Shmarakov Io
Columbia University
30 Papers
121 Citations
Shmarakov Io is an academic researcher from Columbia University. The author has contributed to research in topics: Retinoid & Hepatic stellate cell. The author has an hindex of 12, co-authored 30 publications. Previous affiliations of Shmarakov Io include Chernivtsi University.
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Papers
Macrophage MerTK Promotes Liver Fibrosis in Nonalcoholic Steatohepatitis.
Bishuang Cai,Paola Dongiovanni,Kathleen E. Corey,Xiaobo Wang,Shmarakov Io,Ze Zheng,Canan Kasikara,Viralkumar Davra,Marica Meroni,Raymond T. Chung,Carla V. Rothlin,Robert F. Schwabe,William S. Blaner,Raymond B. Birge,Luca Valenti,Ira Tabas +15 more
TL;DR: It is shown that holo- or myeloid-specific Mertk targeting in NASH mice decreases liver fibrosis, congruent with the human genetic data, and a plausible mechanism underlying MERTK as a genetic risk factor for NASH fibrosis is provided.
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Vitamin A and Vitamin E: Will the Real Antioxidant Please Stand Up?
TL;DR: Vitamin A, acting through its metabolite, all-trans-retinoic acid, is a potent transcriptional regulator affecting expression levels of hundreds of genes through retinic acid response elements.
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Hepatic stellate cells are an important cellular site for β-carotene conversion to retinoid.
Shmarakov Io,Matthew K. Fleshman,Diana N. D'Ambrosio,Roseann Piantedosi,Ken M. Riedl,Steven J. Schwartz,Robert W. Curley,Johannes von Lintig,Lewis P. Rubin,Earl H. Harrison,William S. Blaner +10 more
TL;DR: In this article, the ability of stellate cells (HSCs) to metabolize β-carotene in situ has been explored, and it was shown that HSCs are an important cellular site within the liver for accumulation of dietary β-Carotene.
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Antitumor Activity of Alloy and Core-Shell-Type Bimetallic AgAu Nanoparticles.
Shmarakov Io,Iuliia Mukha,Nadiia Vityuk,Vira Borschovetska,Nelya Zhyshchynska,Galyna Ya. Grodzyuk,Anna Eremenko +6 more
TL;DR: The data suggest that in vivo antitumor activity of the studied NPs strongly depends on gold and silver interaction arising from their ordered topological distribution, which may serve as a suitable anticancerous prototype.
Retinol-binding protein 2 (RBP2) binds monoacylglycerols and modulates gut endocrine signaling and body weight.
Seung-Ah Lee,Kryscilla Jian Zhang Yang,Pierre-Jacques Brun,Josie A. Silvaroli,Jason J. Yuen,Shmarakov Io,Hongfeng Jiang,Jun B. Feranil,Xueting Li,Atreju I. Lackey,Wojciech Krezel,Rudolph L. Leibel,Jenny Libien,Judith Storch,Marcin Golczak,William S. Blaner +15 more
TL;DR: RBP2 is a previously unidentified monoacylglycerol (MAG)-binding protein, interacting with the endocannabinoid 2-arachidonoylglycersol (2-AG) and other MAGs with affinities comparable to retinol, playing a heretofore unknown role in systemic energy balance.
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