magusandConus achatinushave the same pharmacological properties, but differ from the toxins of several other piscivorous species of cone shells..C. magusandC. achatinustoxins are heat labile at pH 8·5.
S E, Freeman, R J, Turner
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Detection of proteins antigenically related to Bothrops asper myotoxin in crotaline snake venoms [PDF]
, 1987 The presence of components antigenically related to Bothrops asper myotoxin was investigated by Western blotting and immunoelectrophoretic techniques. B.
Moreno Robles, Edgardo +3 more
core +1 more source
Journal of Venomous Animals and Toxins including Tropical Diseases, 2011 A myotoxin phospholipase A2 homologue, BmooMtx, was isolated from the venom of Bothrops moojeni by a combination of ion-exchange chromatography on DEAE-Sephacel column and gel filtration on Sephadex G-75. SDS-PAGE showed the enzyme to be a monomer with a
MR Queiroz +9 more
doaj +1 more source