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Arnab Bhattacharjee

Researcher at University of Helsinki

Publications -  26
Citations -  2011

Arnab Bhattacharjee is an academic researcher from University of Helsinki. The author has contributed to research in topics: Factor H & Complement system. The author has an hindex of 9, co-authored 15 publications receiving 1453 citations. Previous affiliations of Arnab Bhattacharjee include Indian Institute of Science.

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A purified membrane protein from Akkermansia muciniphila or the pasteurized bacterium improves metabolism in obese and diabetic mice

TL;DR: It is shown that A. muciniphila retains its efficacy when grown on a synthetic medium compatible with human administration and enhanced its capacity to reduce fat mass development, insulin resistance and dyslipidemia in mice, and Amuc_1100, a specific protein isolated from the outer membrane of A. Sydneyi, interacts with Toll-like receptor 2, is stable at temperatures used for pasteurization and partly recapitulates the beneficial effects of the bacterium.
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Dual interaction of factor H with C3d and glycosaminoglycans in host–nonhost discrimination by complement

TL;DR: It is shown that C3d could replace glycosaminoglycan binding to FH20, thus providing a feedback control for preventing excess C3b deposition and complement amplification, and explains the molecular basis of atypical hemolytic uremic syndrome.
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Collagen structure: the Madras triple helix and the current scenario

TL;DR: Several high resolution crystal structures of oligopeptides related to collagen have been determined in the last ten years, which have confirmed the essential correctness of the coiled‐coil triple helical structure of collagen, as well as the role of water and hydroxyproline residues, but also indicated additional sequence‐dependent features.
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Microbes bind complement inhibitor factor H via a common site.

TL;DR: This study reveals that seven microbes representing different phyla utilize a common binding site on the domain 20 of FH for complement evasion, which enhances function ofFH on the microbial surfaces via the novel mechanism of tripartite complex formation.