Lynda M. Pierini
Cornell University
22 Papers
513 Citations
Lynda M. Pierini is an academic researcher from Cornell University. The author has contributed to research in topics: Biology & Lipoprotein. The author has an hindex of 19, co-authored 22 publications. Previous affiliations of Lynda M. Pierini include Columbia University & Rush University Medical Center.
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Papers
Elevated Plasma Membrane Cholesterol Content Alters Macrophage Signaling and Function
TL;DR: Findings indicate that increased membrane cholesterol causes dramatic effects on macrophage cellular functions related to the actin cytoskeleton, and should provide new insights into the early steps of atherogenesis.
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Uptake of serum-opsonized Francisella tularensis by macrophages can be mediated by class A scavenger receptors
TL;DR: A novel role for SRA in innate immunity is supported and a potential therapeutic approach for modulating F.’tularensis infection is suggested, namely, blocking SRA as a means of hindering F. “t ularensis access to its intracellular niche.
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Spatial and temporal sequence of capsule construction in Cryptococcus neoformans
TL;DR: It is shown that the capsule overlying buds is newly synthesized and differs physically from the corresponding parental material, which is the first model of capsule synthesis and open new lines of investigation into the underlying mechanisms.
89
Fc epsilon RI-mediated association of 6-micron beads with RBL-2H3 mast cells results in exclusion of signaling proteins from the forming phagosome and abrogation of normal downstream signaling.
TL;DR: The results suggest that initiation of phagocytosis diverts normal signaling pathways in a cytoskeleton-driven membrane clearance process that alters the physiological response of the cells.
80
Flotillas of lipid rafts fore and aft
TL;DR: Further evidence is provided for the importance of specialized lipid domains in establishing and maintaining the polarity of motile cells by showing that both the leading edge and the uropod of polarized T lymphocytes are enriched in lipid components that partition into raft-like lipid domains.
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