Zobrazeno 1 - 10
of 49
pro vyhledávání: '"Natalia K. Nagradova"'
Autor:
Natalia K. Nagradova
Publikováno v:
Biochemistry (Moscow). 69:830-843
The mechanisms responsible for protein folding in the cell can be divided in two groups. The ones in the first group would be those preventing the aggregation of unfolded polypeptide chains or of incompletely folded proteins, as well as the mechanism
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3e9986c8fe4f90e54bbfff1fe2b7a7c
https://doi.org/10.1023/b:biry.0000040214.43943.9a
https://doi.org/10.1023/b:biry.0000040214.43943.9a
Publikováno v:
Biochemistry. 41:7556-7564
Tetrameric phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Bacillus stearothermophilus can be described as a dimer of dimers with three nonequivalent interfaces. To investigate the contribution of intra- and intersubunit interac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3920589ebd22e3867c3f5793977dc32c
https://doi.org/10.1021/bi012084+
https://doi.org/10.1021/bi012084+
Autor:
Natalia K. Nagradova
Publikováno v:
Biochemistry (Moscow). 67:839-849
In the process of oligomeric structure formation through a mechanism of three-dimensional domain swapping, one domain of a monomeric protein is replaced by the same domain from an identical monomer. The swapped “domain” can represent an entire te
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3a5ac9192d4de2eb3829e1589850470d
https://doi.org/10.1023/a:1019958402194
https://doi.org/10.1023/a:1019958402194
Autor:
Natalia K. Nagradova
Publikováno v:
Biochemistry (Moscow). 66:1067-1076
The properties of the active center of phosphorylating D-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) are considered with emphasis on the structure of anion-binding sites and their role in catalysis. The results of studies on the molecular mechan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7e566607ae8232445f1804dfa07d2a8e
https://doi.org/10.1023/a:1012472627801
https://doi.org/10.1023/a:1012472627801
Publikováno v:
FEBS Letters. 432:187-190
PC12 cells permeabilized with a low concentration of digitonin (5 μM) under controlled conditions were loaded with monoclonal antibodies (MoAb) against the regulatory subunit type II (RII) of cAMP-dependent protein kinase. After digitonin removal fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a42048e8b774f9f399f12b507606eabe
https://doi.org/10.1016/s0014-5793(98)00861-8
https://doi.org/10.1016/s0014-5793(98)00861-8
Publikováno v:
FEBS Letters. 414:247-252
Incubation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) with micromolar hydrogen peroxide concentrations does not alter the catalytic properties of GAPDH in the reaction of oxidative phosphorylation of glyceraldehyde-3-phosphate, but endows th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28a53a723671c930bd85399ce6bdf71a
https://doi.org/10.1016/s0014-5793(97)01044-2
https://doi.org/10.1016/s0014-5793(97)01044-2
Autor:
Denis Arutyunov, Vladimir I. Muronetz, Sophie Rahuel-Clermont, Guy Branlant, Elena V. Schmalhausen, Natalia K. Nagradova, Victor N. Orlov
Publikováno v:
Biochemistry and Cell Biology
Biochemistry and Cell Biology, NRC Research Press, 2013, 91 (5), pp.295-302. ⟨10.1139/bcb-2012-0104⟩
Biochemistry and Cell Biology, NRC Research Press, 2013, 91 (5), pp.295-302. ⟨10.1139/bcb-2012-0104⟩
International audience; La calorimétrie différentielle à balayage adiabatique a été utilisée afin d’examiner l’effet du NADP+ sur la dénaturation thermique irréversible de la glycéraldéhyde-3-phosphate déshydrogénase non phosphorylant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dbdbce8ae1d29e78d7a4ddea306381ea
https://pubmed.ncbi.nlm.nih.gov/24032678
https://pubmed.ncbi.nlm.nih.gov/24032678
Publikováno v:
Biochemical and Biophysical Research Communications. 187:577-583
Modification of a single arginine residue per subunit of rabbit muscle apo-D-Glyceraldehyde-3-phosphate dehydrogenase does not affect the rate of hydrolysis of p-nitrophenyl acetate catalyzed by the enzyme, but locks the tetramer in a conformation wh
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9491a9b25d0c19da2d18e07ef7f9d43a
https://doi.org/10.1016/0006-291x(92)91233-g
https://doi.org/10.1016/0006-291x(92)91233-g
Publikováno v:
Biochemistry. Biokhimiia. 71(6)
Polyclonal antibodies produced after the immunization of a rabbit with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Bacillus stearothermophilus were used to isolate two types of antibodies interacting with different non-native forms of the a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edcd67548b933a80e05bf77ccfac8147
https://pubmed.ncbi.nlm.nih.gov/16827661
https://pubmed.ncbi.nlm.nih.gov/16827661
Publikováno v:
FEBS Letters. 375:18-20
Incorporation of l -[ 35 S]cysteine into rabbit muscle glyceraldehyde-3-phosphate dehydrogenase was detected following incubation of the enzyme in a mixture containing glyceraldehyde-3-phosphate, NAD + and the labeled cysteine. Insignificant binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ddd7cc3b0b97f179f14d611fddfa4975
https://doi.org/10.1016/0014-5793(95)01151-4
https://doi.org/10.1016/0014-5793(95)01151-4