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Aip1p dynamics are altered by the R256H mutation in actin
Alyson R. Pierick
, Melissa McKane
, Kuo Kuang Wen
, Heather L. Bartlett
Department of Pediatrics
Department of Cell and Biological Systems
Research output
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Contribution to journal
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Article
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peer-review
1
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Scopus citations
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Dive into the research topics of 'Aip1p dynamics are altered by the R256H mutation in actin'. Together they form a unique fingerprint.
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Keyphrases
Actin
100%
Fluorescence Microscopy
60%
Cytoskeletal Dynamics
40%
Amino Acids
20%
Living Cells
20%
Regulatory Interactions
20%
Protein Function
20%
N-terminus
20%
In Vitro Study
20%
Green Fluorescent Protein
20%
Molecular Changes
20%
Human Disease
20%
Wild Strain
20%
Mutant Strains
20%
Fluorescent Label
20%
Missense mutation
20%
Movement Speed
20%
Yeast Model
20%
Cofilin
20%
Actin Depolymerization
20%
Tagged Protein
20%
Actin Isoforms
20%
Actin mutation
20%
Biochemistry, Genetics and Molecular Biology
Dynamics
100%
Actin
100%
Fluorescence Microscopy
37%
Wild Type
37%
Amino Acids
12%
Protein Function
12%
Isoform
12%
In Vitro Study
12%
Depolymerization
12%
Green Fluorescent Protein
12%
Motion
12%
N-Terminus
12%
Missense Mutation
12%
Cofilin
12%
Fluorescent Tag
12%
Immunology and Microbiology
Dynamics
100%
Actin
100%
Wild Type
37%
Fluorescence Microscopy
37%
Amino Terminal Sequence
12%
Missense Mutation
12%
Depolymerization
12%
Motion
12%
Amino Acid
12%
Protein Function
12%
Neuroscience
Actin
100%
Amino Acid
12%
In Vitro
12%
Amino Terminal Sequence
12%
In Vivo
12%
Protein Function
12%
Missense Mutation
12%
Green Fluorescent Protein
12%
Cofilin
12%
Pharmacology, Toxicology and Pharmaceutical Science
Cofilin
12%