TY  - GEN
N2  - The assays developed in this thesis research also offer a path to address some remaining gaps in our knowledge such as substrate assisted gate closure and the substrate release mechanism. The mechanism elucidated in this thesis should also be applicable to human glutamate transporters since the residues identified as important in GltPh are conserved in humans and in their placement in the protein's quaternary structure.
DO  - 10.6083/cz30pt397
DO  - DOI
AB  - The assays developed in this thesis research also offer a path to address some remaining gaps in our knowledge such as substrate assisted gate closure and the substrate release mechanism. The mechanism elucidated in this thesis should also be applicable to human glutamate transporters since the residues identified as important in GltPh are conserved in humans and in their placement in the protein's quaternary structure.
T1  - The transport mechanism of a glutamate transporter homolog
DA  - 2021
AU  - Riederer, Erika A.
L1  - https://digitalcollections.ohsu.edu/record/8957/files/Riederer.Erika.2021.pdf
PB  - Oregon Health and Science University
PY  - 2021
ID  - 8957
L4  - https://digitalcollections.ohsu.edu/record/8957/files/Riederer.Erika.2021.pdf
KW  - Ions
KW  - Mutagenesis
KW  - Fluorescence
KW  - Biological Transport
KW  - Binding Sites
KW  - Molecular Conformation
TI  - The transport mechanism of a glutamate transporter homolog
Y1  - 2021
L2  - https://digitalcollections.ohsu.edu/record/8957/files/Riederer.Erika.2021.pdf
LK  - https://digitalcollections.ohsu.edu/record/8957/files/Riederer.Erika.2021.pdf
UR  - https://digitalcollections.ohsu.edu/record/8957/files/Riederer.Erika.2021.pdf
ER  -