about
Bacterial Sphingomyelinases and Phospholipases as Virulence FactorsAmino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities.Comparison of a nontoxic variant of Clostridium perfringens α-toxin with the toxic wild-type strainSnake venomics and antivenomics of Bothrops colombiensis, a medically important pitviper of the Bothrops atrox-asper complex endemic to Venezuela: Contributing to its taxonomy and snakebite management.Profiling the venom gland transcriptomes of Costa Rican snakes by 454 pyrosequencing.Cellular UDP-glucose deficiency caused by a single point mutation in the UDP-glucose pyrophosphorylase gene.Expanding the neutralization scope of the EchiTAb-plus-ICP antivenom to include venoms of elapids from Southern Africa.Role of Clostridium perfringens phospholipase C in the pathogenesis of gas gangrene.The NanI and NanJ sialidases of Clostridium perfringens are not essential for virulence.Snake venomics and antivenomics: Proteomic tools in the design and control of antivenoms for the treatment of snakebite envenoming.Cross-reactivity, antivenomics, and neutralization of toxic activities of Lachesis venoms by polyspecific and monospecific antivenomsLemnitoxin, the major component of Micrurus lemniscatus coral snake venom, is a myotoxic and pro-inflammatory phospholipase A2.Snake venomics of the Central American rattlesnake Crotalus simus and the South American Crotalus durissus complex points to neurotoxicity as an adaptive paedomorphic trend along Crotalus dispersal in South America.Venoms of Micrurus coral snakes: Evolutionary trends in compositional patterns emerging from proteomic analyses.Internalization of Clostridium perfringens α-toxin leads to ERK activation and is involved on its cytotoxic effect.Reactive oxygen species and the MEK/ERK pathway are involved in the toxicity of clostridium perfringens α-toxin, a prototype bacterial phospholipase C.Studies on the venom proteome of Bothrops asper: perspectives and applications.A cellular deficiency of gangliosides causes hypersensitivity to Clostridium perfringens phospholipase C.A cellular UDP-glucose deficiency causes overexpression of glucose/oxygen-regulated proteins independent of the endoplasmic reticulum stress elements.Identification of residues critical for toxicity in Clostridium perfringens phospholipase C, the key toxin in gas gangrene.Clostridium perfringens phospholipase C induced ROS production and cytotoxicity require PKC, MEK1 and NFκB activationA point mutation in the UDP-glucose pyrophosphorylase gene results in decreases of UDP-glucose and inactivation of glycogen synthase.Impact of regional variation in Bothrops asper snake venom on the design of antivenoms: integrating antivenomics and neutralization approaches.Structural characterization and phylogenetic relationships of myotoxin II from Atropoides (Bothrops) nummifer snake venom, a Lys49 phospholipase A(2) homologue.Snake venomics of Lachesis muta rhombeata and genus-wide antivenomics assessment of the paraspecific immunoreactivity of two antivenoms evidence the high compositional and immunological conservation across Lachesis.Immunization with cDNA of a novel P-III type metalloproteinase from the rattlesnake Crotalus durissus durissus elicits antibodies which neutralize 69% of the hemorrhage induced by the whole venom.Neutralization of venom-induced hemorrhage by equine antibodies raised by immunization with a plasmid encoding a novel P-II metalloproteinase from the lancehead pitviper Bothrops asper.Snake venomics of the lancehead pitviper Bothrops asper: geographic, individual, and ontogenetic variations.Venomic and antivenomic analyses of the Central American coral snake, Micrurus nigrocinctus (Elapidae).Identification of B cell recognized linear epitopes in a snake venom serine proteinase from the central American bushmaster Lachesis stenophrys.Ocatin. A novel tuber storage protein from the andean tuber crop oca with antibacterial and antifungal activities.Phospholipase C and sphingomyelinase activities of the Clostridium perfringens alpha-toxin.Development of a new polyspecific antivenom for snakebite envenoming in Sri Lanka: Analysis of its preclinical efficacy as compared to a currently available antivenom.Effects of Clostridium perfringens phospholipase C in mammalian cells.Effects of bilayer composition and physical properties on the phospholipase C and sphingomyelinase activities of Clostridium perfringens α-toxin.Identification of Residues in the Carboxy-Terminal Domain of Clostridium perfringens α-Toxin (Phospholipase C) Which Are Required for Its Biological ActivitiesUnexpected wide substrate specificity of C. perfringens α-toxin phospholipase CDevelopment of immunoassays for determination of circulating venom antigens during envenomations by coral snakes (Micrurus species)Antibody-mediated neutralization and binding-reversal studies on α-neurotoxins from micrurus nigrocinctus nigrocinctus (coral snake) venomImmunochemical characterization of Micrurus nigrocinctus nigrocinctus venom with monoclonal and polyclonal antibodies
P50
Q26745804-91FA8C98-102C-4132-8E01-F6F95666BD88Q27642198-B687620C-F645-437C-B7A0-928F115D00C8Q27665010-79C3F733-D6F9-4ED8-BC4B-672C279C1734Q33449080-2468AEB5-9B18-4FA2-BEBE-89FD79228A47Q33909226-A7ABFABB-ABCB-413B-B7E8-E255E92D1FBDQ34438991-430A42F5-02E1-4945-A49A-BC75A62A4797Q34545973-0180074B-DB04-48D8-81DF-48823668FB5AQ35690593-98BA4157-209E-43DB-BF0C-F1D36BEFC9BFQ37355868-3F7566B1-99BB-46F2-98D7-B0A755C3CEC4Q37432420-D9E21E57-C6E1-49F5-BD0D-223ACBA8FE77Q38634650-D9BE1B0F-10D0-450B-B9D9-25B2060A2391Q38765452-3FEEEDC7-50E3-4B9B-A44C-B06B757DA0B6Q38929637-3F3EC4BB-0BE4-41F2-94A8-3EB78EED19CAQ38958137-AF3C3575-5900-48CD-87D0-CB860B40D0BDQ39061874-F78F35D9-1EC9-4B99-A181-D8F4599E8AE2Q39294904-972C2F4F-45F0-4EB2-A1D8-EB4DFB8333EDQ39969702-5805F487-6B4C-4CEC-9973-1EC00C55D5EFQ40416619-A1862552-9FB9-4159-ABD9-EBEFF7477F2EQ40578520-DA35A5CA-FAAA-4BA0-B3E7-68F648CC742CQ40863570-45D3505E-98CF-49EE-991E-9A475F23D1E1Q41888502-2D296DC5-53CF-45F4-A012-01C7D4190A12Q42670535-5C4A6B06-3EE0-494D-B691-CC81594F30D9Q43242776-69FFF726-ADC1-433E-BF7F-7A04B35B104BQ44071269-9E83DA30-B4B2-492B-BAF6-C35A468764D1Q44860631-88E3C481-490E-49E4-BD06-552AAF11F363Q44863317-02140FBE-16CB-4DEC-A9DA-7D96316EEDDCQ45383599-02A9C356-B643-4266-97C0-709801760B2DQ46448646-7DAD0D47-BE1C-40A5-9038-324CA08C4E23Q46482259-9CF3D4E0-8124-4A02-91CA-A9D1C587A719Q47432244-D92478C7-549C-4083-9BCF-2802EDA88A77Q47449813-B57EFD7F-A376-4308-8745-E90C52A1880BQ47844464-814935F5-F9C1-4875-BCC3-A866EE13FF89Q51412341-7CF904B8-30AF-407E-BA0A-53446D4D1CCDQ52570889-190C579E-BA7C-404E-B774-F2AFDBCA3822Q54380634-1A3485E9-394A-4A8E-957F-37C2FB3242DAQ57917951-0A79196F-A048-4153-9D3F-AA504495F880Q58482692-7D06F532-16CE-4C55-A214-4533F55E2930Q59290871-1E54D994-B4EC-4589-829D-EB3EA92EEC50Q59290906-0DDC4FB2-F8F7-4CDB-A85C-C68E68F276F8Q59290984-8832DBA7-2733-4754-AB13-A4827B617E52
P50
description
researcher ORCID ID = 0000-0003-3934-8496
@en
wetenschapper
@nl
name
Alberto Alape-Girón
@ast
Alberto Alape-Girón
@en
Alberto Alape-Girón
@es
Alberto Alape-Girón
@nl
type
label
Alberto Alape-Girón
@ast
Alberto Alape-Girón
@en
Alberto Alape-Girón
@es
Alberto Alape-Girón
@nl
prefLabel
Alberto Alape-Girón
@ast
Alberto Alape-Girón
@en
Alberto Alape-Girón
@es
Alberto Alape-Girón
@nl
P21
P31
P496
0000-0003-3934-8496