Conserved high activity binding peptides are involved in adhesion of two detergent-resistant membrane-associated merozoite proteins to red blood cells during invasion
Detergent resistant membranes (DRMs) of Plasmodium falciparum merozoites contain a large number of glycosylphosphatidylinositol (GPI)-anchored proteins that have been implicated in interactions between merozoites and red blood cells (RBCs). In this study, two cysteine-rich proteins anchored by GPI t...
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2010
- Institución:
- Universidad del Rosario
- Repositorio:
- Repositorio EdocUR - U. Rosario
- Idioma:
- eng
- OAI Identifier:
- oai:repository.urosario.edu.co:10336/22401
- Acceso en línea:
- https://doi.org/10.1021/jm901474p
https://repository.urosario.edu.co/handle/10336/22401
- Palabra clave:
- Binding protein
Cell surface receptor
Cysteine
Detergent
Glycosylphosphatidylinositol
High activity binding peptide
Malaria vaccine
Pf113 protein
Pf92 protein
Protozoal protein
Unclassified drug
Amino acid sequence
Animal experiment
Animal model
Article
Binding affinity
Binding assay
Binding site
Cell adhesion
Cell invasion
Circular dichroism
Controlled study
Cross linking
Erythrocyte
Human
Human cell
Immunofluorescence
Lipid raft
Merozoite
Nonhuman
Plasmodium falciparum
Protein binding
Protein localization
Protein polymorphism
Animals
Binding sites
Chymotrypsin
Circular dichroism
Cross-linking reagents
Cysteine
Detergents
Erythrocytes
Glycosylphosphatidylinositols
Host-parasite interactions
Immune sera
Membrane proteins
Merozoites
Neuraminidase
Peptides
Plasmodium falciparum
Protein binding
Protozoan proteins
Rabbits
Succinimides
Trypsin
genetic
secondary
molecular
Models
Polymorphism
Protein structure
- Rights
- License
- Abierto (Texto Completo)