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Glutamate 95 in NqrE Is an Essential Residue for the Translocation of Cations in Na+-NQR

Autor: Oscar Juárez, Katherine G. Mezic, Blanca Barquera, Jonathan J. Cho, Darcie Cook, Petra Hellwig, Yashvin Neehaul

Publikováno v: Biochemistry
Biochemistry, 2019, 58 (16), pp.2167-2175. ⟨10.1021/acs.biochem.8b01294⟩

The sodium-pumping NADH:quinone oxidoreductase (Na+-NQR) is a bacterial enzyme that oxidizes NADH, reduces ubiquinone, and translocates Na+ across the membrane. We previously identified three acidic residues in the membrane-spanning helices, near the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c751748c34ab51d2e1725648fadfd9a4
https://hal.archives-ouvertes.fr/hal-03336127

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LRRK2 levels in immune cells are increased in Parkinson’s disease

Autor: Jianjun Chang, Jeremy M. Boss, Amarallys F. Cintron, George T. Kannarkat, MariadeLourdes Tansey, N. Grigoryan, Kyle B. Fraser, Stewart A. Factor, Andrew B. West, Laura M. Butkovich, Darcie Cook

Publikováno v: NPJ Parkinson's Disease
npj Parkinson's Disease, Vol 3, Iss 1, Pp 1-12 (2017)

Mutations associated with leucine-rich repeat kinase 2 are the most common known cause of Parkinson’s disease. The known expression of leucine-rich repeat kinase 2 in immune cells and its negative regulatory function of nuclear factor of activated

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9224a626662bd5cb8d7e0571a986b798
http://europepmc.org/articles/PMC5459798

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Common genetic variant association with altered HLA expression, synergy with pyrethroid exposure, and risk for Parkinson’s disease: an observational and case–control study

Autor: Jae-Kyung Lee, Jianjun Chang, Jeremy M. Boss, Jaegwon Chung, MariadeLourdes Tansey, George T. Kannarkat, Stewart A. Factor, Beate Ritz, Kimberly C. Paul, Darcie Cook, E Sandy, Jeff M. Bronstein

Publikováno v: NPJ Parkinson's Disease

The common noncoding single-nucleotide polymorphism (SNP) rs3129882 in HLA-DRA is associated with risk for idiopathic Parkinson’s disease (PD). The location of the SNP in the major histocompatibility complex class II (MHC-II) locus implicates regul

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c94116835b471c28cee9edfcb874f9e1
https://doi.org/10.1038/npjparkd.2015.2

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The conformational changes induced by ubiquinone binding in the Na+-pumping NADH:ubiquinone oxidoreductase (Na+-NQR) are kinetically controlled by conserved glycines 140 and 141 of the NqrB subunit

Autor: Madeleine Strickland, Oscar Juárez, Darcie Cook, Petra Hellwig, Yashvin Neehaul, Blanca Barquera

Publikováno v: The Journal of biological chemistry
The Journal of biological chemistry, 2014, 289 (34), pp.23723-23733. ⟨10.1074/jbc.M114.574640⟩

PMID: 25006248 PMCID: PMC4156058; Na(+)-pumping NADH:ubiquinone oxidoreductase (Na(+)-NQR) is responsible for maintaining a sodium gradient across the inner bacterial membrane. This respiratory enzyme, which couples sodium pumping to the electron tra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30bb5c75be6f8ae6b53e81da843e2433
https://hal.archives-ouvertes.fr/hal-03336135

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The Role of Acid Residues in Na+ Uptake and Binding in Na+-NQR from Vibrio Cholerae

Autor: Jonathan J. Cho, Oscar Juárez, Michael E. Shea, Blanca Barquera, Darcie Cook

Publikováno v: Biophysical Journal. 102(3)

The Na+-translocating NADH:quinone oxidoreductase (Na+-NQR) is the gateway for electrons into the respiratory chain of Vibrio cholerae and many other pathogenic bacteria. Na+-NQR is unique among respiratory enzymes in that it pumps sodium rather than

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aaa5f8d67325ed88244a8420e829d66a

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