By Harald Kropshofer, Anne B. Vogt
This novel, multidisciplinary instruction manual highlights fresh facts that antigen providing cells (APCs) aren't merely key avid gamers within the initiation or prevention of an antigen-specific T lymphocyte-mediated adaptive immune reaction, but additionally serious regulators and integrators within the interaction among our innate and adaptive immune system.Structured in a transparent solution to enable entry to a really wide readership, the publication is written from the point of view of a biochemist, immunologist, and scientist with event in drug improvement. It covers all cellphone forms desirous about antigen presentation, delivering the newest immunological proof with a spotlight on drug improvement. subsidized via a word list explaining all vital technical phrases, this brief yet entire reference covers easy introductory points correct as much as information for complicated experts.
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Extra resources for Antigen Presenting Cells: From Mechanisms to Drug Development
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Acad. Sci. A. 2000, 97, 11 460–11 465. 45 Boehncke WH, Takeshita T, Pendleton CD, Houghten RA, Sadeghi-Nasseri S, Racioppi L, Berzofsky JA, Germain RN. The importance of dominant negative effects of amino acid side chain substitution in peptide-MHC molecule interactions and T cell recognition. J. Immunol. 1993, 150, 331–341. 46 Sette A, Sidney J, Oseroff C, del Guercio MF, Southwood S, Arrhenius T, Powell MF, Colon SM, Gaeta FC, Grey HM. HLA DR4w4-binding motifs illustrate the biochemical basis of degeneracy and specificity in peptide-DR interactions.
N-terminally extended variants of final MHC-I-binding ligands are subjected to trimming by the ERresident aminopeptidase ERAP1, and potentially also by ERAP2/L-RAP. Peptides can bind to ER-resident chaperones such as gp96 or PDI and are removed from the ER through the Sec61 channel. Peptides of 8–10 amino acids are loaded onto MHC class I heavy chain (HC)/ b2-microglobulin (b2m) dimers that are tethered to TAP by means of the dedicated chaperone tapasin. Tapasin also recruits the oxidoreductase ERp57, which might isomerize the MHC-I a2 domain disulfide bridge during peptide loading.
Antigen Presenting Cells: From Mechanisms to Drug Development by Harald Kropshofer, Anne B. Vogt
Categories: Molecular Biology