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TAP associates with a unique class I conformation, whereas calnexin associates with multiple class I forms in mouse and man

Autor: B M Carreno, J C Solheim, M Harris, I Stroynowski, J M Connolly, T H Hansen

Publikováno v: The Journal of Immunology. 155:4726-4733

To define the rules governing de novo assembly of the trimeric class I complex, we have identified the class I folding/assembly intermediates associated with calnexin or TAP, using both human and mouse cell lines. To better characterize the class I H

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2b27526221072817a71ae6f4ac3c35f8
https://doi.org/10.4049/jimmunol.155.10.4726

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Peptide-induced rescue of serologic epitopes on class I MHC molecules

Autor: J C Solheim, B M Carreno, N B Myers, D R Lee, T H Hansen

Publikováno v: The Journal of Immunology. 154:1188-1197

To monitor conformational changes in MHC class I structure induced by interaction with peptide or beta 2-microglobulin (beta 2-m), we have taken a serologic approach. Previous studies by us and others have defined circumstances wherein specific pepti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0ac578c364eab5e0d75534982b6d597d
https://doi.org/10.4049/jimmunol.154.3.1188

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Binding of peptides lacking consensus anchor residue alters H-2Ld serologic recognition

Autor: J C Solheim, B M Carreno, J D Smith, J Gorka, N B Myers, Z Wen, J M Martinko, D R Lee, T H Hansen

Publikováno v: The Journal of Immunology. 151:5387-5397

CTL recognize class I MHC/peptide complexes on the surface of target cells. Crystallographic and serologic data have indicated that peptide ligands can influence the conformation of class I molecules and hence T cell recognition. How the binding of p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b8d1500b5286d663bf57eb9add36f937
https://doi.org/10.4049/jimmunol.151.10.5387

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Overlapping epitopes that are recognized by CD8+ HLA class I-restricted and CD4+ class II-restricted cytotoxic T lymphocytes are contained within an influenza nucleoprotein peptide

Autor: B M Carreno, R V Turner, W E Biddison, J E Coligan

Publikováno v: The Journal of Immunology. 148:894-899

Viral epitopes that are recognized by both HLA class I-restricted and class II-restricted T cells have been defined for a type A influenza virus nucleoprotein (NP) peptide. CD8+ and CD4+ CTL lines have been generated against a synthetic peptide encom

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::89ef4834ecf7e68fe6f9e04a71d1d532
https://doi.org/10.4049/jimmunol.148.3.894

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The 45 pocket of HLA-A2.1 plays a role in presentation of influenza virus matrix peptide and alloantigens

Autor: C C Winter, B M Carreno, R V Turner, S Koenig, W E Biddison

Publikováno v: The Journal of Immunology. 146:3508-3512

Amino acid substitutions were introduced into the 45 pocket of HLA-A2.1 to determine the potential role of this structurally defined feature of class I molecules in viral peptide and alloantigen presentation. The 45 pocket lies below the alpha 1-doma

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::5a7d80592a42ff6acefe92ba305078db
https://doi.org/10.4049/jimmunol.146.10.3508

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Malignes Melanom – Neoantigen-spezifische T-Zellantwort

Autor: B M Carreno

Publikováno v: Transfusionsmedizin - Immunhämatologie, Hämotherapie, Immungenetik, Zelltherapie. 5:117-117

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::88b8ce35628eb13b2160f34a15a4a287
https://doi.org/10.1055/s-0034-1397906

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Are transporter associated with antigen processing (TAP) and tapasin class I MHC chaperones?

Autor: J C Solheim, B M Carreno, T H Hansen

Publikováno v: The Journal of Immunology. 158:541-543

Class I MHC heavy chains associate with many proteins in the endoplasmic reticulum, including TAP, calnexin, calreticulin, and the newly defined tapasin molecule. Recent studies have begun to resolve the nature of how these proteins interact with cla

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::fd601c73a0ca451fb89c05ab565769cb
https://doi.org/10.4049/jimmunol.158.2.541

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CTLA-4 ligation delivers a unique signal to resting human CD4 T cells that inhibits interleukin-2 secretion but allows Bcl-X(L) induction

Autor: P J, Blair, J L, Riley, B L, Levine, K P, Lee, N, Craighead, T, Francomano, S J, Perfetto, G S, Gray, B M, Carreno, C H, June

Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 160(1)

We have assessed the functional effects of a panel of CTLA-4 mAbs on resting human CD4+ T cells. Our results demonstrate that some CTLA-4 mAbs can inhibit proliferative responses of resting CD4+ cells and cell cycle transition from G0 to G1. The inhi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a3cb875a2eef4138735a231b65f3ee61
https://pubmed.ncbi.nlm.nih.gov/9551948

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Aglycosylated and phosphatidylinositol-anchored MHC class I molecules are associated with calnexin. Evidence implicating the class I-connecting peptide segment in calnexin association

Autor: B M, Carreno, K L, Schreiber, D J, McKean, I, Stroynowski, T H, Hansen

Publikováno v: Journal of immunology (Baltimore, Md. : 1950). 154(10)

The endoplasmic reticulum resident protein calnexin interacts with several glycoproteins including class I MHC molecules. Calnexin is thought to retain free class I heavy chains and/or promote their folding and assembly with beta 2-microglobulin and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6c8d8e236df5eab9dfd5793e946673f3
https://pubmed.ncbi.nlm.nih.gov/7730623

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