Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate (Q59072772)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:3027569 AND SRC:MED&resulttype=core&format=json

9 October 2019

title

Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate (English)

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:3027569 AND SRC:MED&resulttype=core&format=json

9 October 2019

author name string

Janmey PA

series ordinal

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:3027569 AND SRC:MED&resulttype=core&format=json

9 October 2019

Stossel TP

series ordinal

2

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:3027569 AND SRC:MED&resulttype=core&format=json

9 October 2019

language of work or name

English

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publication date

1 January 1987

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9 October 2019

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:3027569 AND SRC:MED&resulttype=core&format=json

9 October 2019

volume

325

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9 October 2019

issue

6102

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9 October 2019

page(s)

362-364

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Control of cytoplasmic actin gel–sol transformation by gelsolin, a calcium-dependent regulatory protein

9 October 2019

cites work

1 reference

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Interactions of gelsolin and gelsolin-actin complexes with actin. Effects of calcium on actin nucleation, filament severing, and end blocking

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Kinetic analysis of F-actin depolymerization in the presence of platelet gelsolin and gelsolin-actin complexes

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The actin filament-severing domain of plasma gelsolin

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Structure of molecular aggregates of 1-(3-sn-phosphatidyl)-l-myo-inositol 3,4-bis(phosphate) in water

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Sequential binding of actin monomers to plasma gelsolin and its inhibition by vitamin D-binding protein.

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Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain

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Bovine serum brevin. Purification by hydrophobic chromatography and properties.

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Fluorescence study of brevin, the Mr 92 000 actin-capping and -fragmenting protein isolated from serum. Effect of Ca2 on protein conformation.

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Common domain structure of Ca2 and lipid-binding proteins

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Human platelets contain phospholipase C that hydrolyzes polyphosphoinositides

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Dissociation of Ca2 mobilization from breakdown of phosphatidylinositol 4,5-bisphosphate in activated human platelets

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7 January 2021