A
Anu Salminen
Researcher at University of Turku
Publications - 28
Citations - 781
Anu Salminen is an academic researcher from University of Turku. The author has contributed to research in topics: CBS domain & Inorganic pyrophosphatase. The author has an hindex of 15, co-authored 28 publications receiving 732 citations. Previous affiliations of Anu Salminen include Moscow State University.
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Journal ArticleDOI
Endometrial and Endometriotic Concentrations of Estrone and Estradiol Are Determined by Local Metabolism Rather than Circulating Levels
Kaisa Huhtinen,Reena Desai,Mia Ståhle,Anu Salminen,David J. Handelsman,Antti Perheentupa,Antti Perheentupa,Matti Poutanen,Matti Poutanen +8 more
TL;DR: Endometrial or endometriotic tissue E2 concentrations are actively regulated by local estrogen metabolism in the tissue, and the inhibition of local E2 synthesis is a valid, novel approach to reduce local E1-dependent growth of endometiotic tissue.
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Cloning and expression of a unique inorganic pyrophosphatase from Bacillus subtilis: evidence for a new family of enzymes
Toshio Shintani,Toshio Uchiumi,Tomoki Yonezawa,Anu Salminen,Alexander A. Baykov,Reijo Lahti,Akira Hachimori +6 more
TL;DR: An open reading frame located in the COTF‐TETB intergenic region of Bacillus subtilis was cloned and expressed in Escherichia coli and shown to encode inorganic pyrophosphatase (PPase), which suggests that B. subtili PPase represents a new family of soluble PPases (a Bs family), putative members of which were found in Archaeoglobus fulgidus, Methanococcus jannaschii
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Evolutionary aspects of inorganic pyrophosphatase
Toni Sivula,Anu Salminen,Alexey N. Parfenyev,Pekka Pohjanjoki,Adrian Goldman,Barry S. Cooperman,Alexander A. Baykov,Reijo Lahti +7 more
TL;DR: Interestingly, plant pyrophosphatases bear a closer similarity to prokaryotic than to animal/fungal pyroph phosphatases, and remarkably, 15 of these residues are located at the active site.
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Crystal structure of Streptococcus mutans pyrophosphatase: a new fold for an old mechanism.
Michael C. Merckel,Igor P. Fabrichniy,Anu Salminen,Nisse Kalkkinen,Alexander A. Baykov,Reijo Lahti,Adrian Goldman +6 more
TL;DR: The first family II PPase structure has been solved by X-ray crystallography at 2.2 A resolution as mentioned in this paper, and the active site is located at the domain interface, which is a remarkable example of convergent evolution.
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Quaternary structure and metal ion requirement of family II pyrophosphatases from Bacillus subtilis, Streptococcus gordonii, and Streptococcus mutans.
Alexey N. Parfenyev,Anu Salminen,Pasi Halonen,Akira Hachimori,Alexander A. Baykov,Reijo Lahti +5 more
TL;DR: The present work cloned and overexpressed in Escherichia coli putative genes for two more family II PPases, isolated the recombinant proteins, and showed them to be highly specific and active PPases.