V G Grivennikova
Overview
Explore the profile of V G Grivennikova including associated specialties, affiliations and a list of published articles.
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24
Citations
287
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Recent Articles
1.
Grivennikova V, Vinogradov A
Biochemistry (Mosc)
. 2014 Feb;
78(13):1490-511.
PMID: 24490736
Numerous biochemical studies are aimed at elucidating the sources and mechanisms of formation of reactive oxygen species (ROS) because they are involved in cellular, organ-, and tissue-specific physiology. Mitochondria along...
2.
Kalashnikov D, Grivennikova V, Vinogradov A
Biochemistry (Mosc)
. 2011 Oct;
76(8):968-75.
PMID: 22022971
The NADH:ubiquinone oxidoreductase (respiratory complex I) activity of inside-out pig brain submitochondrial particles is inhibited by endogenous or externally added free fatty acids in time-dependent fashion. The rate and degree...
3.
Kalashnikov D, Grivennikova V, Vinogradov A
Biochemistry (Mosc)
. 2011 May;
76(2):209-16.
PMID: 21568854
A number of genetic or drug-induced pathophysiological disorders, particularly neurodegenerative diseases, have been reported to correlate with catalytic impairments of NADH:ubiquinone oxidoreductase (mitochondrial complex I). The vast majority of the...
4.
Elanskaya I, Toporova V, Grivennikova V, Muronets E, Lukashev E, Timofeev K
Biochemistry (Mosc)
. 2009 Nov;
74(10):1080-7.
PMID: 19916920
To study the function of soluble NAD(P)H:quinone oxidoreductase of the cyanobacterium Synechocystis sp. PCC 6803 encoded by drgA gene, recombinant DrgA protein carrying 12 histidine residues on the C-terminal end...
5.
Pepelina T, Chertkova R, Ostroverkhova T, Dolgikh D, Kirpichnikov M, Grivennikova V, et al.
Biochemistry (Mosc)
. 2009 Aug;
74(6):625-32.
PMID: 19645667
Three forms of horse heart cytochrome c with specific substitutions of heme cleft surface located amino acid residues involved in specific interactions with ubiquinol:cytochrome c reductase (complex III) and cytochrome...
6.
Vinogradov A, Grivennikova V
Biochemistry (Mosc)
. 2005 Apr;
70(2):120-7.
PMID: 15807648
Besides major NADH-, succinate-, and other substrate oxidase reactions resulting in four-electron reduction of oxygen to water, the mitochondrial respiratory chain catalyzes one-electron reduction of oxygen to superoxide radical O(2)(-.)...
7.
Elanskaya I, Timofeev K, Grivennikova V, Kuznetsova G, Davletshina L, Lukashev E, et al.
Biochemistry (Mosc)
. 2004 Jun;
69(4):445-54.
PMID: 15170383
Photoautotrophically grown cells of the cyanobacterium Synechocystis sp. PCC 6803 wild type and the Ins2 mutant carrying an insertion in the drgA gene encoding soluble NAD(P)H:quinone oxidoreductase (NQR) did not...
8.
Elanskaya I, Grivennikova V, Groshev V, Kuznetsova G, Semina M, Timofeev K
Biochemistry (Mosc)
. 2004 Mar;
69(2):137-42.
PMID: 15000679
Insertion mutant Ins2 of the cyanobacterium Synechocystis sp. PCC 6803, lacking NAD(P)H:quinone oxidoreductase (NQR) encoded by drgA gene, was characterized by higher sensitivity to quinone-type inhibitors (menadione and plumbagin) than...
9.
Unidirectional effect of lauryl sulfate on the reversible NADH:ubiquinone oxidoreductase (Complex I)
Grivennikova V, USHAKOVA A, Cecchini G, Vinogradov A
FEBS Lett
. 2003 Aug;
549(1-3):39-42.
PMID: 12914921
Lauryl sulfate inhibits the Deltamu;(H)(+)-dependent reverse electron transfer reactions catalyzed by NADH:ubiquinone oxidoreductase (Complex I) in coupled bovine heart submitochondrial particles and in vesicles derived from Paracoccus denitrificans. The inhibitor...
10.
Vinogradov A, Grivennikova V
IUBMB Life
. 2002 Jan;
52(3-5):129-34.
PMID: 11798024
Although the mitochondrial Complex I has been extensively studied for over 4 decades, its catalytic properties in mitochondria are poorly understood. This review summarizes the data on standard and nonstandard...