The Capsid Domain of Arc Changes Its Oligomerization Propensity through Direct Interaction with the NMDA Receptor.
Nielsen, Lau Dalby
The Capsid Domain of Arc Changes Its Oligomerization Propensity through Direct Interaction with the NMDA Receptor. [electronic resource] - Structure (London, England : 1993) 07 2019 - 1071-1081.e5 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1878-4186
10.1016/j.str.2019.04.001 doi
Amino Acid Sequence
Animals
Binding Sites
Capsid Proteins--chemistry
Cloning, Molecular
Crystallography, X-Ray
Cytoskeletal Proteins--chemistry
Escherichia coli--genetics
Gene Expression
Genetic Vectors--chemistry
Humans
Kinetics
Models, Molecular
Nerve Tissue Proteins--chemistry
Neurons--chemistry
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Protein Multimerization
Rats
Receptors, N-Methyl-D-Aspartate--chemistry
Recombinant Proteins--chemistry
Sequence Alignment
Sequence Homology, Amino Acid
The Capsid Domain of Arc Changes Its Oligomerization Propensity through Direct Interaction with the NMDA Receptor. [electronic resource] - Structure (London, England : 1993) 07 2019 - 1071-1081.e5 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1878-4186
10.1016/j.str.2019.04.001 doi
Amino Acid Sequence
Animals
Binding Sites
Capsid Proteins--chemistry
Cloning, Molecular
Crystallography, X-Ray
Cytoskeletal Proteins--chemistry
Escherichia coli--genetics
Gene Expression
Genetic Vectors--chemistry
Humans
Kinetics
Models, Molecular
Nerve Tissue Proteins--chemistry
Neurons--chemistry
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Protein Multimerization
Rats
Receptors, N-Methyl-D-Aspartate--chemistry
Recombinant Proteins--chemistry
Sequence Alignment
Sequence Homology, Amino Acid