31 research outputs found

    Plane-wave impulse approximation extraction of the neutron magnetic form factor from quasielastic 3He(e,e′) at Q2=0.3 to 0.6 (GeV/c)2

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    A high precision measurement of the transverse spin-dependent asymmetry AT′ in 3He(e,e′) quasielastic scattering was performed in Hall A at Jefferson Lab at values of the squared four-momentum transfer, Q2, between 0.1 and 0.6 (GeV/c)2. AT′ is sensitive to the neutron magnetic form factor, GMn. Values of GMn at Q2=0.1 and 0.2 (GeV/c)2, extracted using Faddeev calculations, were reported previously. Here, we report the extraction of GMn for the remaining Q2 values in the range from 0.3 to 0.6 (GeV/c)2 using a plane-wave impulse approximation calculation. The results are in good agreement with recent precision data from experiments using a deuterium target

    Plane-wave impulse approximation extraction of the neutron magnetic form factor from quasielastic 3He(e,e′) at Q2=0.3 to 0.6 (GeV/c)2

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    A high precision measurement of the transverse spin-dependent asymmetry AT′ in 3He(e,e′) quasielastic scattering was performed in Hall A at Jefferson Lab at values of the squared four-momentum transfer, Q2, between 0.1 and 0.6 (GeV/c)2. AT′ is sensitive to the neutron magnetic form factor, GMn. Values of GMn at Q2=0.1 and 0.2 (GeV/c)2, extracted using Faddeev calculations, were reported previously. Here, we report the extraction of GMn for the remaining Q2 values in the range from 0.3 to 0.6 (GeV/c)2 using a plane-wave impulse approximation calculation. The results are in good agreement with recent precision data from experiments using a deuterium target

    Extraction of the Neutron Magnetic Form Factor from Quasi-Elastic 3He(pol)(e(pol),e') at Q^2 = 0.1 - 0.6 (GeV/c)^2

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    We have measured the spin-dependent transverse asymmetry, A_T', in quasi-elastic inclusive electron scattering from polarized 3He with high precision at Q^2 = 0.1 to 0.6 (GeV/c)^2. The neutron magnetic form factor, GMn, was extracted at Q^2 = 0.1 and 0.2 (GeV/c)^2 using a non-relativistic Faddeev calculation that includes both final-state interactions (FSI) and meson-exchange currents (MEC). In addition, GMn was extracted at Q^2 = 0.3 to 0.6 (GeV/c)^2 using a Plane Wave Impulse Approximation calculation. The accuracy of the modeling of FSI and MEC effects was tested and confirmed with a precision measurement of the spin-dependent asymmetry in the breakup threshold region of the 3He(pol)(e(pol),e') reaction. The total relative uncertainty of the extracted GMn data is approximately 3%. Close agreement was found with other recent high-precision GMn data in this Q^2 range.Comment: Archival paper, 17 pages, 10 figures, 5 tables, submitted to Physical Review C. v2: shortened considerably, updated comparison to theor

    Genome-wide bidirectional CRISPR screens identify mucins as host factors modulating SARS-CoV-2 infection

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    Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) causes a range of symptoms in infected individuals, from mild respiratory illness to acute respiratory distress syndrome. A systematic understanding of host factors influencing viral infection is critical to elucidate SARS-CoV-2–host interactions and the progression of Coronavirus disease 2019 (COVID-19). Here, we conducted genome-wide CRISPR knockout and activation screens in human lung epithelial cells with endogenous expression of the SARS-CoV-2 entry factors ACE2 and TMPRSS2. We uncovered proviral and antiviral factors across highly interconnected host pathways, including clathrin transport, inflammatory signaling, cell-cycle regulation, and transcriptional and epigenetic regulation. We further identified mucins, a family of high molecular weight glycoproteins, as a prominent viral restriction network that inhibits SARS-CoV-2 infection in vitro and in murine models. These mucins also inhibit infection of diverse respiratory viruses. This functional landscape of SARS-CoV-2 host factors provides a physiologically relevant starting point for new host-directed therapeutics and highlights airway mucins as a host defense mechanism

    Upregulation of GALNT7 in prostate cancer modifies O-glycosylation and promotes tumour growth

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    Prostate cancer is the most common cancer in men and it is estimated that over 350,000 men worldwide die of prostate cancer every year. There remains an unmet clinical need to improve how clinically significant prostate cancer is diagnosed and develop new treatments for advanced disease. Aberrant glycosylation is a hallmark of cancer implicated in tumour growth, metastasis, and immune evasion. One of the key drivers of aberrant glycosylation is the dysregulated expression of glycosylation enzymes within the cancer cell. Here, we demonstrate using multiple independent clinical cohorts that the glycosyltransferase enzyme GALNT7 is upregulated in prostate cancer tissue. We show GALNT7 can identify men with prostate cancer, using urine and blood samples, with improved diagnostic accuracy than serum PSA alone. We also show that GALNT7 levels remain high in progression to castrate-resistant disease, and using in vitro and in vivo models, reveal that GALNT7 promotes prostate tumour growth. Mechanistically, GALNT7 can modify O-glycosylation in prostate cancer cells and correlates with cell cycle and immune signalling pathways. Our study provides a new biomarker to aid the diagnosis of clinically significant disease and cements GALNT7-mediated O-glycosylation as an important driver of prostate cancer progression
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