Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Maria Rotter"'
Autor:
Hannah Maria Rotter
'Jeder Philosoph hat zwei Philosophien: seine eigene und diejenige Spinozas'– diese Worte Henri Bergsons gelten für Friedrich Nietzsche in besonderem Maße. Sein Denken war von der Auseinandersetzung mit Baruch de Spinoza stark geprägt – ob
Publikováno v:
Journal of Molecular Biology. 428:1506-1514
Sickle cell disease is fundamentally a kinetic disorder, in which cells containing the mutated hemoglobin (HbS) will cause occlusion if they sickle in the microvasculature, but have minimal (or no) consequences if they sickle in the venous return. Ph
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::346f54c34b4f52fb5910554c518bf6e1
https://doi.org/10.1016/j.jmb.2016.03.001
https://doi.org/10.1016/j.jmb.2016.03.001
Publikováno v:
The journal of physical chemistry. B. 122(49)
Proteins that function in aqueous solution can be perturbed by the solvent. Here we present experimental studies on two such interactions in the hemoglobin molecule. (1) Hemoglobin's oxygen binding is altered by introduction of crowding species or os
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e4a86059ad588b78f62a2382fdfc968
https://pubmed.ncbi.nlm.nih.gov/30222355
https://pubmed.ncbi.nlm.nih.gov/30222355
Autor:
Suzanna Kwong, Weijun Weng, Donna Yosmanovich, Maria Rotter, Mikhail N. Zakharov, Alexey Aprelev, Frank A. Ferrone, Robin W. Briehl
Publikováno v:
Journal of Molecular Biology. 369:1170-1174
Sickle cell disease arises from a genetic mutation of one amino acid in each of the two hemoglobin beta chains, leading to the polymerization of hemoglobin in the red cell upon deoxygenation, and is characterized by vascular crises and tissue damage
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::34f0183e327ca3b077ecd0f27d8f6148
https://doi.org/10.1016/j.jmb.2007.04.030
https://doi.org/10.1016/j.jmb.2007.04.030
Autor:
Saul Surrey, Kazuhiko Adachi, Mikhail N. Zakharov, Frank A. Ferrone, Weijun Weng, Min Ding, Maria Rotter, Alexey Aprelev
Publikováno v:
Journal of Molecular Biology. 362:528-538
Polymerization of a 1:1 mixture of hemoglobin S (Hb S) and the artificial mutant HbAbeta73Leu produces a dramatic morphological change in the polymer domains in 1.0 M phosphate buffer that are a characteristic feature of polymer formation. Instead of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33eb0021cb85d16ebeda7212461086d8
https://doi.org/10.1016/j.jmb.2006.07.047
https://doi.org/10.1016/j.jmb.2006.07.047
Autor:
Robin W. Briehl, Maria Rotter, Frank A. Ferrone, Robert M. Bookchin, Alexey Aprelev, Zipora Etzion
Publikováno v:
Biophysical Journal. 88(4):2815-2822
Pathology in sickle cell disease begins with nucleation-dependent polymerization of deoxyhemoglobin S into stiff, rodlike fibers that deform and rigidify red cells. We have measured the effect of erythrocyte membranes on the rate of homogeneous nucle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7beb900722df308548881da4ce977f7e
Publikováno v:
Journal of Molecular Biology. 347:1015-1023
The dominant assumption central to most treatments for sickle cell anemia has been that replacement of sickle hemoglobin (HbS) by fetal hemoglobin (HbF) would have major clinical benefit. Using laser photolysis, we have measured polymerization kineti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d056455570126f96be0acc6037715c47
https://doi.org/10.1016/j.jmb.2005.02.006
https://doi.org/10.1016/j.jmb.2005.02.006
Autor:
Maria Rotter, Frank A. Ferrone
Publikováno v:
Journal of Molecular Recognition. 17:497-504
Under physiological conditions, sickle hemoglobin, a natural mutant of human hemoglobin A with a surface hydrophobic valine in place of a negatively charged glutamic acid, polymerizes at high volume occupancy. Equilibrium solubility of sickle hemoglo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::affdd66516cdcf2e91ff7c46d55c2062
https://doi.org/10.1002/jmr.698
https://doi.org/10.1002/jmr.698