Zobrazeno 1 - 10
of 52
pro vyhledávání: '"Carl M. Cohen"'
Autor:
Rosa Li, Eric Britt Moore, Anna M. Lipkin, Monika Lewinska, Shervin Fatehi, Carl M. Cohen, Beth Adamowicz, Yongsheng Ji, Déna Skye Jansen, Douglas Steinhauff, David M. Cole, Aminata P. Coulibaly, Maria H. Holmström, Joel Henrique Ellwanger, Edmond Sanganyado, Buddini Iroshika Karawdeniya, Naike Bochatay, Joshua I. James, Shaima Ibrahim
Publikováno v:
Science. 366:28-30
Autor:
M. Bozon, Michael J. A. Tanner, C. Korsgren, J. Delaunay, S. Fattoum, L Morle, Mary Risinger, S. Hayette, Carl M. Cohen, A. Ghanem
Publikováno v:
British Journal of Haematology. 89:762-770
A recessively transmitted haemolytic anaemia associated with the lack of protein 4.2 was found in a Tunisian kindred. Trace amounts of this protein (72 kD component) became visible using high-sensitivity Western blots. Band 3 and ankyrin genes were e
Autor:
Narla Mohandas, Carlo Brugnara, Kathryn M. John, Babette Gwynn, Hitesh K. Jindel, Luanne L. Peters, Cathy Korsgren, Michael Cho, Samuel E. Lux, Carl M. Cohen, David E. Golan
Publikováno v:
Journal of Clinical Investigation. 103:1527-1537
Protein 4.2 is a major component of the red blood cell (RBC) membrane skeleton. We used targeted mutagenesis in embryonic stem (ES) cells to elucidate protein 4.2 functions in vivo. Protein 4. 2-null (4.2(-/-)) mice have mild hereditary spherocytosis
Publikováno v:
Experimental Cell Research. 229:421-431
Band 4.2 (pallidin) is a major erythrocyte membrane protein which has been detected in a number of nonerythroid cell types. Increasing evidence suggests that band 4.2 is involved in maintaining membrane stability in the erythrocyte. For example, band
Autor:
Yoshihito Yawata, David E. Golan, Carl M. Cohen, S. Hayette, James D. Corbett, C. Korsgren, Hemant S. Thatte
Publikováno v:
Biophysical Journal. 70(3):1534-1542
Band 4.2 is a human erythrocyte membrane protein of incompletely characterized structure and function. Erythrocytes deficient in band 4.2 protein were used to examine the functional role of band 4.2 in intact erythrocyte membranes. Both the lateral a
Autor:
Elizabeth Dotimas, Anser C. Azim, Athar H. Chishti, Catherine Korsgren, Carl M. Cohen, Shirin M. Marfatia
Publikováno v:
Biochemistry. 35:3001-3006
Dematin and protein 4.2 are peripheral membrane proteins associated with the cytoplasmic surface of the human erythrocyte plasma membrane. Isoforms of dematin and protein 4.2 exist in many nonerythroid cells. In solution, dematin is a trimeric protei
Publikováno v:
Experimental Cell Research. 219:454-460
We have used murine erythroleukemia cells (MEL cells) to investigate the role of phosphatidylinositol 3-kinase (PI 3-kinase) in erythroid differentiation. When treated with dimethyl sulfoxide (DMSO), MEL cells grown on a fibronectin matrix become com
Autor:
Carl M. Cohen
Publikováno v:
Nature Reviews Drug Discovery. 2:751-753
The current use of metrics-driven approaches to improve the productivity of pharmaceutical drug discovery will fail. This article presents an approach to the use of performance metrics that has the potential to guide fundamental industry improvement
Autor:
Carl M. Cohen, Philippe Gascard
Publikováno v:
Blood. 83:1102-1108
We investigated the role of glycophorins C and D in the association of band 4.1 with the erythrocyte membrane by measuring the binding of band 4.1 to erythrocyte inside-out vesicles stripped of endogenous band 4.1. Vesicles were prepared from either
Autor:
Carl M. Cohen, Bipasha GuptaRoy
Publikováno v:
Journal of Biological Chemistry. 267:15326-15333
Treatment of murine erythroleukemia cells (MELC) attached to fibronectin-coated dishes with dimethyl sulfoxide causes the cells to become committed to the erythroid differentiation pathway. These cells mature extensively and acquire the characteristi