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spelling sg-nus-scholar.10635-1612182024-04-22T03:10:57Z ATP competes with PIP 2 for binding to gelsolin Szatmári D. Xue B. Kannan B. Burtnick L.D. Bugyi B. Nyitrai M. Robinson R.C. BIOCHEMISTRY CHEMICAL & BIOMOLECULAR ENGINEERING adenosine triphosphate calcium gelsolin phosphatidylinositol 4,5 bisphosphate phospholipid sodium chloride actin adenosine triphosphate cation gelsolin magnesium phosphatidylinositol 4,5 bisphosphate protein binding actin filament anisotropy Article cell membrane controlled study cytoplasm enzyme activity enzyme regulation fluorescence human human cell in vitro study protein binding protein function protein protein interaction protein secretion steady state animal binding competition Escherichia coli kinetics Leporidae metabolism polymerization Actins Adenosine Triphosphate Animals Binding, Competitive Calcium Cations Cell Membrane Escherichia coli Gelsolin Humans Kinetics Magnesium Phosphatidylinositol 4,5-Diphosphate Polymerization Protein Binding Rabbits 10.1371/journal.pone.0201826 PLoS ONE 13 8 e0201826 2019-11-01T08:13:16Z 2019-11-01T08:13:16Z 2018 Article Szatmári D., Xue B., Kannan B., Burtnick L.D., Bugyi B., Nyitrai M., Robinson R.C. (2018). ATP competes with PIP 2 for binding to gelsolin. PLoS ONE 13 (8) : e0201826. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0201826 19326203 https://scholarbank.nus.edu.sg/handle/10635/161218 Attribution 4.0 International http://creativecommons.org/licenses/by/4.0/ Unpaywall 20191101
institution National University of Singapore
building NUS Library
continent Asia
country Singapore
Singapore
content_provider NUS Library
collection ScholarBank@NUS
topic adenosine triphosphate
calcium
gelsolin
phosphatidylinositol 4,5 bisphosphate
phospholipid
sodium chloride
actin
adenosine triphosphate
cation
gelsolin
magnesium
phosphatidylinositol 4,5 bisphosphate
protein binding
actin filament
anisotropy
Article
cell membrane
controlled study
cytoplasm
enzyme activity
enzyme regulation
fluorescence
human
human cell
in vitro study
protein binding
protein function
protein protein interaction
protein secretion
steady state
animal
binding competition
Escherichia coli
kinetics
Leporidae
metabolism
polymerization
Actins
Adenosine Triphosphate
Animals
Binding, Competitive
Calcium
Cations
Cell Membrane
Escherichia coli
Gelsolin
Humans
Kinetics
Magnesium
Phosphatidylinositol 4,5-Diphosphate
Polymerization
Protein Binding
Rabbits
spellingShingle adenosine triphosphate
calcium
gelsolin
phosphatidylinositol 4,5 bisphosphate
phospholipid
sodium chloride
actin
adenosine triphosphate
cation
gelsolin
magnesium
phosphatidylinositol 4,5 bisphosphate
protein binding
actin filament
anisotropy
Article
cell membrane
controlled study
cytoplasm
enzyme activity
enzyme regulation
fluorescence
human
human cell
in vitro study
protein binding
protein function
protein protein interaction
protein secretion
steady state
animal
binding competition
Escherichia coli
kinetics
Leporidae
metabolism
polymerization
Actins
Adenosine Triphosphate
Animals
Binding, Competitive
Calcium
Cations
Cell Membrane
Escherichia coli
Gelsolin
Humans
Kinetics
Magnesium
Phosphatidylinositol 4,5-Diphosphate
Polymerization
Protein Binding
Rabbits
Szatmári D.
Xue B.
Kannan B.
Burtnick L.D.
Bugyi B.
Nyitrai M.
Robinson R.C.
ATP competes with PIP 2 for binding to gelsolin
description 10.1371/journal.pone.0201826
author2 BIOCHEMISTRY
author_facet BIOCHEMISTRY
Szatmári D.
Xue B.
Kannan B.
Burtnick L.D.
Bugyi B.
Nyitrai M.
Robinson R.C.
format Article
author Szatmári D.
Xue B.
Kannan B.
Burtnick L.D.
Bugyi B.
Nyitrai M.
Robinson R.C.
author_sort Szatmári D.
title ATP competes with PIP 2 for binding to gelsolin
title_short ATP competes with PIP 2 for binding to gelsolin
title_full ATP competes with PIP 2 for binding to gelsolin
title_fullStr ATP competes with PIP 2 for binding to gelsolin
title_full_unstemmed ATP competes with PIP 2 for binding to gelsolin
title_sort atp competes with pip 2 for binding to gelsolin
publishDate 2019
url https://scholarbank.nus.edu.sg/handle/10635/161218
_version_ 1800913784076763136