Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Anu Salminen"'
Autor:
Viktor A. Anashkin, Anu Salminen, Ekaterina Osipova, Svetlana A. Kurilova, Ilia D. Deltsov, Reijo Lahti, Alexander A. Baykov
Publikováno v:
ACS Omega, Vol 4, Iss 13, Pp 15549-15559 (2019)
Externí odkaz:
https://doaj.org/article/56628028b2654ce5956e7c075fa84932
Publikováno v:
Biochemical and Biophysical Research Communications. 517:266-271
Bacterial family II pyrophosphatases (PPases) are homodimeric enzymes, with the active site located between two catalytic domains. Some family II PPases additionally contain regulatory cystathionine β-synthase (CBS) domains and exhibit positive kine
Autor:
Ekaterina A. Osipova, Viktor A. Anashkin, Anu Salminen, S. A. Kurilova, Ilia D Deltsov, Reijo Lahti, Alexander A. Baykov
Publikováno v:
ACS Omega, Vol 4, Iss 13, Pp 15549-15559 (2019)
ACS Omega
ACS Omega
Inorganic pyrophosphatase containing regulatory cystathionine β-synthase (CBS) domains (CBS-PPase) is inhibited by adenosine monophosphate (AMP) and adenosine diphosphate and activated by adenosine triphosphate (ATP) and diadenosine polyphosphates;
Publikováno v:
Archives of biochemistry and biophysics. 692
A quarter of prokaryotic Family II inorganic pyrophosphatases (PPases) contain a regulatory insert comprised of two cystathionine β-synthase (CBS) domains and one DRTGG domain in addition to the two catalytic domains that form canonical Family II PP
Publikováno v:
FEBS Letters. 591:3225-3234
Inorganic pyrophosphatases (PPases) convert pyrophosphate (PPi ) to phosphate and are present in all cell types. Soluble PPases belong to three nonhomologous families, of which Family II is found in approximately a quarter of prokaryotic organisms, o
Publikováno v:
Biochemical Journal. 473:2097-2107
Many prokaryotic soluble PPases (pyrophosphatases) contain a pair of regulatory adenine nucleotide-binding CBS (cystathionine β-synthase) domains that act as ‘internal inhibitors’ whose effect is modulated by nucleotide binding. Although such re
Autor:
Anu Salminen, Saija Kiljunen, Maria Pajunen, Harri Savilahti, Elsi Pulkkinen, Saija Haapa-Paananen, Mauno Vihinen, Lars Paulin, Tiina S Rasila, Phoebe A. Rice
Publikováno v:
Nucleic Acids Research
The phage Mu DNA transposition system provides a versatile species non-specific tool for molecular biology, genetic engineering and genome modification applications. Mu transposition is catalyzed by MuA transposase, with DNA cleavage and integration
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::633c587de09526a4cfe4b478ea758728
http://hdl.handle.net/10138/236500
http://hdl.handle.net/10138/236500
Autor:
Alexander A. Baykov, Reijo Lahti, Victor N. Orlov, Anu Salminen, Heidi Tuominen, Viktor A. Anashkin
Publikováno v:
Journal of Biological Chemistry. 290:27594-27603
Among numerous proteins containing pairs of regulatory cystathionine β-synthase (CBS) domains, family II pyrophosphatases (CBS-PPases) are unique in that they generally contain an additional DRTGG domain between the CBS domains. Adenine nucleotides
Autor:
Reijo Lahti, Anu Salminen, Heidi Tuominen, Viktor A. Anashkin, Alexander A. Baykov, Matti Lahti
Publikováno v:
Journal of Biological Chemistry. 289(33):22865-22876
Regulated family II pyrophosphatases (CBS-PPases) contain a nucleotide-binding insert comprising a pair of cystathionine β-synthase (CBS) domains, termed a Bateman module. By binding with high affinity to the CBS domains, AMP and ADP usually inhibit
Autor:
Matti Poutanen, Reena Desai, Antti Perheentupa, Mia Ståhle, Kaisa Huhtinen, David J. Handelsman, Anu Salminen
Publikováno v:
The Journal of Clinical Endocrinology & Metabolism. 97:4228-4235
Aberrant estrogen synthesis and metabolism have been suggested to increase local estradiol (E2) concentration in endometriosis and thus to promote the growth of the lesions. However, tissue estrogen concentrations within the endometrium and different