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- Publications
- Influence
Auxin regulates functional gene groups in a fold-change-specific manner in Arabidopsis thaliana roots
- N. A. Omelyanchuk, D. Wiebe, +10 authors V. V. Mironova
- Biology, Medicine
- Scientific Reports
- 30 May 2017
Auxin plays a pivotal role in virtually every aspect of plant morphogenesis. It simultaneously orchestrates a diverse variety of processes such as cell wall biogenesis, transition through the cell… Expand
Mitochondrial NUDIX hydrolases: A metabolic link between NAD catabolism, GTP and mitochondrial dynamics
- Aaron N Long, N. Klimova, T. Kristian
- Biology, Medicine
- Neurochemistry International
- 1 October 2017
&NA; NAD+ catabolism and mitochondrial dynamics are important parts of normal mitochondrial function and are both reported to be disrupted in aging, neurodegenerative diseases, and acute brain… Expand
CD38 Knockout Mice Show Significant Protection Against Ischemic Brain Damage Despite High Level Poly-ADP-Ribosylation
- A. Long, J. H. Park, N. Klimova, C. Fowler, D. Loane, T. Kristian
- Biology, Medicine
- Neurochemical Research
- 2016
Several enzymes in cellular bioenergetics metabolism require NAD+ as an essential cofactor for their activity. NAD+ depletion following ischemic insult can result in cell death and has been… Expand
NAD+ precursor modulates post-ischemic mitochondrial fragmentation and reactive oxygen species generation via SIRT3 dependent mechanisms
- N. Klimova, Adam Fearnow, Aaron N Long, T. Kristian
- Chemistry, Medicine
- Experimental Neurology
- 11 December 2019
Global cerebral ischemia depletes brain tissue NAD+, an essential cofactor for mitochondrial and cellular metabolism, leading to bioenergetics failure and cell death. The post-ischemic NAD+ levels… Expand
Significance of Mitochondrial Protein Post-translational Modifications in Pathophysiology of Brain Injury
- N. Klimova, Aaron N Long, T. Kristian
- Biology, Medicine
- Translational Stroke Research
- 1 June 2018
Mitochondria are complex organelles that undergo constant fusion and fission in order to adapt to the ever-changing cellular environment. The fusion/fission proteins, localized in the inner and outer… Expand
The diversity and relationship of prion protein self-replicating states.
- N. Klimova, N. Makarava, I. Baskakov
- Biology, Medicine
- Virus research
- 2 September 2015
It has become evident that the prion protein (PrP) can form a diverse range of self-replicating structures in addition to bona fide PrP(Sc) or strain-specific PrP(Sc) variants. Some self-replicating… Expand
Multi-targeted Effect of Nicotinamide Mononucleotide on Brain Bioenergetic Metabolism
- N. Klimova, T. Kristian
- Chemistry, Medicine
- Neurochemical Research
- 19 January 2019
Dysfunctions in NAD+ metabolism are associated with neurodegenerative diseases, acute brain injury, diabetes, and aging. Loss of NAD+ levels results in impairment of mitochondria function, which… Expand
Nicotinamide mononucleotide alters mitochondrial dynamics by SIRT3‐dependent mechanism in male mice
- N. Klimova, Aaron N Long, T. Kristian
- Chemistry, Medicine
- Journal of neuroscience research
- 1 August 2019
Nicotinamide adenine dinucleotide (NAD+) is a central signaling molecule and enzyme cofactor that is involved in a variety of fundamental biological processes. NAD+ levels decline with age,… Expand
Loss of Cellular Sialidases Does Not Affect the Sialylation Status of the Prion Protein but Increases the Amounts of Its Proteolytic Fragment C1
- E. Katorcha, N. Klimova, +8 authors I. Baskakov
- Biology, Medicine
- PloS one
- 16 November 2015
The central molecular event underlying prion diseases involves conformational change of the cellular form of the prion protein (PrPC), which is a sialoglycoprotein, into the disease-associated,… Expand
Sialylation of Glycosylphosphatidylinositol (GPI) Anchors of Mammalian Prions Is Regulated in a Host-, Tissue-, and Cell-specific Manner*
- E. Katorcha, Saurabh Srivastava, N. Klimova, I. Baskakov
- Biology, Medicine
- The Journal of Biological Chemistry
- 17 June 2016
Prions or PrPSc are proteinaceous infectious agents that consist of misfolded, self-replicating states of the prion protein or PrPC. PrPC is posttranslationally modified with N-linked glycans and a… Expand