Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Viatcheslav Zaitsev"'
Publikováno v:
Academia Letters.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fcf284a242bccc72d93834668737f8c7
https://doi.org/10.20935/al3232
https://doi.org/10.20935/al3232
Autor:
Viatcheslav Zaitsev
Publikováno v:
Academia Letters.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::56a41483832cab2eca1ab8820a054f5f
https://doi.org/10.20935/al2579
https://doi.org/10.20935/al2579
Autor:
Matthias Reher, Garry L. Taylor, Michael J. Danson, Viatcheslav Zaitsev, Susan J. Crennell, Ulrike Johnsen, Peter Schönheit, Marius Ortjohann
Publikováno v:
Biochemistry. 57:3797-3806
The thermoacidophilic archaea Picrophilus torridus and Sulfolobus solfataricus catabolize glucose via a nonphosphorylative Entner–Doudoroff pathway and a branched Entner–Doudoroff pathway, respecti...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::21ac4e7e27f22b2f195ebd6f08f97370
https://doi.org/10.1021/acs.biochem.8b00535
https://doi.org/10.1021/acs.biochem.8b00535
Autor:
Viatcheslav, Zaitsev, Ulrike, Johnsen, Matthias, Reher, Marius, Ortjohann, Garry L, Taylor, Michael J, Danson, Peter, Schönheit, Susan J, Crennell
Publikováno v:
Biochemistry. 57(26)
The thermoacidophilic archaea Picrophilus torridus and Sulfolobus solfataricus catabolize glucose via a nonphosphorylative Entner-Doudoroff pathway and a branched Entner-Doudoroff pathway, respectively. Key enzymes for these Entner-Doudoroff pathways
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::db69fd16cf23188ac6b02d36a4837df8
https://pubmed.ncbi.nlm.nih.gov/29812914
https://pubmed.ncbi.nlm.nih.gov/29812914
Autor:
Peter F. Lindley, Viatcheslav Zaitsev
Publikováno v:
Acta Crystallographica Section A Foundations and Advances. 75:e192-e192
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::84b26f780a11271e44444f02683001be
https://doi.org/10.1107/s2053273319093641
https://doi.org/10.1107/s2053273319093641
Autor:
Azat Gabdulkhakov, Al'bert M. Mikhailov, A. V. Lyashenko, Elena V. Stepanova, I. Bento, Vladimir I. Tishkov, Yu. N. Zhukova, N. E. Zhukhlistova, Ch. Betzel, P. F. Lindley, E. Yu. Morgunova, O. V. Koroleva, Wolfang Voelter, Galina S. Kachalova, Viatcheslav Zaitsev
Publikováno v:
Crystallography Reports. 51:817-823
Laccase (oxygen oxidoreductase, EC 1.14.18.1) belongs to the copper-containing oxidases. This enzyme catalyzes reduction of molecular oxygen by different organic and inorganic compounds to water without the formation of hydrogen peroxide. The three-d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cb21c0aa989857b2242fbaecc98d35d8
https://doi.org/10.1134/s1063774506050117
https://doi.org/10.1134/s1063774506050117
Autor:
A. V. Lyashenko, O. V. Koroleva, Wolfang Voelter, Galina S. Kachalova, Vladimir I. Tishkov, Yuliya N. Zhukova, Viatcheslav Zaitsev, Victor S. Lamzin, Ekaterina Morgunova, Isabel Bento, Peter F. Lindley, Christian Betzel, Elena V. Stepanova, Al'bert M. Mikhailov, Katja Schirwitz, A.G. Gabdoulkhakov, Nadegda E. Zhukhlistova, Evgeniy A. Cherkashyn
Publikováno v:
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
The crystallization and preliminary X-ray structure at 1.9 Å resolution of the fungal laccase from C. maxima are presented.
Laccases are members of the blue multi-copper oxidase family that oxidize substrate molecules by accepting electrons at
Laccases are members of the blue multi-copper oxidase family that oxidize substrate molecules by accepting electrons at
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ae8c4a92b2efdc4e1660cd79112a3a5
http://europepmc.org/articles/PMC2225196
http://europepmc.org/articles/PMC2225196
Autor:
Mark von Itzstein, Garry L. Taylor, Allen Portner, Viatcheslav Zaitsev, Darrin R. Groves, Toru Takimoto, Milton J. Kiefel
Publikováno v:
Journal of Virology. 78:3733-3741
Paramyxoviruses are the leading cause of respiratory disease in children. Several paramyxoviruses possess a surface glycoprotein, the hemagglutinin-neuraminidase (HN), that is involved in attachment to sialic acid receptors, promotion of fusion, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0acad400a8dc4cecf507bc5991380cbc
https://doi.org/10.1128/jvi.78.7.3733-3741.2004
https://doi.org/10.1128/jvi.78.7.3733-3741.2004
Autor:
Vladimir I. Tishkov, Ekaterina Morgunova, Christian Betzel, Elena V. Stepanova, A. V. Lyashenko, O. V. Koroleva, Galina S. Kachalova, Wolfgang Voelter, Yuliya N. Zhukova, Isabel Bento, Peter F. Lindley, Viatcheslav Zaitsev, N. E. Zhukhlistova, Victor S. Lamzin, A.G. Gabdoulkhakov, Al 'Bert M Mikhailov
Publikováno v:
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry. 11(8)
Laccases are members of the blue multi-copper oxidase family. These enzymes oxidize substrate molecules by accepting electrons at a mononuclear copper centre and transferring them to a trinuclear centre. Dioxygen binds to the trinuclear centre and fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a8a26cba919b39211c09f6112ea6a6a
https://pubmed.ncbi.nlm.nih.gov/16944230
https://pubmed.ncbi.nlm.nih.gov/16944230
Autor:
Robert Charles Hunter
Have you ever been thinking about someone and they call? Or a package arrives from them? That's synchronicity. If it's happened to you, you've already stepped into the land of the New Age. If not and you want to know what others are talking about, th
