Zobrazeno 1 - 10
of 24
pro vyhledávání: '"R, Winardi"'
Publikováno v:
IOP Conference Series: Earth and Environmental Science. 1059:012048
The technology that is commonly used to control postharvest pathogen attacks is coating with synthetic chemicals, but this has an unfriendly impact on the environment and consumers. Coating with A. vera L gel and plant extracts is a natural way to ex
Autor:
Narla Mohandas, Karen Mays, Dennis E. Discher, Clare Kelley, R Winardi, John G. Conboy, Len Zon
Publikováno v:
Blood. 86:4315-4322
A developmental alternative splicing switch, involving exon 16 of protein 4.1 pre-mRNA, occurs during mammalian erythropoiesis. By controlling expression of a 21-amino acid peptide required for high- affinity interaction of protein 4.1 with spectrin
Autor:
H. Ewa Witkowska, Narla Mohandas, John G. Conboy, R Winardi, Dennis E. Discher, Stephen E. Bicknese, P. Olivier Schischmanoff, Marilyn Parra
Publikováno v:
Journal of Biological Chemistry. 270:21243-21250
The spectrin-actin-binding domain of protein 4.1 is encoded by a 21-amino acid alternative exon and a 59-amino acid constitutive exon. To characterize the minimal domain active for interactions with spectrin and actin, we functionally characterized r
Autor:
Narla Mohandas, John G. Conboy, R Winardi, P O Schischmanoff, Marilyn Parra, Dennis E. Discher
Publikováno v:
The Journal of Cell Biology
Mechanical strength of the red cell membrane is dependent on ternary interactions among the skeletal proteins, spectrin, actin, and protein 4.1. Protein 4.1's spectrin-actin-binding (SAB) domain is specified by an alternatively spliced exon encoding
Publikováno v:
Blood. 81:2799-2803
Human erythrocyte glycophorin C plays a functionally important role in maintaining erythrocyte shape and regulating membrane mechanical stability. We report here the characterization of the glycophorins C and D deficiency in erythrocytes of the Leach
Publikováno v:
Journal of Clinical Investigation. 91:77-82
Multiple protein 4.1 isoforms are expressed in a variety of tissues through complex alternative pre-mRNA splicing events, one function of which is to regulate use of two alternative translation initiation signals. Late erythroid cells express mainly
Publikováno v:
Blood. 78:2438-2443
Protein 4.1 is an important structural component of the membrane skeleton that helps determine erythrocyte morphology and membrane mechanical properties. In a previous study we identified a case of human hereditary elliptocytosis (HE) in which decrea
Publikováno v:
Blood. 81(10)
Human erythrocyte glycophorin C plays a functionally important role in maintaining erythrocyte shape and regulating membrane mechanical stability. We report here the characterization of the glycophorins C and D deficiency in erythrocytes of the Leach
Autor:
A Leung, E George, Narla Mohandas, Marilyn Parra, Joel Anne Chasis, R Winardi, John G. Conboy, David W. Knowles
Hereditary ovalocytic red cells are characterized by a marked increase in membrane rigidity and resistance to invasion by malarial parasites. The underlying molecular defect in ovalocytes remained a mystery until Liu and colleagues (N. Engl. J. Med.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9697f3f51e7fbbfb5982f8e09e1c8056
https://europepmc.org/articles/PMC442903/
https://europepmc.org/articles/PMC442903/
Publikováno v:
Blood. 78(9)
Protein 4.1 is an important structural component of the membrane skeleton that helps determine erythrocyte morphology and membrane mechanical properties. In a previous study we identified a case of human hereditary elliptocytosis (HE) in which decrea