Zobrazeno 1 - 10
of 14
pro vyhledávání: '"J G Conboy"'
Publikováno v:
Journal of Biological Chemistry. 267:18753-18758
Erythroid 5-aminolevulinate synthase (ALAS) is expressed exclusively in differentiating erythroid cells as the principal isoform of the enzyme to catalyze the first step of the heme biosynthetic pathway. The human gene encoding this isozyme was isola
Autor:
Terence P. Speed, Ken M. Simpson, Mark D. Robinson, J. G. Conboy, Elizabeth Purdom, Anna Lapuk
Publikováno v:
Bioinformatics
Motivation: Analyses of EST data show that alternative splicing is much more widespread than once thought. The advent of exon and tiling microarrays means that researchers now have the capacity to experimentally measure alternative splicing on a geno
Publikováno v:
The Journal of biological chemistry. 275(9)
In vitro protein binding assays identified two distinct calmodulin (CaM) binding sites within the NH(2)-terminal 30-kDa domain of erythrocyte protein 4.1 (4.1R): a Ca(2+)-independent binding site (A(264)KKLWKVCVEHHTFFRL) and a Ca(2+)-dependent bindin
Autor:
P, Gascard, G, Lee, L, Coulombel, I, Auffray, M, Lum, M, Parra, J G, Conboy, N, Mohandas, J A, Chasis
Publikováno v:
Blood. 92(11)
In erythrocytes, 80-kD protein 4.1R regulates critical membrane properties of deformability and mechanical strength. However, previously obtained data suggest that multiple isoforms of protein 4. 1, generated by alternative pre-mRNA splicing, are exp
Autor:
J G, Conboy
Publikováno v:
Seminars in hematology. 30(1)
Publikováno v:
The Journal of biological chemistry. 267(26)
Erythroid 5-aminolevulinate synthase (ALAS) is expressed exclusively in differentiating erythroid cells as the principal isoform of the enzyme to catalyze the first step of the heme biosynthetic pathway. The human gene encoding this isozyme was isola
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
Publikováno v:
The Journal of biological chemistry. 266(13)
Protein 4.1, a multifunctional structural protein originally described as an 80-kDa component of the erythroid membrane skeleton, exhibits tissue- and development-specific heterogeneity in molecular weight, subcellular localization, and primary amino
Publikováno v:
Journal of Biological Chemistry. 257:8467-8471
Publikováno v:
Journal of Biological Chemistry. 256:10739-10742
Biogenesis of the mitochondrial matrix enzyme, ornithine transcarbamylase, has been shown to begin with synthesis on cytoplasmic ribosomes of a precursor, designated pre-ornithine transcarbamylase, which is approximately 4000 daltons larger than its