Publications by authors named "J Gor"
Clonal evolution (CE) is a driving force behind the development and progression of acute myeloid leukemia (AML). Advances in molecular and cytogenetic assays have improved the depth and breadth of detection of CE in AML, which is defined here as a detected change in cytogenetic or molecular profile at relapsed or refractory (RR) disease. In this study, we demonstrate the clinical impact of CE in a cohort of patients with RR AML treated between 2013 and 2023.
View Article and Find Full Text PDFHuman complement factor H (CFH) plays a central role in regulating activated C3b to protect host cells. CFH contain 20 short complement regulator (SCR) domains and eight N-glycosylation sites. The N-terminal SCR domains mediate C3b degradation while the C-terminal CFH domains bind to host cell surfaces to protect these.
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- Human IgG consists of four subclasses (IgG1-4), with IgG4 having a notably short hinge region and two glycan chains on its Fc subunit, the significance of which is not fully known.
- A study compared the structure and stability of glycosylated and deglycosylated IgG4 A33, revealing that deglycosylation resulted in a monomeric form with minimal changes in overall structure as observed through various analytical techniques.
- The findings suggest that while deglycosylated IgG4 exhibits greater conformational variability in its Fc structure compared to its glycosylated form, significant structural changes are more pronounced in IgG1 than in IgG4.
Relapsed or refractory acute myeloid leukemia (AML) is associated with poor outcomes and resistance to therapy. The addition of venetoclax, a BCL-2 antagonist, to lower-intensity therapies results in improved survival in the first-line setting compared to monotherapy with a hypomethylating agent or low-dose cytarabine. Despite this, much remains unknown about the performance of venetoclax with a hypomethylating agent following the first-line setting.
View Article and Find Full Text PDFHeavy chain-only antibodies can offer advantages of higher binding affinities, reduced sizes, and higher stabilities than conventional antibodies. To address the challenge of SARS-CoV-2 coronavirus, a llama-derived single-domain nanobody C5 was developed previously that has high COVID-19 virus neutralization potency. The fusion protein C5-Fc comprises two C5 domains attached to a glycosylated Fc region of a human IgG1 antibody and shows therapeutic efficacy in vivo.
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