Zobrazeno 1 - 10
of 120
pro vyhledávání: '"Philip Aisen"'
Autor:
Ekaterina Dadachova, Ruth A Bryan, Xianchun Huang, Tiffany Moadel, Andrew D Schweitzer, Philip Aisen, Joshua D Nosanchuk, Arturo Casadevall
Publikováno v:
PLoS ONE, Vol 2, Iss 5, p e457 (2007)
BackgroundMelanin pigments are ubiquitous in nature. Melanized microorganisms are often the dominating species in certain extreme environments, such as soils contaminated with radionuclides, suggesting that the presence of melanin is beneficial in th
Externí odkaz:
https://doaj.org/article/8ac7421f5f7f42e0b3015c43aa222e60
Autor:
Naoko Mizuno, Philip Aisen, Alasdair C. Steven, Muse Oke, Evzen Boura, James C. Gumbart, Anne B. Mason, Nicole C. Easley, Andrew Gorringe, Emad Tajkhorshid, Robert W. Evans, Nicholas Noinaj, Olga Zak, Susan K. Buchanan, Ashley N. Steere
Publikováno v:
Nature
Neisseria are obligate human pathogens causing bacterial meningitis, septicaemia and gonorrhoea. Neisseria require iron for survival and can extract it directly from human transferrin for transport across the outer membrane. The transport system cons
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56fcdaebbaf200b0fde112eb2d2d3635
https://doi.org/10.1038/nature10823
https://doi.org/10.1038/nature10823
Publikováno v:
Journal of Molecular Biology. 397:375-384
Author
Transferrin receptor 2 (TfR2), a homologue of the classical transferrin receptor 1 (TfR1), is found in two isoforms, alpha and beta. Like TfR1, TfR2alpha is a type II membrane protein, but the beta form lacks transmembrane portions and th
Transferrin receptor 2 (TfR2), a homologue of the classical transferrin receptor 1 (TfR1), is found in two isoforms, alpha and beta. Like TfR1, TfR2alpha is a type II membrane protein, but the beta form lacks transmembrane portions and th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7ddf54ba24d3d68d837ed43b57714d5
https://doi.org/10.1016/j.jmb.2010.01.026
https://doi.org/10.1016/j.jmb.2010.01.026
Autor:
Arturo Casadevall, Joshua D. Nosanchuk, Andrew D. Schweitzer, Ruth A. Bryan, Philip Aisen, Ekaterina Dadachova, Robertha C. Howell
Publikováno v:
Pigment Cell & Melanoma Research. 21:192-199
Melanized microorganisms are often found in environments with very high background radiation levels such as in nuclear reactor cooling pools and the destroyed reactor in Chernobyl. These findings and the laboratory observations of the resistance of m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b13b76c3fdd3a9658c8ecfb8a3addda9
https://doi.org/10.1111/j.1755-148x.2007.00430.x
https://doi.org/10.1111/j.1755-148x.2007.00430.x
Autor:
Nikolaus Grigorieff, Olga Zak, Philip Aisen, Yifan Cheng, Mykol Larvie, Stephen C. Harrison, Thomas Walz, Elmar Wolf
Publikováno v:
Journal of Molecular Biology. 355:1048-1065
The outcome of three-dimensional (3D) reconstructions in single particle electron microscopy (EM) depends on a number of parameters. We have used the well-characterized structure of the transferrin (Tf)–transferrin receptor (TfR) complex to study h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::916af6e40b25534ea65e8c95a0e20f3f
https://doi.org/10.1016/j.jmb.2005.11.021
https://doi.org/10.1016/j.jmb.2005.11.021
Publikováno v:
Molecular & Cellular Proteomics. 4:1959-1967
The structural allostery and binding interface for the human serum transferrin (Tf)·transferrin receptor (TfR) complex were identified using radiolytic footprinting and mass spectrometry. We have determined previously that the transferrin C-lobe bin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::074a49d17226e1aa5859d3381b7e254b
https://doi.org/10.1074/mcp.m500095-mcp200
https://doi.org/10.1074/mcp.m500095-mcp200
Publikováno v:
Journal of Structural Biology. 152:204-210
Most organisms depend on iron as a co-factor for proteins catalyzing redox reactions. Iron is, however, a difficult element for cells to deal with, as it is insoluble in its ferric (Fe3+) form and potentially toxic in its ferrous (Fe2+) form. Thus, i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53a8b59e9f42d2a027a33b4b7158da30
https://doi.org/10.1016/j.jsb.2005.10.006
https://doi.org/10.1016/j.jsb.2005.10.006
Autor:
Javier Garcia-Rivera, Joshua D. Nosanchuk, Helene C. Eisenman, Philip Aisen, Arturo Casadevall, Oscar Zaragoza, Tiffany Moadel, Ekaterina Dadachova
Publikováno v:
Fungal Genetics and Biology. 42:989-998
Cryptococcus neoformans produces pigments in vitro in the presence of exogenous substrate. We characterized acid-resistant particles isolated from pigmented cells grown in L-dopa, methyl-dopa, (-)-epinephrine or (-)-norepinephrine. The goals of this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f395a828ba63288b149d6f7b34eb0dc3
https://doi.org/10.1016/j.fgb.2005.09.003
https://doi.org/10.1016/j.fgb.2005.09.003
Autor:
Arturo Casadevall, Alfred M. Legendre, Piyali Mandal, Joshua D. Nosanchuk, Philip Aisen, David van Duin
Publikováno v:
FEMS Microbiology Letters. 239:187-193
Melanin is made by several important pathogenic fungi and is implicated in the pathogenesis of a number of mycoses. This study investigates whether the thermally dimorphic fungal pathogen Blastomyces dermatitidis produces melanin. Using techniques de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ce08875af72d4a8e586f3c315fc109c
https://doi.org/10.1016/j.femsle.2004.08.040
https://doi.org/10.1016/j.femsle.2004.08.040
Autor:
Olga Zak, Philip Aisen
Publikováno v:
Biochemistry. 42:12330-12334
Human transferrin, like other members of the transferrin class of iron-binding proteins, is a bilobal structure, the product of duplication and fusion of an ancestral gene during the course of biochemical evolution. Although the two lobes exhibit 45%
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d898980c155d445a5b5ea521026911c1
https://doi.org/10.1021/bi034991f
https://doi.org/10.1021/bi034991f