Zobrazeno 1 - 10
of 67
pro vyhledávání: '"V. T. Marchesi"'
Autor:
V. T. Marchesi
Publikováno v:
Annals of the New York Academy of Sciences. 116:774-788
Autor:
Edward J. Benz, Guang-Hsiung Kou, Tang K. Tang, Jen-Pin Huang, Chieh-Ju C. Tang, V. T. Marchesi
Publikováno v:
Journal of Biological Chemistry. 268:3758-3766
Protein 4.1 (P4.1) is a multifunctional protein with heterogeneity in molecular weight, intracellular localization, tissue- and development-specific expression patterns. We have analyzed the genomic structure of the locus encoding mouse P4.1 and have
Autor:
V T, Marchesi
Publikováno v:
The American journal of pathology. 108(3)
Autor:
V T, Marchesi
Publikováno v:
The American journal of pathology. 108(3)
Autor:
V T, Marchesi
Publikováno v:
The American journal of pathology. 137(3)
Publikováno v:
Blood. 87(9)
Protein 4.1 is an 80-kD structural component of the red blood cell (RBC) cytoskeleton. It is critical for the formation of the spectrin/actin/protein 4.1 junctional complex, the integrity of which is important for the horizontal strength and elastici
Autor:
V T, Marchesi
Publikováno v:
Molecular medicine (Cambridge, Mass.). 1(5)
Publikováno v:
The Journal of biological chemistry. 268(5)
Protein 4.1 (P4.1) is a multifunctional protein with heterogeneity in molecular weight, intracellular localization, tissue- and development-specific expression patterns. We have analyzed the genomic structure of the locus encoding mouse P4.1 and have
Autor:
K E, Sahr, P, Laurila, L, Kotula, A L, Scarpa, E, Coupal, T L, Leto, A J, Linnenbach, J C, Winkelmann, D W, Speicher, V T, Marchesi
Publikováno v:
The Journal of biological chemistry. 265(8)
Overlapping human erythroid alpha-spectrin cDNA clones were isolated from lambda gt11 libraries constructed from cDNAs of human fetal liver and erythroid bone marrow. The composite 8001-base pair (bp) cDNA nucleotide sequence contains 187-bp 5'- and
Autor:
J S Morrow, V T Marchesi
Publikováno v:
The Journal of Cell Biology
Purified human erythrocyte spectrin is able to form large oligomeric species without the collaboration of any other proteins. This reversible self-assembly process is both temperature and concentration dependent and seems to be mediated by the same k