Zobrazeno 1 - 10
of 251
pro vyhledávání: '"John S Olson"'
Autor:
MarCia T Ekworomadu, Catherine B Poor, Cedric P Owens, Miriam A Balderas, Marian Fabian, John S Olson, Frank Murphy, Erol Bakkalbasi, Erin S Honsa, Chuan He, Celia W Goulding, Anthony W Maresso
Publikováno v:
PLoS Pathogens, Vol 8, Iss 3, p e1002559 (2012)
To replicate in mammalian hosts, bacterial pathogens must acquire iron. The majority of iron is coordinated to the protoporphyrin ring of heme, which is further bound to hemoglobin. Pathogenic bacteria utilize secreted hemophores to acquire heme from
Externí odkaz:
https://doaj.org/article/56c677eeda1c4146833e8d2069b9ff28
Publikováno v:
Molecular Systems Biology, Vol 6, Iss 1, Pp n/a-n/a (2010)
Systems biology can offer a great deal of insight into evolution by quantitatively linking complex properties such as protein structure, folding, and function to the fitness of an organism. Although the link between diseases such as Alzheimer's and m
Externí odkaz:
https://doaj.org/article/462318ae2c134908aca7021d8980ba09
Autor:
Patrick Barry, Wesley A. Larson, Diana S. Baetscher, William Dokai, Jacek Maselko, John S. Olson
Publikováno v:
Environmental DNA. 4:868-880
Nearshore marine habitats are critical for a variety of commercially important fish species, but assessing fish communities in these habitats is costly and time-intensive. Here, we leverage eDNA metabarcoding to characterize nearshore fish communitie
Autor:
Mark A. White, William C. Ou, Premila P. Samuel, David A. Case, George N. Phillips, John S. Olson
Publikováno v:
Biophysical Journal. 118:1381-1400
Hemoglobin functions as a tetrameric oxygen transport protein, with each subunit containing a heme cofactor. Its denaturation, either in vivo or in vitro, involves autoxidation to methemoglobin, followed by cofactor loss and globin unfolding. We have
Autor:
John S. Olson
Publikováno v:
Antioxidants & Redox Signaling. 32:228-246
Significance: Over the past 50 years, the mechanisms for O(2) storage and transport have been determined quantitatively on distance scales from millimeters to tenths of nanometers and timescales from seconds to picoseconds. Recent Advances: In this r
Autor:
John S. Olson
Publikováno v:
Mol Aspects Med
Antonini and Brunori’s 1971 book “Hemoglobin and Myoglobin in Their Reactions with Ligands” was a truly remarkable publication that summarized almost 100 years of research on O(2) binding to these globins. Over the ensuing 50 years, ultra-fast
Autor:
Megan, Sjodt, Ramsay, Macdonald, Joanna D, Marshall, Joseph, Clayton, John S, Olson, Martin, Phillips, David A, Gell, Jeff, Wereszczynski, Robert T, Clubb
Publikováno v:
The Journal of biological chemistry. 295(33)
Staphylococcus aureus is a leading cause of life-threatening infections in the United States. It actively acquires the essential nutrient iron from human hemoglobin (Hb) using the iron-regulated surface-determinant (Isd) system. This process is initi
Autor:
John S. Olson, Mark A. White, William C. Ou, Premila P. Samuel, George N. Phillips, David A. Case
Hemoglobin functions as an oxygen transport protein, with each subunit containing a heme cofactor. We have developed a global disassembly model for human hemoglobin, linking hemin (ferric heme) disassociation and apo(heme-free)-protein unfolding path
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6824ef55b597b83b1a55d09a66c357a9
Autor:
Michael Brad Strader, Abdu I. Alayash, John S. Olson, Jayashree Soman, Fantao Meng, Tigist Kassa
Publikováno v:
The Journal of Biological Chemistry
After reacting with hydrogen peroxide (H2O2), sickle-cell hemoglobin (HbS, βE6V) remains longer in a highly oxidizing ferryl form (HbFe4+=O) and induces irreversible oxidation of "hot-spot" amino acids, including βCys-93. To control the damaging fe
Autor:
David A. Gell, Ramsay Macdonald, Robert T. Clubb, Megan Sjodt, Jeff Wereszczynski, Joseph Clayton, Joanna D. Marshall, John S. Olson, Martin L. Phillips
Publikováno v:
Journal of Biological Chemistry. 295:11947