Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Elena V. Usova"'
Autor:
Elena V. Usova, Guirec Y. Cosquer, Youngjoo Byun, Ashraf S. Al-Madhoun, Rohit Tiwari, Achintya K. Bandyopadhyaya, Jayaseharan Johnsamuel, Staffan Eriksson, Sureshbabu Narayanasamy, B. T. S. Thirumamagal, Werner Tjarks, Junhua Yan
Publikováno v:
Bioorganic & Medicinal Chemistry. 14:6886-6899
Five novel 3-carboranyl thymidine analogues (3CTAs) were designed and synthesized for boron neutron capture therapy (BNCT) of cancer. Phosphorylation of all five 3CTAs was catalyzed by recombinant human thymidine kinase (hTK1) using adenosine triphos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b3da9c24537a5ae3cd1d5c9ef5da254
https://doi.org/10.1016/j.bmc.2006.06.039
https://doi.org/10.1016/j.bmc.2006.06.039
Publikováno v:
Journal of Molecular Biology. 344:1347-1358
Human deoxycytidine kinase (dCK) is a key enzyme in the 5′-phosphorylation of purine and pyrimidine deoxynucleosides with deoxycytidine as the most efficient substrate. The ability of dCK to degrade 2′-deoxyribonucleosides to free nucleobases and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b08351552b2fbf2a71f86b599f88805
https://doi.org/10.1016/j.jmb.2004.10.016
https://doi.org/10.1016/j.jmb.2004.10.016
Autor:
Staffan Eriksson, Elena V. Usova
Publikováno v:
Biochemical Pharmacology. 64:1559-1567
Deoxycytidine kinase (dCK) is a salvage pathway enzyme that can phosphorylate both pyrimidine and purine deoxynucleosides, including important antiviral and cytostatic agents. Earlier studies showed that there are differences in kinetic properties be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a12010a8671c816db2fcd7576b54b8d7
https://doi.org/10.1016/s0006-2952(02)01389-8
https://doi.org/10.1016/s0006-2952(02)01389-8
Autor:
G H Morrison, Subhash Chandra, Elena V. Usova, A. J. Lunato, Weihua Ji, Q Li, Werner Tjarks, C Boyer, Jianghai Wang, Staffan Eriksson, Jin-Cong Zhuo, Guirec Y. Cosquer
Publikováno v:
Nucleosides, Nucleotides and Nucleic Acids. 20:695-698
Several N-3 substituted carboranyl Thd analogs were synthesized. These agents as well as some non-boronated nucleosides were evaluated in phosphoryl transfer assays with recombinant human TK1 and TK2. For some carboranyl thymidine analogs, TK1 phosph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0eba1064e3fb9dbaf7c42e0302b7f516
https://doi.org/10.1081/ncn-100002353
https://doi.org/10.1081/ncn-100002353
Autor:
Tatiana Maltseva, András Földesi, Jyoti Chattopadhayaya, Staffan Eriksson, Elena V. Usova, J Milecki
Publikováno v:
Nucleosides, Nucleotides and Nucleic Acids. 20:1225-1228
The structures of the bound 13C/2H double-labelled 2'(R/S), 5'(R/S)-2H2-1',2',3',4',5'-13C5-2'-deoxyadenosine and the corresponding 2'-deoxycytidine moieties in the complexes with human deoxycytidine kinase (dCK) have been characterized for the first
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18a1485fa31882fedaadcdbb215780c5
https://doi.org/10.1081/ncn-100002523
https://doi.org/10.1081/ncn-100002523
Autor:
J Milecki, Tatiana Maltseva, Jyoti Chattopadhayaya, A Eriksson, András Földesi, Elena V. Usova
Publikováno v:
Journal of the Chemical Society, Perkin Transactions 2. :2199-2207
13 C5)-2-deoxyadenosine (dAdo) and the corresponding 2-deoxycytidine (dCyd) moieties in the complexes with human recombinant deoxycytidine kinase (dCK) have been characterized for the first time by solution NMR spectroscopy. Transferred dipole-dipole
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3dac18058b0641d6f5b4fc4cc53d94b5
https://doi.org/10.1039/b005732k
https://doi.org/10.1039/b005732k
Autor:
Elena V. Usova, Staffan Eriksson
Publikováno v:
European Journal of Biochemistry. 248:762-766
Deoxycytidine kinase (dCK) is a salvage pathway enzyme with broad substrate specificity that can phosphorylate both pyrimidine and purine deoxynucleosides, including important antiviral and cytostatic agents. The kinetic behaviour of dCK is complex w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95fa9d18a4e2c720d71f75fd44ee0dfc
https://doi.org/10.1111/j.1432-1033.1997.t01-2-00762.x
https://doi.org/10.1111/j.1432-1033.1997.t01-2-00762.x
Autor:
Anniek De Witte, Michael R. Irwin, Nicole Inocencio, Mark D. Smith, Ezra Tai, Isabel Najera, Genadiy Kalayanov, Nick Cammack, Joseph A. Martin, Tatiana Maltseva, David Bernard Smith, Sophie Le Pogam, Han Ma, Nils Gunnar Johansson, Elena V. Usova, Wen-Rong Jiang, Sushmita Chanda, Vincent Leveque, Staffan Eriksson, Klaus Klumpp, Sonal Rajyaguru, Christian Sund, André Alker, Anna Winqist
Publikováno v:
The Journal of biological chemistry. 283(4)
RNA polymerases effectively discriminate against deoxyribonucleotides and specifically recognize ribonucleotide substrates most likely through direct hydrogen bonding interaction with the 2'-alpha-hydroxy moieties of ribonucleosides. Therefore, ribon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0af6020ae83cb04df5bb019ff05cf9a7
https://pubmed.ncbi.nlm.nih.gov/18003608
https://pubmed.ncbi.nlm.nih.gov/18003608
Publikováno v:
Biochemistry. 45(11)
Human deoxycytidine kinase (dCK) phosphorylates both pyrimidine and purine deoxynucleosides, including numerous nucleoside analogue prodrugs. Energy transfer studies of transfer between Trp residues of dCK and the fluorescent probe N-(1-pyrene)maleim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e47a41a10ab16ebcaea053cddd6d4158
https://pubmed.ncbi.nlm.nih.gov/16533034
https://pubmed.ncbi.nlm.nih.gov/16533034
Publikováno v:
Nucleosides, nucleotidesnucleic acids. 23(8-9)
Deoxycytidine kinase (dCK), is responsible for the phosphorylation of deoxynucleosides to the corresponding monophosphates using ATP or UTP as phosphate donors. Steady-state intrinsic fluorescence measurements were used to study interaction of dCK wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::75a987764b63b138355cc315327c7e0d
https://pubmed.ncbi.nlm.nih.gov/15571255
https://pubmed.ncbi.nlm.nih.gov/15571255