Results 141 to 150 of about 21,720 (189)
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Brain spectrin: A review

Brain Research Bulletin, 1984
Red blood cell spectrin, along with actin and several other proteins, forms a skeletal meshwork on the cytoplasmic surface of the erythrocyte plasma membrane. This structure is thought to maintain red blood cell shape, membrane structural stability, and cellular elasticity, as well as controlling the lateral mobility of integral membrane proteins and ...
S R, Goodman, I S, Zagon
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Phosphorylation and dephosphorylation of spectrin

Journal of Supramolecular Structure, 1978
AbstractThe phosphorylation of spectrin polypeptide 2 is thought to be involved in the metabolically dependent regulation of red cell shape and deformability. Spectrin phosphorylation is not affected by cAMP. The reaction in isolated membranes resembles the cAMP‐independent, salt‐stimulated phosphorylation of an exogenous substrate, casein, by enzyme(s)
G, Fairbanks   +3 more
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Evolution of the spectrin repeat

BioEssays, 1997
AbstractWe now know that the evolution of multidomain proteins has frequently involved genetic duplication events. These, however, are sometimes difficult to trace because of low sequence similarity between duplicated segments. Spectrin, the major component of the membrane skeleton that provides elasticity to the cell, contains tandemly repeated ...
J, Pascual, J, Castresana, M, Saraste
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Spectrin and Spherocytosis

New England Journal of Medicine, 1982
Knowledge of the structure and function of the red-cell membrane has increased during the past several years.
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Spectrin and ankyrin in brain

Cell Motility, 1983
AbstractFurther similarity between mammalian erythrocyte spectrin and pig brain spectrin has been demonstrated by (a) formation of hybrid molecules with brain α‐chains and erythrocyte β‐chains and by (b) identification of an ankyrin protein in brain membranes.
V, Bennett, J, Davis
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Brain α erythroid spectrin: identification, compartmentalization, and β spectrin associations

Brain Research, 1994
Using isoform and subunit specific antibodies we have determined the presence, localization, and beta spectrin associations of alpha erythroid spectrin, alpha SpI sigma*, as well as alpha non-erythroid spectrin, alpha SpII sigma 1, in mouse brain. Peptide specific antibodies against unique sequences within the beta SpII sigma 1, non-erythroid beta ...
Warren Zimmer   +2 more
exaly   +3 more sources

β spectrinPRAGUE: a truncated β spectrin producing spectrin deficiency, defective spectrin heterodimer self‐association and a phenotype of spherocytic elliptocytosis

British Journal of Haematology, 1995
Summary. Spherocytic elliptocytosis is a phenotypic hybrid between hereditary spherocytosis (HS) and hereditary elliptocytosis (HE) characterized by the presence of spheroovalocytes and spherocytes which exhibit increased osmotic fragility, indicating a deficiency of surface area.
P, Jarolim   +5 more
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Spectrin: The ghost in the machine

BioEssays, 2001
It has long been speculated that spectrin, the actin crosslinking and molecular scaffold protein, is involved in the development of apicobasal polarity in epithelia. While spectrins can undoubtedly influence the protein content of specific membrane domains, recent genetic evidence indicates that this activity is not necessary for the establishment or ...
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Spectrins

1999
Abstract First identified in the mammalian erythrocyte, spectrins are now recognized as ubiquitous proteins present in all metazoan organisms including plants. Because of this great diversity, a bewildering array of names, such as fodrin, calspectin, brain spectrin, spectrin G, lung spectrin, γ spectrin, 1W260/240, and so on, have been ...
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Interaction of spectrin with phospholipids. Quenching of spectrin intrinsic fluorescence by phospholipid suspensions

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1987
Phospholipid suspensions prepared of phosphatidylethanolamine, phosphatidylserine and their mixtures are able to influence the intrinsic protein fluorescence of spectrin. In the case of phosphatidylethanolamine suspension up to 75% of protein fluorescence can be quenched.
A F, Sikorski, K, Michalak, M, Bobrowska
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