Linked Life Data

19961869

Source:http://linkedlifedata.com/resource/pubmed/id/19961869

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-2-17
pubmed:abstractText
The tri-dimensional (3D) structure determined by NMR of functionally relevant High Activity Binding Peptides (HABPs) of chemically-synthesized malarial proteins, involved in invasion to target cells, is practically identical, at the atomic level, to their corresponding recombinantly produced proteins, determined by X-ray crystallography. Both recombinant proteins as well as these chemically-synthesized HABPs bind to host-cell receptors through channels or troughs formation, stabilized by hydrogen bonding; most of them are located on distant segments to the highly polymorphic, highly antigenic, strain specific amino acid sequences the parasite uses to evade immune pressure. When these immunologically silent conserved HABPs are specifically modified, they become highly immunogenic and capable of inducing protective immune responses, supporting the specifically modified minimal subunit-based, multiepitopic, chemically-synthesized vaccines concept.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1873-1732
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
102
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
38-44
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Atomic fidelity of subunit-based chemically-synthesized antimalarial vaccine components.
pubmed:affiliation
Fundación Instituto de Inmunología de Colombia (FIDIC), Bogotá D.C., Colombia; Universidad Nacional de Colombia, Ciudad Universitaria, Bogotá D.C., Colombia. mepatarr@mail.com <mepatarr@mail.com>
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't