Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Marianne Kuuslahti"'
Autor:
Ashok Aspatwar, Harlan Barker, Heidi Aisala, Ksenia Zueva, Marianne Kuuslahti, Martti Tolvanen, Craig R. Primmer, Jaakko Lumme, Alessandro Bonardi, Amit Tripathi, Seppo Parkkila, Claudiu T. Supuran
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 37, Iss 1, Pp 1577-1586 (2022)
A β-class carbonic anhydrase (CA, EC 4.2.1.1) was cloned from the genome of the Monogenean platyhelminth Gyrodactylus salaris, a parasite of Atlantic salmon. The new enzyme, GsaCAβ has a significant catalytic activity for the physiological reaction
Externí odkaz:
https://doaj.org/article/bdf016d9e23e49eba9c8db7310530d47
Publikováno v:
BMC Genomics, Vol 21, Iss 1, Pp 1-8 (2020)
Abstract Background The inaccuracy of DNA sequence data is becoming a serious problem, as the amount of molecular data is multiplying rapidly and expectations are high for big data to revolutionize life sciences and health care. In this study, we inv
Externí odkaz:
https://doaj.org/article/5d93c63f5dad41ec9f9f0837e8ad8fe4
Autor:
Linda J. Urbanski, Silvia Bua, Andrea Angeli, Marianne Kuuslahti, Vesa. P. Hytönen, Claudiu T. Supuran, Seppo Parkkila
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 35, Iss 1, Pp 1834-1839 (2020)
This paper presents the production and kinetic and inhibitory characterisation of β-carbonic anhydrase from the opportunistic bacterium Staphylococcus aureus (SauBCA). From the eight different carbonic anhydrase (CA) families known to date, humans h
Externí odkaz:
https://doaj.org/article/290ba6c7433f4c6483a56ded8286952c
Autor:
Linda J. Urbański, Anna Di Fiore, Latifeh Azizi, Vesa P. Hytönen, Marianne Kuuslahti, Martina Buonanno, Simona M. Monti, Andrea Angeli, Reza Zolfaghari Emameh, Claudiu T. Supuran, Giuseppina De Simone, Seppo Parkkila
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 35, Iss 1, Pp 1292-1299 (2020)
We report the biochemical and structural characterisation of a beta-carbonic anhydrase (β-CA) from Trichomonas vaginalis, a unicellular parasite responsible for one of the world’s leading sexually transmitted infections, trichomoniasis. CAs are ub
Externí odkaz:
https://doaj.org/article/bb522e938cd9481cb5e365a4cda810fe
Autor:
Helen Zirnask, Pasi Pöllanen, Siim Suutre, Marianne Kuuslahti, Andres Kotsar, Tomi Pakarainen, Kersti Kokk
Publikováno v:
Journal of Men's Health, Vol 15, Iss 4 (2019)
The aim of this study is to investigate the expression of adenosine 3',5'-cyclic monophosphate (cAMP) and cAMP-response element-binding protein (CREB) in the human penis as it is known that luteinizing hor-mone (LH) regulates cellular function mostly
Externí odkaz:
https://doaj.org/article/6fdf82f7963c439faf269544a5a7fcb7
Publikováno v:
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 33, Iss 1, Pp 359-363 (2018)
An anion inhibition study of the β-class carbonic anhydrase, AgaCA, from the malaria mosquito Anopheles gambiae is reported. A series of simple as well as complex inorganic anions, and small molecules known to interact with CAs were included in the
Externí odkaz:
https://doaj.org/article/93dddfafe6bf4e91bd5e98d95feb9688
Autor:
Reza Zolfaghari Emameh, Marianne Kuuslahti, Daniela Vullo, Harlan R. Barker, Claudiu T. Supuran, Seppo Parkkila
Publikováno v:
Parasites & Vectors, Vol 8, Iss 1, Pp 1-10 (2015)
Abstract Background A parasitic roundworm, Ascaris lumbricoides, is the causative agent of ascariasis, with approximately 760 million cases around the world. Helminthic infections occur with a high prevalence mostly in tropical and developing xcountr
Externí odkaz:
https://doaj.org/article/5119e1abbdd24317887f27060a6a3cd0
Publikováno v:
Metabolites, Vol 9, Iss 2, p 26 (2019)
The β-carbonic anhydrase (CA, EC 4.2.1.1) from the pathogenic protozoan Entamoeba histolytica, EhiCA, was investigated for its activation with a panel of natural and non-natural amino acids and amines. EhiCA was potently activated by D-His, D-Phe, D
Externí odkaz:
https://doaj.org/article/295cc9a16a82423083847f8afbecadb8
Publikováno v:
International Journal of Molecular Sciences, Vol 19, Iss 12, p 3946 (2018)
A newly described β-carbonic anhydrase (CA, EC 4.2.1.1) from the pathogenic protozoan Entamoeba histolytica, EhiCA, was recently shown to possess a significant catalytic activity for the physiologic CO2 hydration reaction (kcat of 6.7 × 105 s−1 a
Externí odkaz:
https://doaj.org/article/485ab127403d4684a69ae30b1c6a6069
Publikováno v:
Molecules, Vol 23, Iss 12, p 3112 (2018)
We report the cloning and catalytic activity of a β-carbonic anhydrase (CA, EC 4.2.1.1), isolated from the pathogenic protozoan Entamoeba histolytica, EhiCA. This enzyme has a high catalytic activity for the physiologic CO2 hydration reaction, with
Externí odkaz:
https://doaj.org/article/41785ea81f3d4050aa8caf490b164921