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Hilary Linda Hoare

Researcher at Monash University, Clayton campus

Publications -  6
Citations -  706

Hilary Linda Hoare is an academic researcher from Monash University, Clayton campus. The author has contributed to research in topics: Human leukocyte antigen & Receptor. The author has an hindex of 6, co-authored 6 publications receiving 625 citations. Previous affiliations of Hilary Linda Hoare include Monash University.

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CD94-NKG2A recognition of human leukocyte antigen (HLA)-E bound to an HLA class I leader sequence

TL;DR: Differences in the docking strategies used by the NKG2D and CD94-NKG2A receptors provided a basis for understanding the promiscuous nature of ligand recognition by NKg2D compared with the fidelity of the CD 94-NKg2 receptors.
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Crystal structure of HLA-G: A nonclassical MHC class I molecule expressed at the fetal-maternal interface

TL;DR: The alpha3 domain of HLA-G, a candidate binding site for the LIR-1 and -2 inhibitory receptors, is structurally distinct from the alpha3 domains of classical MHC-I molecules, providing a rationale for the observed affinity differences for these ligands.
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Structural basis for a major histocompatibility complex class Ib–restricted T cell response

TL;DR: The results emphasize the evolutionary 'ambiguity' of HLA-E, which not only interacts with innate immune receptors but also has the functional capacity to mediate virus-specific cytotoxic T lymphocyte responses during adaptive immunity.
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Subtle Changes in Peptide Conformation Profoundly Affect Recognition of the Non-Classical MHC Class I Molecule HLA-E by the CD94–NKG2 Natural Killer Cell Receptors

TL;DR: The data indicate that the CD94-NKG2 receptors interact with HLA-E in a manner that maximises the ability of the receptors to discriminate between subtle changes in both the sequence and conformation of peptides bound to Hla-E.
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The heterodimeric assembly of the CD94-NKG2 receptor family and implications for human leukocyte antigen-E recognition.

TL;DR: This work describes the 2.5 A resolution crystal structure of CD94-NKG2A in which the mode of dimerization contrasts with that of other homodimeric NK receptors, and indicates that the dimer interface is asymmetric, thereby providing a structural basis for the preferred heterodimerics assembly.