James R. Byrnes
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View article: β-Amyloid induces microglial expression of GPC4 and APOE leading to increased neuronal tau pathology and toxicity
β-Amyloid induces microglial expression of GPC4 and APOE leading to increased neuronal tau pathology and toxicity Open
To define how Aβ pathology alters microglia function in Alzheimer’s disease, we profiled the microglia surfaceome following treatment with Aβ fibrils. Our findings reveal that Aβ-associated human microglia upregulate Glypican 4 (GPC4), a G…
View article: β-Amyloid Induces Microglial Expression of GPC4 and APOE Leading to Increased Neuronal Tau Pathology and Toxicity
β-Amyloid Induces Microglial Expression of GPC4 and APOE Leading to Increased Neuronal Tau Pathology and Toxicity Open
SUMMARY To elucidate the impact of Aβ pathology on microglia in Alzheimer’s disease pathogenesis, we profiled the microglia surfaceome following treatment with Aβ fibrils. Our findings reveal that Aβ-associated human microglia upregulate G…
View article: Figure S1 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
Figure S1 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Supplementary Figure S1: Proteomic analysis identifies PVRL2 on tumor-derived exosomes.
View article: Table S1 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
Table S1 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Supplementary Table S1: Statistical analysis comparing the areas under curves (AUC) of tumor growth data between groups using an unpaired Student’s t test.
View article: Figure S2 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
Figure S2 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Supplementary Figure S2: PVRL2 promotes tumor growth through an immune-dependent mechanism.
View article: Figure S5 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
Figure S5 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Supplementary Figure S5: Combined loss of PVRL2 and PVR loss does not further inhibit tumor growth.
View article: Figure S3 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
Figure S3 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Supplementary Figure S3: PVRL2 regulates CD8 T cell and NK cell activation.
View article: Figure S1 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
Figure S1 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Supplementary Figure S1: Proteomic analysis identifies PVRL2 on tumor-derived exosomes.
View article: Data from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
Data from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Poliovirus receptor-related 2 (PVRL2, also known as nectin-2 or CD112) is believed to act as an immune checkpoint protein in cancer; however, most insight into its role is inferred from studies on its known receptor, poliovirus receptor (P…
View article: Figure S3 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
Figure S3 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Supplementary Figure S3: PVRL2 regulates CD8 T cell and NK cell activation.
View article: Data from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
Data from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Poliovirus receptor-related 2 (PVRL2, also known as nectin-2 or CD112) is believed to act as an immune checkpoint protein in cancer; however, most insight into its role is inferred from studies on its known receptor, poliovirus receptor (P…
View article: Table S1 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
Table S1 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Supplementary Table S1: Statistical analysis comparing the areas under curves (AUC) of tumor growth data between groups using an unpaired Student’s t test.
View article: Figure S2 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
Figure S2 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Supplementary Figure S2: PVRL2 promotes tumor growth through an immune-dependent mechanism.
View article: Figure S4 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
Figure S4 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Supplementary Figure S4: PVRL2 functions independently of PVRIG and TIGIT pathways.
View article: Figure S4 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
Figure S4 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Supplementary Figure S4: PVRL2 functions independently of PVRIG and TIGIT pathways.
View article: Figure S5 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
Figure S5 from PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Supplementary Figure S5: Combined loss of PVRL2 and PVR loss does not further inhibit tumor growth.
View article: PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways
PVRL2 Suppresses Antitumor Immunity through PVRIG- and TIGIT-independent Pathways Open
Poliovirus receptor-related 2 (PVRL2, also known as nectin-2 or CD112) is believed to act as an immune checkpoint protein in cancer; however, most insight into its role is inferred from studies on its known receptor, poliovirus receptor (P…
View article: PVRL2 Suppresses Anti-tumor Immunity Through PVRIG- and TIGIT-Independent Pathways
PVRL2 Suppresses Anti-tumor Immunity Through PVRIG- and TIGIT-Independent Pathways Open
PVRL2 is believed to act as an immune checkpoint protein in cancer; however, most insight into PVRL2’s role is inferred from studies on its known receptor PVRIG. Here, we directly study PVRL2. PVRL2 levels are high in tumor cells and tumor…
View article: Photoproximity Labeling from Single Catalyst Sites Allows Calibration and Increased Resolution for Carbene Labeling of Protein Partners In Vitro and on Cells
Photoproximity Labeling from Single Catalyst Sites Allows Calibration and Increased Resolution for Carbene Labeling of Protein Partners In Vitro and on Cells Open
The cell surface proteome (surfaceome) plays a pivotal role in virtually all extracellular biology, and yet we are only beginning to understand the protein complexes formed in this crowded environment. Recently, a high-resolution approach …
View article: Reciprocal stabilization of coagulation factor XIII-A and -B subunits is a determinant of plasma FXIII concentration
Reciprocal stabilization of coagulation factor XIII-A and -B subunits is a determinant of plasma FXIII concentration Open
Transglutaminase factor XIII (FXIII) is essential for hemostasis, wound healing, and pregnancy maintenance. Plasma FXIII is composed of A and B subunit dimers synthesized in cells of hematopoietic origin and hepatocytes, respectively. The …
View article: Site-specific proximity labeling at single residue resolution for identification of protein partners<i>in vitro</i>and on cells
Site-specific proximity labeling at single residue resolution for identification of protein partners<i>in vitro</i>and on cells Open
The cell surface proteome, or surfaceome, is encoded by more than 4000 genes, but we are only beginning to understand the complexes they form. Rapid proximity labeling around specific membrane targets allows for capturing weak and transien…
View article: Direct Identification of Proteolytic Cleavages on Living Cells Using a Glycan-Tethered Peptide Ligase
Direct Identification of Proteolytic Cleavages on Living Cells Using a Glycan-Tethered Peptide Ligase Open
Proteolytic cleavage of cell surface proteins triggers critical processes including cell-cell interactions, receptor activation, and shedding of signaling proteins. Consequently, dysregulated extracellular proteases contribute to malignant…
View article: Modular cytokine receptor-targeting chimeras for targeted degradation of cell surface and extracellular proteins
Modular cytokine receptor-targeting chimeras for targeted degradation of cell surface and extracellular proteins Open
Targeted degradation of cell surface and extracellular proteins via lysosomal delivery is an important means to modulate extracellular biology. However, these approaches have limitations due to lack of modularity, ease of development, rest…
View article: Cell-surface tethered promiscuous biotinylators enable comparative small-scale surface proteomic analysis of human extracellular vesicles and cells
Cell-surface tethered promiscuous biotinylators enable comparative small-scale surface proteomic analysis of human extracellular vesicles and cells Open
Characterization of cell surface proteome differences between cancer and healthy cells is a valuable approach for the identification of novel diagnostic and therapeutic targets. However, selective sampling of surface proteins for proteomic…
View article: Hypoxia Is a Dominant Remodeler of the Effector T Cell Surface Proteome Relative to Activation and Regulatory T Cell Suppression
Hypoxia Is a Dominant Remodeler of the Effector T Cell Surface Proteome Relative to Activation and Regulatory T Cell Suppression Open
Immunosuppressive factors in the tumor microenvironment (TME) impair T cell function and limit the antitumor immune response. T cell surface receptors and surface proteins that influence interactions and function in the TME are proven targ…
View article: Author response: Cell-surface tethered promiscuous biotinylators enable comparative small-scale surface proteomic analysis of human extracellular vesicles and cells
Author response: Cell-surface tethered promiscuous biotinylators enable comparative small-scale surface proteomic analysis of human extracellular vesicles and cells Open
View article: Cell-surface tethered promiscuous biotinylators enable small-scale surface proteomics of human exosomes
Cell-surface tethered promiscuous biotinylators enable small-scale surface proteomics of human exosomes Open
Characterization of cell surface proteome differences between cancer and healthy cells is a valuable approach for the identification of novel diagnostic and therapeutic targets. However, selective sampling of surface proteins for proteomic…
View article: Hypoxia is a dominant remodeler of the CD8<sup>+</sup>T cell surface proteome relative to activation and regulatory T cell-mediated suppression
Hypoxia is a dominant remodeler of the CD8<sup>+</sup>T cell surface proteome relative to activation and regulatory T cell-mediated suppression Open
Immunosuppressive factors in the tumor microenvironment (TME) impair T cell function and limit the anti-tumor immune response. T cell surface receptors that influence interactions and function in the TME are already proven targets for canc…
View article: Engineering luminescent biosensors for point-of-care SARS-CoV-2 antibody detection
Engineering luminescent biosensors for point-of-care SARS-CoV-2 antibody detection Open
Current serology tests for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) antibodies mainly take the form of enzyme-linked immunosorbent assays, chemiluminescent microparticle immunoassays or lateral flow assays, which are ei…
View article: Mapping proteolytic neo-N termini at the surface of living cells
Mapping proteolytic neo-N termini at the surface of living cells Open
Significance Cell surface proteolysis is a key mechanism for cell-cell communication and cellular signaling that is commonly dysregulated in human disease. Proteolytic cleavage events at the cell surface often evade detection by convention…