Results 181 to 190 of about 25,119 (232)
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Brain α erythroid spectrin: identification, compartmentalization, and β spectrin associations
Brain Research, 1994Using 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 ...
Jane E Barker +2 more
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Current Biology, 2021
Lindsay Teliska and Matthew Rasband introduce spectrins - cytoskeletal proteins that localise to the inner face of the plasma membrane and serve a scaffolding function between membrane proteins and the actin cortex.
Lindsay H, Teliska, Matthew N, Rasband
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Lindsay Teliska and Matthew Rasband introduce spectrins - cytoskeletal proteins that localise to the inner face of the plasma membrane and serve a scaffolding function between membrane proteins and the actin cortex.
Lindsay H, Teliska, Matthew N, Rasband
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Avian lens spectrin: subunit composition compared with erythrocyte and brain spectrin. [PDF]
Journal of Cell Biology, 1983 Chicken lens spectrin is composed predominantly of equimolar amounts of two polypeptides with solubility properties similar, but not identical, to erythrocyte spectrin.
Bruce L Granger +2 more
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Translational Research, 2022
Spectrin, as one of the major components of a plasma membrane-associated cytoskeleton, is a cytoskeletal protein composed of the modular structure of α and β subunits. The spectrin-based skeleton is essential for preserving the integrity and mechanical characteristics of the cell membrane.
Shan, Li +7 more
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Spectrin, as one of the major components of a plasma membrane-associated cytoskeleton, is a cytoskeletal protein composed of the modular structure of α and β subunits. The spectrin-based skeleton is essential for preserving the integrity and mechanical characteristics of the cell membrane.
Shan, Li +7 more
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Cell Motility, 1983
AbstractWe have investigated the presence and localization of an α‐spectrinlike protein and its potential role in the morphological transformation of sea urchin coelomocytes. In immunofluorescence images there is a diffuse fluorescence throughout the petaloid cytoplasm, indicating a random distribution of the spectrinlike protein prior to the ...
K T, Edds, J, Venuti-Henderson
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AbstractWe have investigated the presence and localization of an α‐spectrinlike protein and its potential role in the morphological transformation of sea urchin coelomocytes. In immunofluorescence images there is a diffuse fluorescence throughout the petaloid cytoplasm, indicating a random distribution of the spectrinlike protein prior to the ...
K T, Edds, J, Venuti-Henderson
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Critical Reviews in Biochemistry, 1988
This review begins with a complete discussion of the erythrocyte spectrin membrane skeleton. Particular attention is given to our current knowledge of the structure of the RBC spectrin molecule, its synthesis, assembly, and turnover, and its interactions with spectrin-binding proteins (ankyrin, protein 4.1, and actin). We then give a historical account
Steven R. Goodman +5 more
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This review begins with a complete discussion of the erythrocyte spectrin membrane skeleton. Particular attention is given to our current knowledge of the structure of the RBC spectrin molecule, its synthesis, assembly, and turnover, and its interactions with spectrin-binding proteins (ankyrin, protein 4.1, and actin). We then give a historical account
Steven R. Goodman +5 more
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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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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, 1978AbstractThe 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, 1997AbstractWe 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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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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Knowledge of the structure and function of the red-cell membrane has increased during the past several years.
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