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Effect of pH on the Mechanism of Actin Polymerization
Chris T. Zimmerle,
Carl Frieden
Department of Biochemistry & Molecular Biophysics
Roy and Diana Vagelos Division of Biology & Biomedical Sciences (DBBS)
Institute of Clinical and Translational Sciences (ICTS)
Bursky Center for Human Immunology & Immunotherapy Programs (CHiiPs)
Research output
:
Contribution to journal
›
Article
›
peer-review
42
Scopus citations
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Keyphrases
Mg2+
100%
Actin Polymerization
100%
PH Effect
100%
Ca2+
66%
Actin
66%
G-actin
66%
Mg2+ Binding
66%
Order of Magnitude
33%
High Affinity
33%
Low Affinity
33%
Actin Filaments
33%
Skeletal muscle
33%
Isomerization
33%
PH Range
33%
Low pH
33%
Non-specific Binding
33%
Critical Concentration
33%
Ca2+ Release
33%
Filament Formation
33%
Kinetic Data
33%
Trimer Formation
33%
Kinetic Mechanism
33%
Polymerization Kinetics
33%
Chemistry
Polymerization
100%
formation
75%
Filament
50%
Nucleation
50%
Kd
25%
Kinetics Type
25%
Isomerization
25%
Polymerization Kinetics
25%
Ethane
25%
dimer
25%
Biochemistry, Genetics and Molecular Biology
Actin
100%
Actin Polymerization
100%
Nucleation
40%
Skeletal Muscle
20%
Conformation
20%
Isomerization
20%
Kinetics
20%
Leporidae
20%
Neuroscience
Actin Polymerization
100%
Actin
100%
Actin Filament
25%
Skeletal Muscle
25%
Material Science
Polymerization
100%
Nucleation
50%
Polymerization Kinetics
25%
Engineering
Polymerization
100%
Polymerization Kinetics
25%
Critical Concentration
25%
Initial Concentration
25%