Zobrazeno 1 - 10
of 72
pro vyhledávání: '"Purine-nucleoside phosphorylase activity"'
Publikováno v:
Analytica chimica acta. 1139
Several novel non-typical nucleoside analogs were examined as potential fluorescent indicators of purine-nucleoside phosphorylase (PNP) activity in human blood. The substrates included N7-riboside of 8-aza-2,6-diaminopurine, N6-riboside of 1,N6-ethen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b3d46a38b714d03bb359a3a36aa35f7
https://pubmed.ncbi.nlm.nih.gov/33190694
https://pubmed.ncbi.nlm.nih.gov/33190694
Autor:
M. Mamus, E. Mozgovaya, Ekaterina Tikhomirova, A. S. Trofimenko, S.A. Bedina, S.S. Spitsina, I.A. Zborovskaya
Publikováno v:
Abstracts Accepted for Publication.
Background: Cytotoxic immunosuppressants are widely used nowadays for outcome improvement and better quality of life in severe systemic lupus erythematosus (SLE). As purine and pyrimidine metabolism suggest to be the major targets of most cytotoxic i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::84209f2acf52d32a2b2eb130c150eda7
https://doi.org/10.1136/annrheumdis-2019-eular.4622
https://doi.org/10.1136/annrheumdis-2019-eular.4622
Autor:
Francesco Caciagli, Patricia Giuliani, Mariachiara Zuccarini, Antonio Marzo, Patrizia Di Iorio, Silvana Buccella, Matteo Marzo, Iolanda D'Alimonte, Renata Ciccarelli, Margherita Rossini
Publikováno v:
Journal of Chromatography B. :114-121
Purine nucleoside phosphorylase (PNP) activity is involved in cell survival and function, since PNP is a key enzyme in the purine metabolic pathway where it catalyzes the phosphorolysis of the nucleosides to the corresponding nucleobases. Its dysfunc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d867e4bc215bfdb824640d125ac59928
https://doi.org/10.1016/j.jchromb.2015.12.012
https://doi.org/10.1016/j.jchromb.2015.12.012
Autor:
Anna Modrak-Wójcik, Beata Wielgus-Kutrowska, Alicja Dyzma, Agnieszka Bzowska, Michal Zolkiewski, Katarzyna Breer
Publikováno v:
Archives of Biochemistry and Biophysics. 549:40-48
Homotrimeric mammalian purine nucleoside phosphorylase (PNP) plays a key role in the nucleoside and nucleotide metabolic salvage pathway. Each monomer in the active PNP trimer is composed of a central β-sheet flanked by several α-helices. We invest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a84ecbc1f38885186cf60d6b88d08717
https://doi.org/10.1016/j.abb.2014.03.009
https://doi.org/10.1016/j.abb.2014.03.009
Autor:
R. G. Da Silva, Luiz Augusto Basso, L. Ayub, D.S. Santos, L. C. C. Filho, Eraldo L. Batista, Candida Deves
Publikováno v:
Journal of Periodontal Research. 45:664-671
Batista EL Jr, Deves C, Ayub L, da Silva RG, Filho LCC, Basso LA, Santos DS. Purine nucleoside phosphorylase activity and expression are upregulated in sites affected by periodontal disease. J Periodont Res 2010; 45: 664–671. © 2010 John Wiley & S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3ea10553a17a6cc78a108d0c76af0f13
https://doi.org/10.1111/j.1600-0765.2010.01282.x
https://doi.org/10.1111/j.1600-0765.2010.01282.x
Publikováno v:
Biosensors and Bioelectronics. 25:1032-1036
In this paper, an electrochemical biosensor to assay purine nucleoside phosphorylase (PNP) activity is reported. Due to the facilitation of sliver nanoparticles, which are modified on an electrode surface, to the electron transfer reactivity of guano
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::963881c09290ee1ec698e4140daf091d
https://doi.org/10.1016/j.bios.2009.09.021
https://doi.org/10.1016/j.bios.2009.09.021
Autor:
E. M. Tucker, J. D. Young
Publikováno v:
Animal Blood Groups and Biochemical Genetics. 7:109-117
Summary The purine nucleoside phosphorylase (NP) activity of sheep red cells was determined by starch gel electrophoresis and by a spectrophotometric assay technique. Some sheep had high activity (NP-high type) and some had low or zero activity (NP-l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7be1e1d55ae8a8aa1e7e95cfbc2d14b3
https://doi.org/10.1111/j.1365-2052.1976.tb01384.x
https://doi.org/10.1111/j.1365-2052.1976.tb01384.x
Autor:
Colin G. N. Turnbull, Celia M. James, Barbara J. Warnes, Jennifer R. Bromley, David E. Hanke, Christine A. Newell, Jamie C. P. Thomson
Publikováno v:
The Biochemical journal. 458(2)
StCKP1 (Solanum tuberosum cytokinin riboside phosphorylase) catalyses the interconversion of the N9-riboside form of the plant hormone CK (cytokinin), a subset of purines, with its most active free base form. StCKP1 prefers CK to unsubstituted aminop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d062c6a4456c156fd9e4d664ba1d3c3e
https://pubmed.ncbi.nlm.nih.gov/24325449
https://pubmed.ncbi.nlm.nih.gov/24325449
Autor:
Hajime Nakae, Michihiko Kitamura, Hiroyuki Suzuki, Hideo Inaba, Satoshi Saito, Shuichi Kamata, Yoshihiro Minamiya, Satoru Motoyama, Reijiro Saito, Jun-ichi Ogawa
Publikováno v:
Liver. 20:200-208
Aims/background Rat liver perfused with an oxygenated buffered solution alone results in degenerative changes even when the perfusion flow is accelerated to give a sufficient oxygen supply. On the other hand, perfusion media supplemented with red blo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::76348f90e20ad750b0bff3d05731727e
https://doi.org/10.1034/j.1600-0676.2000.020003200.x
https://doi.org/10.1034/j.1600-0676.2000.020003200.x
Autor:
David W. Parkin
Publikováno v:
Journal of Biological Chemistry. 271:21713-21719
Trypanosomes have no de novo purine biosynthesis and thus depend upon salvage pathways to obtain purines for their metabolic pathways and for the biosynthesis of nucleic acids. An inosine-adenosine-guanosine preferring nucleoside hydrolase (IAG-nucle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::75e43bb3e4b1ce41d25ea6631e758b56
https://doi.org/10.1074/jbc.271.36.21713
https://doi.org/10.1074/jbc.271.36.21713