Zobrazeno 1 - 10 of 10 pro vyhledávání: '"R K Ribaudo"'
1
Polymorphism at position nine of the MHC class I heavy chain affects the stability of association with beta 2-microglobulin and presentation of a viral peptide
Autor: R K Ribaudo, D H Margulies
Publikováno v: The Journal of Immunology. 155:3481-3493
To identify residues that control the interactions between MHC-heavy chains and (beta 2m) sequence comparisons were made between murine class I MHC molecules with high (H-2Dd, H-2Kb) and low (H-2Ld, H-2Db) affinities for beta 2m. A single residue at
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::458b5ec29b4cd5b765027efec0a01335
https://doi.org/10.4049/jimmunol.155.7.3481
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2
Major histocompatibility complex class II-restricted presentation of an internally synthesized antigen displays cell-type variability and segregates from the exogenous class II and endogenous class I presentation pathways
Autor: R K Ribaudo, George E. Loss, C G Elias, M McKisic, Andrea J. Sant, P E Fields
Publikováno v: The Journal of Experimental Medicine
Although reported examples of endogenous antigen (Ag) presentation by major histocompatibility complex (MHC) class II molecules have increased, the mechanisms governing this process remain poorly defined. In this communication, we describe an experim
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3948bd2c0cad8f0e0b1e5c84bd0bcb11
https://doi.org/10.1084/jem.178.1.73
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3
Independent and synergistic effects of disulfide bond formation, beta 2-microglobulin, and peptides on class I MHC folding and assembly in an in vitro translation system
Autor: R K Ribaudo, D H Margulies
Publikováno v: The Journal of Immunology. 149:2935-2944
We have examined the post-translational processing, intrachain disulfide bond formation, folding, and assembly of MHC class I H chains with beta 2-microglobulin after coupled in vitro translation of homogeneous mRNA and transport of nascent chains in
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7dbf64eed935e212d71cb446fd5a57dd
https://doi.org/10.4049/jimmunol.149.9.2935
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4
The effect of human beta2-microglobulin on major histocompatibility complex I peptide loading and the engineering of a high affinity variant. Implications for peptide-based vaccines
Autor: M J, Shields, R, Kubota, W, Hodgson, S, Jacobson, W E, Biddison, R K, Ribaudo
Publikováno v: The Journal of biological chemistry. 273(43)
The ability to directly load cell surface major histocompatibility complex (MHC) class I molecules with peptides provides a potentially powerful approach toward the development of vaccines to generate cell-mediated immunity. We demonstrate that exoge
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a60203f1ffa8936d62075578312857d8
https://pubmed.ncbi.nlm.nih.gov/9774416
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5
Characterization of the interactions between MHC class I subunits: a systematic approach for the engineering of higher affinity variants of beta 2-microglobulin
Autor: M J, Shields, N, Assefi, W, Hodgson, E J, Kim, R K, Ribaudo
Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 160(5)
Human beta 2m (h beta 2m) binds to murine MHC I molecules with higher affinity than does murine beta2m and therefore can be used as a model system to define and dissect the interactions between beta2m and MHC I heavy chains that promote the stability
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::951defa7ee88b327cf6ffb898ce2b731
https://pubmed.ncbi.nlm.nih.gov/9498770
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6
Polymorphism at position nine of the MHC class I heavy chain affects the stability of association with beta 2-microglobulin and presentation of a viral peptide
Autor: R K, Ribaudo, D H, Margulies
Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 155(7)
To identify residues that control the interactions between MHC-heavy chains and (beta 2m) sequence comparisons were made between murine class I MHC molecules with high (H-2Dd, H-2Kb) and low (H-2Ld, H-2Db) affinities for beta 2m. A single residue at
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4d127f9a0d28288e6387c8a20bf4ca1b
https://pubmed.ncbi.nlm.nih.gov/7561043
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7
Independent and synergistic effects of disulfide bond formation, beta 2-microglobulin, and peptides on class I MHC folding and assembly in an in vitro translation system
Autor: R K, Ribaudo, D H, Margulies
Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 149(9)
We have examined the post-translational processing, intrachain disulfide bond formation, folding, and assembly of MHC class I H chains with beta 2-microglobulin after coupled in vitro translation of homogeneous mRNA and transport of nascent chains in
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::83d7a3a8ea214a9d54fefe8a722372a8
https://pubmed.ncbi.nlm.nih.gov/1401922
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8
Peptide and beta 2-microglobulin regulation of cell surface MHC class I conformation and expression
Autor: G R, Otten, E, Bikoff, R K, Ribaudo, S, Kozlowski, D H, Margulies, R N, Germain
Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 148(12)
We have examined the roles of peptide and beta 2-microglobulin (beta 2m) in regulating the conformation and expression level of class I molecules on the cell surface. Using a cell line synthesizing H-2Dd H chain and mouse beta 2m but defective in end
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::81594412c19dcff20df591fb698a4e40
https://pubmed.ncbi.nlm.nih.gov/1602127
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10
Aqueous humor composition in Fuchs' dystrophy
Autor: S E, Wilson, W M, Bourne, L J, Maguire, F M, Rahhal, R K, Ribaudo, D L, Kreutzer, J, O'Rourke
Publikováno v: Investigative ophthalmologyvisual science. 30(3)
Several studies have suggested differences in aqueous humor composition in Fuchs' dystrophy, including elevations in fibrinogen-related factors, compared with controls. In the current study, aqueous humor was obtained at surgery from 10 uninflamed ey
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::809c2cc08c9be6f82d60e9fe98657df9
https://pubmed.ncbi.nlm.nih.gov/2784424
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