Linked Life Data

11051811

Source:http://linkedlifedata.com/resource/pubmed/id/11051811

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-11-13
pubmed:abstractText
Many heat shock proteins, e.g. gp96, HSP90, HSP70, etc have elicited rejection and immunotherapy immunogenicity of tumor and infectious diseases. Further study indicated that hsps can chaperone the endogenous repertoire of peptides, and the antigenicity of hsp-peptide complexes lies in the peptides, not HSPs. HSPs present peptides associated with them to MHC class I molecules for recognition by CTL and memory T cells, and elicit cellular immune responses. The latest finding shows that gp96 may present antigenic peptides directly to T lymphocytes functionally as MHC. In recent years the mechanism of immunogenicity and advantages as vaccine therapy of gp96 and HSP70, the two main hsps in mammals have been studied in detail, which offers a new opportunity for immunotherapy of hepatitis B and hepatocellular carcinoma.
pubmed:language
chi
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1000-3061
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
425-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
[Role of heat shock protein-peptide complexes on tumor and infectious diseases immunity].
pubmed:affiliation
Institute of Microbiology, Chinese Academy of Sciences, Beijing.
pubmed:publicationType
Journal Article, English Abstract