Zobrazeno 1 - 10
of 93
pro vyhledávání: '"Yannis D. Clonis"'
Autor:
Michael Karpusas, Irine Axarli, Lykourgos Chiniadis, Athanasios Papakyriakou, Kostas Bethanis, Katholiki Scopelitou, Yannis D Clonis, Nikolaos E Labrou
Publikováno v:
PLoS ONE, Vol 8, Iss 2, p e56337 (2013)
Glutathione transferases (GSTs) are enzymes that contribute to cellular detoxification by catalysing the nucleophilic attack of glutathione (GSH) on the electrophilic centre of a number of xenobiotic compounds, including several chemotherapeutic drug
Externí odkaz:
https://doaj.org/article/bb5eeee6130443a781e0b3d0a368e240
Autor:
Yannis D. Clonis
Publikováno v:
Separation Processes in Biotechnology
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::dd785e8d57482a991865b7eaac2c25f2
https://doi.org/10.1201/9781003066392-17
https://doi.org/10.1201/9781003066392-17
Autor:
Trias Thireou, Paul Cordopatis, Nikolaos E. Labrou, Nikolaos Georgakis, Elias Eliopoulos, Eleni V. Pappa, Yannis D. Clonis, Aikaterini A. Zompra
Publikováno v:
Biopolymers. 106:330-344
Glutathione (GSH) structure-guided tripeptide analogues were designed and synthesized by solid phase technology, purified (≥95%) by RP and/or GF column chromatography, to identify those that, compared with GSH, exhibited similar or higher binding a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::819ceda9c0a86b76083dee03ae8e8296
https://doi.org/10.1002/bip.22844
https://doi.org/10.1002/bip.22844
Autor:
Elias Eliopoulos, Trias Thireou, Nikolaos E. Labrou, Nikolaos Georgakis, Dionisis A. Karagiannopoulos, Petros G. Tsoungas, Yannis D. Clonis, Michael Koutsilieris
Publikováno v:
Chemical biologydrug design. 90(5)
A series of 2,2′-dihydroxybenzophenones and their carbonyl N-analogues were studied as potential inhibitors against human glutathione transferase M1-1 (hGSTM1-1) purified from recombinant E. coli. Their screening revealed an inhibition against hGST
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09980d42270e0c3f84eabed471492d42
https://pubmed.ncbi.nlm.nih.gov/28440951
https://pubmed.ncbi.nlm.nih.gov/28440951
Publikováno v:
Journal of Chromatographic Science. 48:496-502
Reverse transcriptase (RT) catalyzes the formation of dsDNA from single-stranded retroviral RNA genome. This enzyme is unique among DNA polymerases in its ability to use either RNA or DNA as a template. Moloney Murine Leukemia virus reverse transcrip
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::404cdeae3ee0cc4bb5bb99f3ab686002
https://doi.org/10.1093/chromsci/48.6.496
https://doi.org/10.1093/chromsci/48.6.496
Publikováno v:
Journal of Chromatography A. 1122:63-75
The commercial availability of DNA polymerases has revolutionized molecular biotechnology and certain sectors of the bio-industry. Therefore, the development of affinity adsorbents for purification of DNA polymerases is of academic interest and pract
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::95ee91b41f4ab6de4550f9ff2811677e
https://doi.org/10.1016/j.chroma.2006.04.044
https://doi.org/10.1016/j.chroma.2006.04.044
Publikováno v:
Biomolecular Engineering. 22:121-128
Glutathione S -transferases (GSTs, EC 2.5.1.18) are a multigene family of detoxification enzymes that biotransform a wide variety of endogenous and exogenous electrophilic substrates, including herbicides. The isozyme GST I from maize exhibits signif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad520dd5ba8cd2e68f76e63161cb3dc6
https://doi.org/10.1016/j.bioeng.2005.03.001
https://doi.org/10.1016/j.bioeng.2005.03.001
Publikováno v:
Protein Engineering Design and Selection. 17:741-748
Glutathione S-transferases (GSTs) are a heterogeneous family of enzymes that catalyse the conjugation of glutathione (GSH) to electrophilic sites on a variety of hydrophobic substrates. In the present study three amino acid residues (Trp12, Phe35 and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f241b9dc4ddd2f8d166aa598aea879f5
https://doi.org/10.1093/protein/gzh086
https://doi.org/10.1093/protein/gzh086
Publikováno v:
Journal of Chromatography B. 807:277-285
Glutamate oxidase (GOX, EC 1.4.3.11) from Streptomyces catalyses the oxidation of L-glutamate to alpha-ketoglutarate. Its kinetic constants for L-glutamate were measured equal to 2 mM for Km and 85.8 s(-1) for kcat. BLAST search and amino acid sequen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8fa43aa191d5976eb8f41a5265a07968
https://doi.org/10.1016/j.jchromb.2004.04.032
https://doi.org/10.1016/j.jchromb.2004.04.032
Publikováno v:
Biomolecular Engineering. 21:61-66
The optimisation of enzymes for particular application or conditions remains an important target in all protein engineering endeavours. Here, we report a successful strategy for altering the pH-profile of kinetic parameters and to define in detail th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e5496609588824727c058547334831b5
https://doi.org/10.1016/j.bioeng.2003.10.002
https://doi.org/10.1016/j.bioeng.2003.10.002