Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
Through major histocompatibility complex class Ia leader sequence-derived (VL9) peptide binding and CD94/NKG2 receptor engagement, human leucocyte antigen E (HLA-E) reports cellular health to NK cells. Previous studies demonstrated a strong bias for VL9 binding by HLA-E, a preference subsequently su...
Үндсэн зохиолчид: | Walters, L, Harlos, K, Brackenridge, S, Rozbesky, D, Barrett, J, Jain, V, Walter, T, O'Callaghan, C, Borrow, P, Toebes, M, Hansen, S, Sacha, J, Abdulhaqq, S, Greene, J, Früh, K, Marshall, E, Picker, L, Jones, E, McMichael, A, Gillespie, G |
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Формат: | Journal article |
Хэл сонгох: | English |
Хэвлэсэн: |
Springer Nature
2018
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Author Correction: Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding.
-н: Walters, LC, зэрэг
Хэвлэсэн: (2018) -
Pathogen-derived HLA-E bound epitopes reveal broad primary anchor pocket tolerability and conformationally malleable peptide binding
-н: Lucy C. Walters, зэрэг
Хэвлэсэн: (2018-08-01) -
The antibodies 3D12 and 4D12 recognise distinct epitopes and conformations of HLA-E
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The antibodies 3D12 and 4D12 recognise distinct epitopes and conformations of HLA-E
-н: Simon Brackenridge, зэрэг
Хэвлэсэн: (2024-03-01) -
Mouse and human antibodies bind HLA-E-leader peptide complexes and enhance NK cell cytotoxicity
-н: Li, D, зэрэг
Хэвлэсэн: (2022)