(Q28259392)

English

Purification and characterization of erythrocyte caldesmon. Hypothesis for an actin-linked regulation of a contractile activity in the red blood cell membrane

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scholarly article

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Purification and characterization of erythrocyte caldesmon. Hypothesis for an actin-linked regulation of a contractile activity in the red blood cell membrane (English)

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author name string

E der Terrossian

1

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C Deprette

2

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I Lebbar

3

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R Cassoly

4

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language of work or name

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publication date

15 January 1994

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219

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1-2

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503-11

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Modulation of spectrin-actin assembly by erythrocyte adducin

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https://api.crossref.org/works/10.1111/J.1432-1033.1994.TB19965.X

20 April 2017

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1 reference

https://api.crossref.org/works/10.1111%2FJ.1432-1033.1994.TB19965.X

20 April 2017

The spectrin-actin junction of erythrocyte membrane skeletons

1 reference

https://api.crossref.org/works/10.1111%2FJ.1432-1033.1994.TB19965.X

21 January 2018

The labelling of proteins to high specific radioactivities by conjugation to a 125I-containing acylating agent. Application to the radioimmunoassay

1 reference

https://api.crossref.org/works/10.1111%2FJ.1432-1033.1994.TB19965.X

21 January 2018

Interaction of caldesmon with phospholipids

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https://api.crossref.org/works/10.1111%2FJ.1432-1033.1994.TB19965.X

21 January 2018

Involvement of caldesmon at the actin-myosin interface

1 reference

https://api.crossref.org/works/10.1111%2FJ.1432-1033.1994.TB19965.X

21 January 2018

Visualization of the hexagonal lattice in the erythrocyte membrane skeleton

1 reference

https://api.crossref.org/works/10.1111%2FJ.1432-1033.1994.TB19965.X

21 January 2018

Caldesmon-phospholipid interaction. Effect of protein kinase C phosphorylation and sequence similarity with other phospholipid-binding proteins.

1 reference

https://api.crossref.org/works/10.1111%2FJ.1432-1033.1994.TB19965.X

21 January 2018

Identifiers

10.1111/J.1432-1033.1994.TB19965.X

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