MHC binding affects the dynamics of different T-cell receptors in different ways

MHC binding affects the dynamics of different T-cell receptors in different ways

التفاصيل البيبلوغرافية
المؤلفون الرئيسيون:	Knapp, B, Van Der Merwe, P, Dushek, O, Deane, C
التنسيق:	Journal article
اللغة:	English
منشور في:	Public Library of Science 2019

مواد مشابهة

MHC binding affects the dynamics of different T-cell receptors in different ways.
حسب: Bernhard Knapp, وآخرون
منشور في: (2019-09-01)

The contribution of major histocompatibility complex contacts to the affinity and kinetics of T cell receptor binding
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Dependence of T cell antigen recognition on T cell receptor-peptide MHC confinement time.
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Analysis of serial engagement and peptide-MHC transport in T cell receptor microclusters.
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T cell receptor and coreceptor CD8 alphaalpha bind peptide-MHC independently and with distinct kinetics.
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Mechanisms for T cell receptor triggering.
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TCR–pMHC kinetics under force in a cell-free system show no intrinsic catch bond, but a minimal encounter duration before binding
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Fluctuations in T cell receptor and pMHC interactions regulate T cell activation
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Fluctuations in T cell receptor and pMHC interactions regulate T cell activation
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منشور في: (2022)

Kinetics and mechanics of two-dimensional interactions between T cell receptors and different activating ligands.
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T-cell receptor triggering is critically dependent on the dimensions of its peptide-MHC ligand.
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TCR binding to peptide-MHC stabilizes a flexible recognition interface.
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Mechanical forces impair antigen discrimination by reducing differences in T cell receptor off-rates
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Non-catalytic tyrosine-phosphorylated receptors.
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Basic residues in the T-cell receptor ζ cytoplasmic domain mediate membrane association and modulate signaling.
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Computationally profiling peptide:MHC recognition by T-cell receptors and T-cell receptor-mimetic antibodies
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Systems model of T cell receptor proximal signaling reveals emergent ultrasensitivity
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CD8 helps TCR catch slippery self pMHC
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Variable regions of antibodies and T-cell receptors may not be sufficient in molecular simulations investigating binding.
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Structural features underlying T-cell receptor sensitivity to concealed MHC class I micropolymorphisms.
حسب: Stewart-Jones, G, وآخرون
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Structural features underlying T-cell receptor sensitivity to concealed MHC class I micropolymorphisms.
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Regulation of temporal cytokine production by co-stimulation receptors in TCR-T cells is lost in CAR-T cells
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Intrinsic disorder in the T cell receptor creates cooperativity and controls ZAP70 binding
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Exploring peptide/MHC detachment processes using hierarchical natural move Monte Carlo
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منشور في: (2015)

Effects of common mutations in the SARS-CoV-2 Spike RBD and its ligand, the human ACE2 receptor on binding affinity and kinetics
حسب: Barton, MI, وآخرون
منشور في: (2021)

Cooperative binding of T cell receptor and CD4 to peptide-MHC enhances antigen sensitivity
حسب: Muaz Nik Rushdi, وآخرون
منشور في: (2022-11-01)

PeptX: Using Genetic Algorithms to optimize peptides for MHC binding
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pyHVis3D: Visualising Molecular Simulation deduced H-bond networks in 3D: Application to T-cell receptor interactions
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Human inhibitory receptors Ig-like transcript 2 (ILT2) and ILT4 compete with CD8 for MHC class I binding and bind preferentially to HLA-G.
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Decoupling peptide binding from T cell receptor recognition with engineered chimeric MHC-I molecules
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NNAlign_MA; MHC peptidome deconvolution for accurate MHC binding motif characterization and improved T-cell epitope predictions
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Quantifying conformational changes in the TCR:pMHC-I binding interface
حسب: Benjamin McMaster, وآخرون
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Elementary steps in T cell receptor triggering.
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Homodimerisation of the lymph vessel endothelial receptor LYVE-1 through a redox-labile disulfide is critical for hyaluronan binding in lymphatic endothelium
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Homodimerisation of the lymph vessel endothelial receptor LYVE-1 through a redox-labile disulfide is critical for hyaluronan binding in lymphatic endothelium
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T-cell receptors binding orientation over peptide/MHC class I is driven by long-range interactions.
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