O
Olga Kifor
Researcher at Brigham and Women's Hospital
Publications - 68
Citations - 11596
Olga Kifor is an academic researcher from Brigham and Women's Hospital. The author has contributed to research in topics: Calcium-sensing receptor & Parathyroid chief cell. The author has an hindex of 51, co-authored 68 publications receiving 11241 citations. Previous affiliations of Olga Kifor include Harvard University & University of Picardie Jules Verne.
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Journal ArticleDOI
Filamin-A Binds to the Carboxyl-terminal Tail of the Calcium-sensing Receptor, an Interaction That Participates in CaR-mediated Activation of Mitogen-activated Protein Kinase
TL;DR: The binding of the CaR's COOH-terminal tail to filamin-A may contribute to its localization in caveolae, link it to the actin-based cytoskeleton, and participate in CaR-mediated activation of MAPK.
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In vivo and in vitro characterization of neonatal hyperparathyroidism resulting from a de novo, heterozygous mutation in the Ca2+-sensing receptor gene: normal maternal calcium homeostasis as a cause of secondary hyperparathyroidism in familial benign hypocalciuric hypercalcemia.
Mei Bai,Simon H. S. Pearce,Olga Kifor,Sunita Trivedi,U. G. Stauffer,Rajesh V. Thakker,Edward M. Brown,Beat Steinmann +7 more
TL;DR: This de novo, heterozygous CaR mutation may exert a dominant negative action on the normal CaR, producing NHPT and more severe hypercalcemia than typically seen with FBHH.
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The calcium sensing receptor is directly involved in both osteoclast differentiation and apoptosis
R. Mentaverri,R. Mentaverri,Shozo Yano,Naibedya Chattopadhyay,L. Petit,Olga Kifor,Olga Kifor,Said Kamel,Ernest F. Terwilliger,Michel Brazier,Edward M. Brown +10 more
TL;DR: It is suggested that stimulation of the CaR may play a pivotal role in the control of both osteoclast differentiation and apoptosis in the systems studied here through a signaling pathway involving activation of theCaR, phospholipase C, and NF‐κB.
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Functional characterization of calcium-sensing receptor mutations expressed in human embryonic kidney cells.
TL;DR: It is demonstrated that mutations which enhance or reduce the responsiveness of the CaR to [Ca2+]o cause the disorders ADH, FBH, and NSHPT, respectively.
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Intermolecular interactions between dimeric calcium-sensing receptor monomers are important for its normal function.
TL;DR: The study suggests that intermolecular interactions within the dimeric CaR are important for the receptor's function, and suggests that the CaR has at least two functionally separable domains.