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protein 4.1

 
National Institutes of Health

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Highly Cited
2005
Highly Cited
2005
Erythrocyte membrane mechanical function is regulated by the spectrin-based membrane skeleton composed of alpha- and beta… Expand
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Highly Cited
2001
Highly Cited
2001
Rearrangements of the actin cytoskeleton are involved in a variety of cellular processes from locomotion of cells to… Expand
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Highly Cited
2000
Highly Cited
2000
Meningiomas are common nervous system tumors, whose molecular pathogenesis is poorly understood. To date, the most frequent… Expand
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Highly Cited
1999
Highly Cited
1999
We report the molecular cloning and characterization of 4.1N, a novel neuronal homolog of the erythrocyte membrane cytoskeletal… Expand
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Highly Cited
1998
Highly Cited
1998
In Caenorhabditis elegans, mutations in the lin-2 gene inactivate the LET-23 receptor tyrosine kinase/Ras/MAP kinase pathway… Expand
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Highly Cited
1996
Highly Cited
1996
Septate and tight junctions are thought to seal neighboring cells together and to function as barriers between epithelial cells… Expand
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Highly Cited
1995
Highly Cited
1995
Protein 4.1 is the prototype of a family of proteins that include ezrin, talin, brain tumor suppressor merlin, and tyrosine… Expand
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Highly Cited
1994
Highly Cited
1994
The Drosophila discs large tumor suppressor protein, dlg, has been shown to regulate the growth of imaginal discs during… Expand
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Highly Cited
1985
Highly Cited
1985
Protein 4.1 from human erythrocytes formed a complex with band 3 in inside-out erythrocyte membrane vesicles and with soluble… Expand
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Highly Cited
1985
Highly Cited
1985
Many of the physical properties of the erythrocyte membrane appear to depend on the membrane skeleton, which is attached to the… Expand
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