Alexander A Shcherbakov
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Explore the profile of Alexander A Shcherbakov including associated specialties, affiliations and a list of published articles.
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19
Citations
496
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Recent Articles
1.
Ingersoll J, Shcherbakov A, Vaish A, Poppe L
ACS Med Chem Lett
. 2023 Aug;
14(8):1063-1066.
PMID: 37583825
Biophysical research plays a crucial role in drug discovery, but many druglike molecules are poorly soluble and prone to aggregation, making their analysis challenging and susceptible to artifacts. To address...
2.
Shcherbakov A, Brousseau M, Henzler-Wildman K, Hong M
J Am Chem Soc
. 2023 Apr;
145(18):10104-10115.
PMID: 37097985
The bacterial transporter EmrE is a homo-dimeric membrane protein that effluxes cationic polyaromatic substrates against the concentration gradient by coupling to proton transport. As the archetype of the small multidrug...
3.
Shcherbakov A, Spreacker P, Dregni A, Henzler-Wildman K, Hong M
Nat Commun
. 2022 Feb;
13(1):991.
PMID: 35181664
The homo-dimeric bacterial membrane protein EmrE effluxes polyaromatic cationic substrates in a proton-coupled manner to cause multidrug resistance. We recently determined the structure of substrate-bound EmrE in phospholipid bilayers by...
4.
Shcherbakov A, Medeiros-Silva J, Tran N, Gelenter M, Hong M
Chem Rev
. 2021 Oct;
122(10):9848-9879.
PMID: 34694769
Internuclear distances represent one of the main structural constraints in molecular structure determination using solid-state NMR spectroscopy, complementing chemical shifts and orientational restraints. Although a large number of magic-angle-spinning (MAS)...
5.
Shcherbakov A, Hisao G, Mandala V, Thomas N, Soltani M, Salter E, et al.
Nat Commun
. 2021 Jan;
12(1):172.
PMID: 33420032
The dimeric transporter, EmrE, effluxes polyaromatic cationic drugs in a proton-coupled manner to confer multidrug resistance in bacteria. Although the protein is known to adopt an antiparallel asymmetric topology, its...
6.
Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers
Mandala V, McKay M, Shcherbakov A, Dregni A, Kolocouris A, Hong M
Nat Struct Mol Biol
. 2020 Nov;
27(12):1202-1208.
PMID: 33177698
An essential protein of the SARS-CoV-2 virus, the envelope protein E, forms a homopentameric cation channel that is important for virus pathogenicity. Here we report a 2.1-Å structure and the...
7.
Mandala V, McKay M, Shcherbakov A, Dregni A, Kolocouris A, Hong M
Res Sq
. 2020 Sep;
PMID: 32995764
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of the ongoing COVID-19 pandemic. Successful development of vaccines and antivirals against SARS-CoV-2 requires a comprehensive understanding of the...
8.
Shcherbakov A, Roos M, Kwon B, Hong M
J Biomol NMR
. 2020 Feb;
74(2-3):193-204.
PMID: 32088840
F solid-state NMR is an excellent approach for measuring long-range distances for structure determination and for studying molecular motion. For multi-fluorinated proteins, assignment of F chemical shifts has been traditionally...
9.
Mandala V, Loftis A, Shcherbakov A, Pentelute B, Hong M
Nat Struct Mol Biol
. 2020 Feb;
27(2):160-167.
PMID: 32015551
The influenza B M2 (BM2) proton channel is activated by acidic pH to mediate virus uncoating. Unlike influenza A M2 (AM2), which conducts protons with strong inward rectification, BM2 conducts...
10.
Goloshchapov O, Olekhnovich E, Sidorenko S, Moiseev I, Kucher M, Fedorov D, et al.
BMC Microbiol
. 2020 Jan;
19(1):312.
PMID: 31888470
Background: Fecal microbiota transplantation (FMT) has been recently approved by FDA for the treatment of refractory recurrent clostridial colitis (rCDI). Success of FTM in treatment of rCDI led to a...