Výsledky vyhledávání - "Megan Brunjes Brophy"

Biochemical and Spectroscopic Observation of Mn(II) Sequestration from Bacterial Mn(II) Transport Machinery by Calprotectin

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

Zobrazit plný text záznamu

Biochemical and Functional Evaluation of the Intramolecular Disulfide Bonds in the Zinc-Chelating Antimicrobial Protein Human S100A7 (Psoriasin)

Autor: Megan Brunjes Brophy, Lisa S. Cunden, Elizabeth M. Nolan, Hope A. Flaxman, Grayson E. Rodriguez

Publikováno v: Biochemistry. 56:5726-5738

Human S100A7 (psoriasin) is a metal-chelating protein expressed by epithelial cells. It is a 22-kDa homodimer with two EF-hand domains per subunit, and two transition-metal-binding His3Asp sites at the dimer interface. Each subunit contains two cyste

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb3b803d5955de2aa282dcf2fde668c5
https://doi.org/10.1021/acs.biochem.7b00781

Zobrazit plný text záznamu

The Hexahistidine Motif of Host-Defense Protein Human Calprotectin Contributes to Zinc Withholding and Its Functional Versatility

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

Zobrazit plný text záznamu

Calprotectin influences the aggregation of metal-free and metal-bound amyloid-β by direct interaction

Autor: Masha G. Savelieff, Juhye Kang, Elizabeth M. Nolan, Hyuck Jin Lee, Shin Jung C. Lee, Toshiki G. Nakashige, Megan Brunjes Brophy, Mi Hee Lim

Publikováno v: Prof. Nolan via Ye Li

Proteins from the S100 family perform numerous functions and may contribute to Alzheimer's disease (AD). Herein, we report the effects of S100A8/S100A9 heterooligomer calprotectin (CP) and the S100B homodimer on metal-free and metal-bound amyloid-β

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3ebfce1bfddb7f18ac9cac7c6082c75
https://pubmed.ncbi.nlm.nih.gov/30046785

Zobrazit plný text záznamu

Manganese Binding Properties of Human Calprotectin under Conditions of High and Low Calcium: X-ray Crystallographic and Advanced Electron Paramagnetic Resonance Spectroscopic Analysis

Autor: Elizabeth M. Nolan, Sarah E. J. Bowman, Catherine L. Drennan, R. David Britt, Megan Brunjes Brophy, Derek M. Gagnon, Troy A. Stich

Publikováno v: Journal of the American Chemical Society, vol 137, iss 8

The antimicrobial protein calprotectin (CP), a hetero-oligomer of the S100 family members S100A8 and S100A9, is the only identified mammalian Mn(II)-sequestering protein. Human CP uses Ca(II) ions to tune its Mn(II) affinity at a biologically unprece

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b8df98dbff2f2197d19fc5e6ccc0077
https://doi.org/10.1021/ja512204s

Zobrazit plný text záznamu

Impaired cholecystokinin-induced gallbladder emptying incriminated in spontaneous 'black' pigment gallstone formation in germfree Swiss Webster mice

Autor: James G. Fox, Stephanie E. Woods, Kara R. Bernert, Elizabeth M. Nolan, Gary M. Mawe, Mark T. Whary, Joshua A. Hayden, Monika R. Leonard, Sureshkumar Muthupalani, Megan Brunjes Brophy, Martin C. Carey, Brigitte Lavoie

Publikováno v: Prof. Nolan via Erja Kajosalo

“Black” pigment gallstones form in sterile gallbladder bile in the presence of excess bilirubin conjugates (“hyperbilirubinbilia”) from ineffective erythropoiesis, hemolysis, or induced enterohepatic cycling (EHC) of unconjugated bilirubin. I

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f65a62037b2a469208e87e7e76f7f4b
http://hdl.handle.net/1721.1/96251

Zobrazit plný text záznamu

High-affinity Manganese Coordination by Human Calprotectin is Calcium-dependent and Requires the Histidine-rich Site Formed at the Dimer Interface

Autor: Elizabeth M. Nolan, Lisa S. Cunden, Joshua A. Hayden, Megan Brunjes Brophy

Publikováno v: PMC

Calprotectin (CP) is a transition metal-chelating antimicrobial protein of the calcium-binding S100 family that is produced and released by neutrophils. It inhibits the growth of various pathogenic microorganisms by sequestering the transition metal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::db9c4ddfab98b86b7c645308e3e48bc3
https://europepmc.org/articles/PMC3575579/

Zobrazit plný text záznamu

Calcium Ion Gradients Modulate the Zinc Affinity and Antibacterial Activity of Human Calprotectin

Autor: Elizabeth M. Nolan, Megan Brunjes Brophy, Joshua A. Hayden

Calprotectin (CP) is an antimicrobial protein produced and released by neutrophils that inhibits the growth of pathogenic microorganisms by sequestering essential metal nutrients in the extracellular space. In this work, spectroscopic and thermodynam

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::30fbde7408bbcbb70695f18d77904cda
https://europepmc.org/articles/PMC3579771/

Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání