The Experts below are selected from a list of 231 Experts worldwide ranked by ideXlab platform
Masanori Kasahara - One of the best experts on this subject based on the ideXlab platform.
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Evolution of the Major Histocompatibility Complex: Molecular cloning of Major Histocompatibility Complex class I from the amphibian Xenopus (Major Histocompatibility Complex class II/immunoglobulin superfamily/CDl/expression library)
2016Co-Authors: Martin F. Flajnik, Camilo Canel, Jack Kramer, Masanori KasaharaAbstract:Class I Major Histocompatibility Complex (MHC) cDNA clones have been isolated from an expression library derived from mRNA of an MHC homozygous Xenopus laevis. The nucleotide and predicted amino acid sequences show definite similarity to MHC class I molecules of higher verte- brates. The immunoglobulin-like a-3 domain is more similar to the immunoglobulin-like domains of mammalian class II 13 chains than to those of mammalian class I molecules, and a tree based on nucleotide sequences of representative MHC genes is presented.
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The chromosomal duplication model of the Major Histocompatibility Complex
Immunological reviews, 1999Co-Authors: Masanori KasaharaAbstract:The Major Histocompatibility Complex (MHC) is a genetic region that has been extensively studied by immunologists, molecular biologists, and evolutionary biologists. Nevertheless, our knowledge of how the MHC acquired its present-day organization is quite limited. The recent discovery that the mammalian genome contains regions paralogous to the MHC has led us to the proposal that the MHC region of jawed vertebrates arose as a result of ancient chromosomal duplications. Here, I review the current status of this proposal.
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Evolution of the Major Histocompatibility Complex: molecular cloning of Major Histocompatibility Complex class I from the amphibian Xenopus
Proceedings of the National Academy of Sciences of the United States of America, 1991Co-Authors: Martin F. Flajnik, Camilo Canel, Jack Kramer, Masanori KasaharaAbstract:Abstract Class I Major Histocompatibility Complex (MHC) cDNA clones have been isolated from an expression library derived from mRNA of an MHC homozygous Xenopus laevis. The nucleotide and predicted amino acid sequences show definite similarity to MHC class I molecules of higher vertebrates. The immunoglobulin-like alpha-3 domain is more similar to the immunoglobulin-like domains of mammalian class II beta chains than to those of mammalian class I molecules, and a tree based on nucleotide sequences of representative MHC genes is presented.
Alfred L Goldberg - One of the best experts on this subject based on the ideXlab platform.
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Post-proteasomal antigen processing for Major Histocompatibility Complex class I presentation
Nature Immunology, 2004Co-Authors: Kenneth L Rock, Ian A. York, Alfred L GoldbergAbstract:Peptides presented by Major Histocompatibility Complex class I molecules are derived mainly from cytosolic oligopeptides generated by proteasomes during the degradation of intracellular proteins. Proteasomal cleavages generate the final C terminus of these epitopes. Although proteasomes may produce mature epitopes that are eight to ten residues in length, they more often generate N-extended precursors that are too long to bind to Major Histocompatibility Complex class I molecules. Such precursors are trimmed in the cytosol or in the endoplasmic reticulum by aminopeptidases that generate the N terminus of the presented epitope. Peptidases can also destroy epitopes by trimming peptides to below the size needed for presentation. In the cytosol, endopeptidases, especially thimet oligopeptidase, and aminopeptidases degrade many proteasomal products, thereby limiting the supply of many antigenic peptides. Thus, the extent of antigen presentation depends on the balance between several proteolytic processes that may generate or destroy epitopes.
Lutz Walter - One of the best experts on this subject based on the ideXlab platform.
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The Major Histocompatibility Complex of the rat (Rattus norvegicus)
Immunogenetics, 2001Co-Authors: Eberhard Günther, Lutz WalterAbstract:This review of the RT1 Complex, the Major Histocompatibility Complex (MHC) of the rat, focuses on genetic, genomic, evolutionary, and functional aspects at the molecular level. The class I, class II, and framework genes are listed. The physical map of the RT1 Complex as revealed by analysis of clonal contigs is compared with the human and mouse MHC, and the degree of orthologous relationship is outlined. Elucidation of the RT1 Complex provides important information for using the rat as a model of experimental transplantation and Complex diseases.
Chu-young Kim - One of the best experts on this subject based on the ideXlab platform.
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Engineering the polyproline II propensity of a class II Major Histocompatibility Complex ligand peptide.
ACS chemical biology, 2013Co-Authors: Sathya D. Unudurthi, Kinya Hotta, Chu-young KimAbstract:Our immune system constantly samples peptides found inside the body as a means to detect foreign pathogens, infected cells, and tumorous cells. T cells, which carry out the critical task of distinguishing self from nonself peptides, can only survey peptides that are presented by the Major Histocompatibility Complex protein. We investigated how the secondary structure of a peptide, namely, the polyproline II helix content, influences Major Histocompatibility Complex binding. We synthesized 12 analogues of the wheat gluten derived α-I-gliadin peptide and tested their binding to the celiac disease associated HLA-DQ2 protein. Our analogue library represents a broad spectrum of polyproline II propensities, ranging from random coil structure to high polyproline II helix content. Overall, there was no noticeable correlation between the peptide polyproline II helix content and HLA-DQ2 binding. One analogue peptide, which has low polyproline II helix content, showed a 4.5-fold superior binding compared to native α...
Kenneth L Rock - One of the best experts on this subject based on the ideXlab platform.
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Post-proteasomal antigen processing for Major Histocompatibility Complex class I presentation
Nature Immunology, 2004Co-Authors: Kenneth L Rock, Ian A. York, Alfred L GoldbergAbstract:Peptides presented by Major Histocompatibility Complex class I molecules are derived mainly from cytosolic oligopeptides generated by proteasomes during the degradation of intracellular proteins. Proteasomal cleavages generate the final C terminus of these epitopes. Although proteasomes may produce mature epitopes that are eight to ten residues in length, they more often generate N-extended precursors that are too long to bind to Major Histocompatibility Complex class I molecules. Such precursors are trimmed in the cytosol or in the endoplasmic reticulum by aminopeptidases that generate the N terminus of the presented epitope. Peptidases can also destroy epitopes by trimming peptides to below the size needed for presentation. In the cytosol, endopeptidases, especially thimet oligopeptidase, and aminopeptidases degrade many proteasomal products, thereby limiting the supply of many antigenic peptides. Thus, the extent of antigen presentation depends on the balance between several proteolytic processes that may generate or destroy epitopes.
