Articles by Melissa V. Fernandez in JoVE
激活和NLRP3炎性活性的人单核细胞来源的树突状细胞用IL-1β测量 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 树突状细胞（DC）分泌IL-1β响应于TLR8识别合成嘌呤，R848，接着NLRP3炎性体激活与尼日利亚菌素，因此，IL-1β可以用来测量NLRP3炎性活性。细胞内细胞因子染色法，免疫印迹和ELISA法用于准确地测量通过IL-1β表达NLRP3炎性引发和活化。
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.