Nina Maliar

ORCID: 0000-0002-9216-4525
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About
Contact & Profiles
Research Areas
  • Photoreceptor and optogenetics research
  • Neuroscience and Neuropharmacology Research
  • Photosynthetic Processes and Mechanisms
  • Mitochondrial Function and Pathology
  • Neuroscience and Neural Engineering
  • ATP Synthase and ATPases Research
  • RNA and protein synthesis mechanisms
  • Molecular Communication and Nanonetworks
  • Neuroinflammation and Neurodegeneration Mechanisms
  • Photochromic and Fluorescence Chemistry
  • Advanced Fluorescence Microscopy Techniques
  • bioluminescence and chemiluminescence research
  • Plant and Biological Electrophysiology Studies
  • Nicotinic Acetylcholine Receptors Study
  • interferon and immune responses
  • Ubiquitin and proteasome pathways
  • Mass Spectrometry Techniques and Applications
  • Spectroscopy Techniques in Biomedical and Chemical Research

University of Cambridge
2023-2024

Moscow Institute of Physics and Technology
2020-2022

Moscow Power Engineering Institute
2022

Abstract The light-driven sodium-pumping rhodopsin KR2 from Krokinobacter eikastus is the only non-proton cation active transporter with demonstrated potential for optogenetics. However, existing structural data on correspond exclusively to its ground state, and show no sodium inside protein, which hampers understanding of mechanism. Here we present crystal structure O-intermediate physiologically relevant pentameric form at resolution 2.1 Å, revealing a ion near retinal Schiff base,...

10.1038/s41467-020-16032-y article EN cc-by Nature Communications 2020-05-01

Abstract Light-driven sodium pumps (NaRs) are unique ion-transporting microbial rhodopsins. The major group of NaRs is characterized by an NDQ motif and has two aspartic acid residues in the central region essential for transport. Here we identify a subgroup rhodopsins bearing additional glutamic residue close vicinity to retinal Schiff base. We thoroughly characterize member this subgroup, namely protein Er NaR from Erythrobacter sp. HL-111 show that results almost complete loss pH...

10.1038/s41467-024-47469-0 article EN cc-by Nature Communications 2024-04-10

This is a review of relevant Raman spectroscopy (RS) techniques and their use in structural biology, biophysics, cells, tissues imaging towards development various medical diagnostic tools, drug design, other applications. Classical contemporary studies different water-soluble membrane proteins, DNA, RNA, interactions behavior systems were analyzed terms applicability RS complementarity to corresponding methods. We show that powerful method links the fundamental biology its applications...

10.3390/cryst10010038 article EN cc-by Crystals 2020-01-15

Protein-fragment complementation assays are used ubiquitously for probing protein–protein interactions. Most commonly, the reporter protein is split in two parts, which then fused to proteins of interest and can reassemble provide a readout if interact with each other. The currently known fluorescent either be only aerobic conditions assemble irreversibly, or require addition exogenous chromophores, complicates design experiments. In recent years, light-oxygen-voltage (LOV) domains several...

10.1021/acssynbio.0c00454 article EN ACS Synthetic Biology 2020-12-16

Mitochondrial protein biogenesis relies almost exclusively on the expression of nuclear-encoded polypeptides. The current model postulates that most these proteins have to be delivered their final mitochondrial destination after synthesis in cytoplasm. However, knowledge this process remains limited due absence proper experimental real-time approaches study mitochondria native cellular environment. We developed a gentle microinjection procedure for fluorescent reporter allowing direct...

10.3389/fcell.2021.698658 article EN cc-by Frontiers in Cell and Developmental Biology 2021-07-07

The light-driven sodium pump KR2, found in 2013 the marine bacteria Krokinobacter eikastus, serves as a model protein for studies of sodium-pumping microbial rhodopsins (NaRs). KR2 possesses unique NDQ (N112, D116, and Q123) set amino acid residues functionally relevant positions, named motif. N112 was shown to determine Na+/H+ selectivity pumping efficiency protein. Thus, N112A mutation converts into an outward proton pump. However, no structural data on functional conversions pumps are...

10.3390/cryst10060496 article EN cc-by Crystals 2020-06-08

The maintenance of genome stability is crucial for cell homeostasis and tissue integrity. Numerous human neuropathologies display chronic inflammation in the central nervous system, set against a backdrop instability, implying close interplay between DNA damage immune responses context neurological disease. Dissecting molecular mechanisms this crosstalk essential holistic understanding neuroinflammatory pathways instability disorders. Non-neuronal types, specifically microglia, are major...

10.1016/j.dnarep.2024.103634 article EN cc-by DNA repair 2024-01-24

ABSTRACT Light-driven sodium pumps (NaRs) are unique ion-transporting microbial rhodopsins. The major group of NaRs is characterized by an NDQ motif and has two aspartic acid residues in the central region essential for transport. Here we identified a new subgroup rhodopsins bearing additional glutamic residue close vicinity to retinal Schiff base. We thoroughly member this subgroup, namely protein Er NaR from Erythrobacter sp. HL-111 showed that results almost complete loss pH sensitivity...

10.1101/2023.10.11.561842 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2023-10-12

Abstract Mitochondrial protein biogenesis relies almost exclusively on the expression of nuclear-encoded polypeptides. The current model postulates that most these proteins have to be delivered their final mitochondrial destination after synthesis in cytoplasm. However, knowledge this process remains limited due absence proper experimental real-time approaches study mitochondria native cellular environment. We developed a gentle microinjection procedure for fluorescent reporter allowing...

10.1101/2020.09.30.317412 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2020-10-01
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