Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Toshiki G. Nakashige"'
Autor:
Louis J. Cohen, Sun M. Han, Pearson Lau, Daniela Guisado, Yupu Liang, Toshiki G. Nakashige, Thamina Ali, David Chiang, Adeeb Rahman, Sean F. Brady
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
Lectins are non-enzymatic carbohydrate binding proteins important to human cellular functions. Here, the authors characterize a lectin produced by a human associated bacterium, and show that interacts with myeloid cells in the blood and intestine, su
Externí odkaz:
https://doaj.org/article/1df5145a09fe429d8021a79dc2379add
Autor:
Frank J. Piscotta, Shawn T. Whitfield, Toshiki G. Nakashige, Andreia B. Estrela, Thahmina Ali, Sean F. Brady
Publikováno v:
Cell Reports, Vol 36, Iss 12, Pp 109746- (2021)
Summary: The human microbiota plays a critical role in host health. Proper development of the infant microbiome is particularly important. Its dysbiosis leads to both short-term health issues and long-term disorders lasting into adulthood. A central
Externí odkaz:
https://doaj.org/article/4f332560ce144da4821cde24d9a701af
Autor:
Andreia B. Estrela, Toshiki G. Nakashige, Christophe Lemetre, Ian D. Woodworth, Jazz L. Weisman, Louis J. Cohen, Sean F. Brady
Publikováno v:
mBio, Vol 10, Iss 6 (2019)
ABSTRACT The effect of the microbiota on its human host is driven, at least in part, by small-molecule and protein effectors it produces. Here, we report on the use of functional multigenomic screening to identify microbiota-encoded effectors. In thi
Externí odkaz:
https://doaj.org/article/c30310d16176471586d2970fd4e6b38e
Autor:
Louis J. Cohen, Sun M. Han, Pearson Lau, Daniela Guisado, Yupu Liang, Toshiki G. Nakashige, Thamina Ali, David Chiang, Adeeb Rahman, Sean F. Brady
Publikováno v:
Nature communications. 13(1)
The mechanisms by which commensal organisms affect human physiology remain poorly understood. Lectins are non-enzymatic carbohydrate binding proteins that all organisms employ as part of establishing a niche, evading host-defenses and protecting agai
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55b2c4a5bc637d6446d6d4ad9c6b9aa5
https://pubmed.ncbi.nlm.nih.gov/35661736
https://pubmed.ncbi.nlm.nih.gov/35661736
Autor:
Emily M. Zygiel, Elizabeth M. Nolan, Catherine L. Drennan, Toshiki G. Nakashige, Sarah E. J. Bowman
Publikováno v:
Biochemistry. 57:4155-4164
Calprotectin (CP, S100A8/S100A9 oligomer, MRP-8/MRP-14 oligomer) is a host-defense protein that sequesters nutrient transition metals from microbes. Each S100A8/S100A9 heterodimer contains four EF-hand domains and two transition-metal-binding sites.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::38707285085ef5963c4563abc5392598
https://doi.org/10.1021/acs.biochem.8b00415
https://doi.org/10.1021/acs.biochem.8b00415
Autor:
Elizabeth M. Nolan, Derek M. Gagnon, Yu Gu, R. David Britt, Toshiki G. Nakashige, Megan Brunjes Brophy, Rose C. Hadley
Publikováno v:
Journal of the American Chemical Society, vol 140, iss 1
Human calprotectin (CP, S100A8/S100A9 oligomer) is a metal-sequestering host-defense protein that prevents bacterial acquisition of Mn(II). In this work, we investigate Mn(II) competition between CP and two solute-binding proteins that Staphylococcus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31c7e174a1f75870c1eb5a77b71101d3
https://doi.org/10.1021/jacs.7b11207
https://doi.org/10.1021/jacs.7b11207
Autor:
Toshiki G. Nakashige, Louis J. Cohen, Sean F. Brady, Jazz L. Weisman, Ian D. Woodworth, Christophe Lemetre, Andreia B. Estrela
Publikováno v:
mBio, Vol 10, Iss 6, p e02587-19 (2019)
mBio, Vol 10, Iss 6 (2019)
mBio
mBio, Vol 10, Iss 6 (2019)
mBio
Human-associated bacteria are thought to encode bioactive small molecules and proteins that play an intimate role in human health and disease. Here, we report on the creation and functional screening of a multigenomic library constructed using genomi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8b19f703e2c85dba5513dada0f77ac4
https://doaj.org/article/fdb4f33b4d574bbf82a543f583741732
https://doaj.org/article/fdb4f33b4d574bbf82a543f583741732
Publikováno v:
Royal Society of Chemistry
Calprotectin (CP) is an abundant metal-chelating protein involved in host defense, and the ability of human CP to bind Fe(ii) in a calcium-dependent manner was recently discovered. In the present study, near-infrared magnetic circular dichroism spect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6cbf7fab3e6d98454fb73a6f8417fcb
https://doi.org/10.1039/c6sc03487j
https://doi.org/10.1039/c6sc03487j
Publikováno v:
PMC
We report that the metal-sequestering human host-defense protein calprotectin (CP, S100A8/S100A9 oligomer) affects the redox speciation of iron (Fe) in bacterial growth media and buffered aqueous solution. Under aerobic conditions and in the absence
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6669665e7551a9706b579554b5994d70
https://doi.org/10.1039/c7mt00044h
https://doi.org/10.1039/c7mt00044h
Autor:
Jules R. Stephan, Brenna C. Keegan, Toshiki G. Nakashige, Jason Shearer, Megan Brunjes Brophy, Lisa S. Cunden, Andrew J. Wommack, Elizabeth M. Nolan
Publikováno v:
Journal of the American Chemical Society. 138:12243-12251
Human calprotectin (CP, S100A8/S100A9 oligomer, MRP-8/MRP-14 oligomer) is an abundant host-defense protein that is involved in the metal-withholding innate immune response. CP coordinates a variety of divalent first-row transition metal ions, which i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3d8acd663bf863f1dbd0e86df43bc32
https://doi.org/10.1021/jacs.6b06845
https://doi.org/10.1021/jacs.6b06845