Zobrazeno 1 - 10 of 20 pro vyhledávání: '"E. M. Schaefer"'
1
Mucosal acidosis elicits a unique molecular signature in epithelia and intestinal tissue mediated by GPR31-induced CREB phosphorylation
Autor: Jordi M. Lanis, Ian M. Cartwright, Nichole Welch, Kathryn R. Brink, Jeffrey J. Tabor, Andrew Mu, Rachael Kostelecky, Caroline H. T. Hall, Alexander S. Dowdell, Mark E. Gerich, Sean P. Colgan, Joseph C. Onyiah, Rachel E. M. Schaefer
Publikováno v: Proc Natl Acad Sci U S A
Metabolic changes associated with tissue inflammation result in significant extracellular acidosis (EA). Within mucosal tissues, intestinal epithelial cells (IEC) have evolved adaptive strategies to cope with EA through the up-regulation of SLC26A3 t
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9a8d963f5b60a814945a263878b5f0e
https://doi.org/10.1073/pnas.2023871118
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3
Disruption of monocyte-macrophage differentiation and trafficking by a heme analog during active inflammation
Autor: Rachel E M, Schaefer, Rosemary C, Callahan, Shaikh M, Atif, David J, Orlicky, Ian M, Cartwright, Andrew P, Fontenot, Sean P, Colgan, Joseph C, Onyiah
Publikováno v: Mucosal immunology. 15(2)
Heme metabolism is a key regulator of inflammatory responses. Cobalt protoporphyrin IX (CoPP) is a heme analog and mimic that potently activates the NRF2/heme oxygenase-1 (HO-1) pathway, especially in monocytes and macrophages. We investigated the in
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::98a5b0ec2e0189b7e8e31226ada9dcc3
https://pubmed.ncbi.nlm.nih.gov/34916594
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4
A Central Role for Heme Oxygenase-1 in the Control of Intestinal Epithelial Chemokine Expression
Autor: Joseph C. Onyiah, Rachel E. M. Schaefer, Sean P. Colgan
Publikováno v: Journal of Innate Immunity. 10:228-238
In mucosal inflammatory disorders, the protective influence of heme oxygenase-1 (HO-1) and its metabolic byproducts, carbon monoxide (CO) and biliverdin, is a topic of significant interest. Mechanisms under investigation include the regulation of mac
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f16957165f84d150da1e21cd1dcdfa9
https://doi.org/10.1159/000488914
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5
Microbial-derived Butyrate Promotes Epithelial Barrier Function Through IL-10 Receptor-dependent Repression of Claudin-2
Autor: Caleb J. Kelly, Jordi M. Lanis, Ruth Wang, Leon Zheng, Douglas J. Kominsky, Erica E. Alexeev, Kayla D. Battista, Sean P. Colgan, Joseph C. Onyiah, Rachel E. M. Schaefer
Commensal interactions between the enteric microbiota and distal intestine play important roles in regulating human health. Short-chain fatty acids (SCFAs), such as butyrate, produced through anaerobic microbial metabolism represent a major energy so
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54c296401e0c7d57fb32ce7918ce3928
https://europepmc.org/articles/PMC5636678/
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6
Kinetic partitioning during de novo septin filament assembly creates a critical G1 'window of opportunity' for mutant septin function
Autor: David J. Odde, Lydia R. Heasley, Rachel E. M. Schaefer, Michael A. McMurray
Publikováno v: Cell cycle (Georgetown, Tex.). 15(18)
Septin proteins form highly conserved cytoskeletal filaments composed of hetero-oligomers with strict subunit stoichiometry. Mutations within one hetero-oligomerization interface (the "G" interface) bias the mutant septin toward conformations that ar
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::64b908622b082ad343f2fa827fad46c2
https://pubmed.ncbi.nlm.nih.gov/27715407
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7
Akademický článek
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8
Multiple stimuli induce tyrosine phosphorylation of the Crk-binding sites of paxillin
Autor: M D, Schaller, E M, Schaefer
Publikováno v: The Biochemical journal. 360(Pt 1)
Paxillin is a focal-adhesion-associated, tyrosine-phosphorylated protein. In cells transformed by the src, crk or BCR-Abl oncogenes, the phosphotyrosine content of paxillin is elevated. In normal cells paxillin functions in signalling following integ
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0ce6eb29da93b3e7d2e79abf942affcc
https://pubmed.ncbi.nlm.nih.gov/11695992
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10
Structural organization of the human insulin receptor ectodomain
Autor: E M, Schaefer, H P, Erickson, M, Federwisch, A, Wollmer, L, Ellis
Publikováno v: The Journal of biological chemistry. 267(32)
To provide an experimental system amenable to a detailed biochemical and structural investigation of the extracellular (ligand binding) domain of the insulin receptor, we developed a mammalian heterologous cell expression system from which tens of mi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::bba16ea3517491cf2101f0e9e73a094a
https://pubmed.ncbi.nlm.nih.gov/1385419
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