Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Julie A. Gegner"'
Publikováno v:
Educational Technology Research and Development. 57:79-97
High school students can access original scientific research articles on the Internet, but may have trouble understanding them. To address this problem of online literacy, the authors developed a computer-based prototype for guiding students’ compr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::032101faf995a41995d4583723aee08e
https://doi.org/10.1007/s11423-008-9088-3
https://doi.org/10.1007/s11423-008-9088-3
Autor:
Julie A. Gegner, J. D. Lee, Vladimir V. Kravchenko, Peter S. Tobias, Richard I. Tapping, John C. Mathison, Sally Orr, Jiahuai Han, Richard J. Ulevitch
Publikováno v:
Journal of Periodontal Research. 32:99-103
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23bb118201ef65fe615b5b9113b13890
https://doi.org/10.1111/j.1600-0765.1997.tb01388.x
https://doi.org/10.1111/j.1600-0765.1997.tb01388.x
Publikováno v:
Journal of Biological Chemistry. 270:5320-5325
Under physiological conditions, lipopolysaccharide (LPS) activation of cells involves the LPS binding protein (LBP) and either membrane or soluble CD14. We find LPS forms a ternary complex with LBP and membrane CD14 (mCD14). Subsequent to complex for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::319b99c1ee776a5fe4f2db1501c6da10
https://doi.org/10.1074/jbc.270.10.5320
https://doi.org/10.1074/jbc.270.10.5320
Publikováno v:
Clinical infectious diseases : an official publication of the Infectious Diseases Society of America. 28(3)
Recent work has identified two proteins that work together to enable many cell types to respond to endotoxin. These two proteins, lipopolysaccharide (LPS) binding protein (LBP) and CD14, also participate in cellular internalization of endotoxin, whic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10c372337c5815879371c20225f84f20
https://pubmed.ncbi.nlm.nih.gov/10194064
https://pubmed.ncbi.nlm.nih.gov/10194064
Publikováno v:
The Journal of biological chemistry. 271(30)
Mitogen-activated protein (MAP) kinase cascades represent one of the major signal systems used by eukaryotic cells to transduce extracellular signals into cellular responses. Four MAP kinase subgroups have been identified in humans: ERK, JNK (SAPK),
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ab40eb8917a573cafe49db3792ff7e2
https://pubmed.ncbi.nlm.nih.gov/8663524
https://pubmed.ncbi.nlm.nih.gov/8663524
Publikováno v:
The Journal of biological chemistry. 270(18)
Endotoxin (lipopolysaccharide; LPS) activates a wide variety of host defense mechanisms. In mammals LPS binding protein (LBP) and CD14 interact with LPS to mediate cellular activation. Using sucrose density gradients and a fluorescent endotoxin deriv
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ef19c5b10f333fed2e8fe7d956447e6
https://pubmed.ncbi.nlm.nih.gov/7537731
https://pubmed.ncbi.nlm.nih.gov/7537731
Publikováno v:
Cell. 70(6)
We examined the binding interactions of the methylation-dependent chemotaxis receptors Tsr and Tar with the chemotaxis-specific protein kinase CheA and the coupling factor CheW. Receptor directly bound CheW, but receptor-CheA binding was dependent up
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc57f66081b1400e66b964df7028d9ba
https://pubmed.ncbi.nlm.nih.gov/1326408
https://pubmed.ncbi.nlm.nih.gov/1326408
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 88(3)
An essential step in the signal transduction pathway of Escherichia coli is the control of the protein kinase activity of CheA by the chemotaxis receptor proteins. This control requires the participation of the CheW protein. Although the biochemical
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44619988ca137b60fc7dee8854c79e2a
https://pubmed.ncbi.nlm.nih.gov/1992467
https://pubmed.ncbi.nlm.nih.gov/1992467