Articles by Melissa V. Fernandez in JoVE
Attivazione e misurazione dei NLRP3 inflammasome all'attività utilizzando IL-1β in cellule dendritiche umane derivate da monociti Melissa V. Fernandez1, Elizabeth A. Miller2, Nina Bhardwaj3 1Department of Pathology, New York University School of Medicine, 2Division of Infectious Diseases, Department of Medicine, Mount Sinai Medical Center, 3Division of Hematology and Oncology, Hess Center for Science and Medicine, Mount Sinai Medical Center Le cellule dendritiche (DC) secernono IL-1β in risposta al riconoscimento di TLR8 purinico sintetico, R848, seguita dall'attivazione inflammasome NLRP3 con nigericin, dunque, IL-1β può essere utilizzata per misurare l'attività inflammasome NLRP3. Intracellulare colorazione citochina, immunoblotting, ELISA e sono utilizzati per misurare con precisione NLRP3 inflammasome adescamento e l'attivazione tramite l'espressione di IL-1β.
Other articles by Melissa V. Fernandez on PubMed
The Conformation of End-groups is One Determinant of Carotenoid Topology Suitable for High Fidelity Molecular Recognition: a Study of Beta- and Epsilon-end-groups Archives of Biochemistry and Biophysics. Jan, 2010 | Pubmed ID: 19850003 Conformation affects a carotenoid's ability to bind selectively to proteins. We calculated adiabatic energy profiles for rotating the ring end-groups around the C6C7 bond and for flexing of the ring with respect to the polyene chain. The choice of computational methods is important. A low, 4.2 kcal/mol barrier to rotation exists for a beta-ring. An 8.3 kcal/mol barrier exists for rotation of an epsilon-ring. Rotation of the epsilon-ring is sensitive to substitution at C3. In the absence of external forces neither beta- nor epsilon-rings are rotationally constrained. The nearly parallel alignment of the beta-ring to the C6C7 bond axis contrasts to the more perpendicular orientation of the epsilon-ring. Flexion of a beta-ring to the minimized epsilon-ring conformation requires approximately 23 kcal/mol; extension of the epsilon-ring to the minimized beta-ring conformation requires approximately 8 kcal/mol. Selectivity associated with beta- versus epsilon-rings is dominated by the inability of the beta-ring to flex to minimize protein/ring steric interactions and maximize van der Waal's attractions with the binding site.