Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap Velos
ORGANISM(S): Bothrops Cotiara
TISSUE(S): Venom
SUBMITTER: Alexandre Keiji Tashima
LAB HEAD: Alexandre Keiji Tashima
PROVIDER: PXD036130 | Pride | 2023-10-20
REPOSITORIES: Pride
Action | DRS | |||
---|---|---|---|---|
2022_Bcotiarapep.mgf | Mgf | |||
CompiledDB_BjGenome_BPPs_311entries.fasta | Fasta | |||
OB_BCOT_PEP_R1_20150409_16.raw | Raw | |||
OB_BCOT_PEP_R2_20150409_17.raw | Raw | |||
OB_BCOT_PEP_R3_20150409_18.raw | Raw |
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Miyamoto Jackson Gabriel JG Kitano Eduardo Shigueo ES Zelanis André A Nachtigall Pedro Gabriel PG Junqueira-de-Azevedo Inácio I Sant'Anna Sávio Stefanini SS Lauria da Silva Rogério R Bersanetti Patrícia Alessandra PA Carmona Adriana Karaoglanovic AK Barbosa Pereira Pedro José PJ Serrano Solange M T SMT Vilela Oliva Maria Luiza ML Tashima Alexandre Keiji AK
Biochimie 20231014
Snake venoms are primarily composed of proteins and peptides, which selectively interact with specific molecular targets, disrupting prey homeostasis. Identifying toxins and the mechanisms involved in envenoming can lead to the discovery of new drugs based on natural peptide scaffolds. In this study, we used mass spectrometry-based peptidomics to sequence 197 peptides in the venom of Bothrops cotiara, including a novel 7-residue peptide derived from a snake venom metalloproteinase. This peptide, ...[more]