Zobrazeno 1 - 10
of 66
pro vyhledávání: '"Peptide editing"'
Publikováno v:
Wellcome Open Research, Vol 9 (2024)
Background Major histocompatibility class I (MHC-I, human leukocyte antigen [HLA]-I in humans) molecules present small fragments of the proteome on the cell surface for immunosurveillance, which is pivotal to control infected and malignant cells. Imm
Externí odkaz:
https://doaj.org/article/ab62c45160514459b941413a277bb80b
Autor:
Lina Sagert, Christian Winter, Ina Ruppert, Maximilian Zehetmaier, Christoph Thomas, Robert Tampé
Publikováno v:
eLife, Vol 12 (2023)
Adaptive immune responses are triggered by antigenic peptides presented on major histocompatibility complex class I (MHC I) at the surface of pathogen-infected or cancerous cells. Formation of stable peptide-MHC I complexes is facilitated by tapasin
Externí odkaz:
https://doaj.org/article/4afe7db9f697492296b426c4fb3a9539
Autor:
Siddhartha Kundu
Publikováno v:
Heliyon, Vol 7, Iss 7, Pp e07466- (2021)
The peptide loading complex (PLC) is a multi-protein complex of the endoplasmic reticulum (ER) which optimizes major histocompatibility I (MHC1)-mediated export of intracellular high-affinity peptides. Whilst, the molecular biology of MHC1-mediated e
Externí odkaz:
https://doaj.org/article/bf586303850b49928d833ca99c79717a
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Publikováno v:
eLife, Vol 9 (2020)
Adaptive immunity vitally depends on major histocompatibility complex class I (MHC I) molecules loaded with peptides. Selective loading of peptides onto MHC I, referred to as peptide editing, is catalyzed by tapasin and the tapasin-related TAPBPR. An
Externí odkaz:
https://doaj.org/article/aad042b8eaa3460a8d3651d4aef5bd71
Akademický článek
Tento výsledek nelze pro nepřihlášené uživatele zobrazit.
K zobrazení výsledku je třeba se přihlásit.
K zobrazení výsledku je třeba se přihlásit.
Autor:
Ilca, F Tudor, Boyle, Louise
Glycosylation plays a crucial role in the folding, structure, quality control and trafficking of glycoproteins. Here, we explored whether the glycosylation status of MHC class I (MHC-I) molecules impacts their affinity for the peptide editor, TAPBPR.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2f7795209443fc277df8b5032058c80
https://www.repository.cam.ac.uk/handle/1810/328105
https://www.repository.cam.ac.uk/handle/1810/328105
Autor:
Jihye Park, Danai Moschidi, Jugmohit S. Toor, Christine A. Devlin, Hannah Choi, Sarvind Tripathi, Nikolaos G. Sgourakis, David Flores-Solis, Andrew C. McShan, Erik Procko, Sarah A. Overall
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America 116(51), 25602-25613 (2019). doi:10.1073/pnas.1915562116
Proceedings of the National Academy of Sciences of the United States of America, vol 116, iss 51
Proceedings of the National Academy of Sciences of the United States of America 116(51), 25602-25613 (2019). doi:10.1073/pnas.1915562116
Proceedings of the National Academy of Sciences of the United States of America, vol 116, iss 51
Significance The human population contains thousands of MHC-I alleles, showing a range of dependencies on molecular chaperones for loading of their peptide cargo, which are then displayed on the cell surface for T cell surveillance. Using the chapero
Autor:
Louise H. Boyle, F. Tudor Ilca
Publikováno v:
Molecular Immunology
Highlights • The interaction between TAPBPR and MHC-I is stronger when MHC-I lacks a glycan. • TAPBPR dissociates peptides more easily from non-glycosylated MHC-I. • Glycosylation status of MHC-I influences their ability to undergo peptide exch
Revisiting nonclassical HLA II functions in antigen presentation: Peptide editing and its modulation
Autor:
Christian Freund, Miguel Álvaro-Benito
Publikováno v:
HLAREFERENCES. 96(4)
The nonclassical major histocompatibility complex of class II molecules (ncMHCII) HLA-DM (DM) and HLA-DO (DO) feature essential functions for the selection of the peptides that are displayed by classical MHCII proteins (MHCII) for CD4(+)T(h)cell surv