Hochschulschrift
Cell-free expression and solution NMR of the N-terminal domain TMD0 of the lysosomal ABC transporter TAPL
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Dimensions
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30 cm
- Extent
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XI, 138 Seiten
- Language
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Englisch
- Notes
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Illustrationen, Diagramme
Johann Wolfgang Goethe-Universität in Frankfurt am Main, Dissertation, 2015
- Keyword
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Membranproteine
Carrier-Proteine
Molekülstruktur
Strukturbiologie
NMR-Spektroskopie
- Creator
- Table of contents
- Rights
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Bei diesem Objekt liegt nur das Inhaltsverzeichnis digital vor. Der Zugriff darauf ist unbeschränkt möglich.
- Last update
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11.03.2025, 12:11 PM CET
Data provider
This object is provided by:
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Object type
- Hochschulschrift
Associated
Other Objects (12)
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Characterization of the lysosomal targeting of the ABC transporter TAPL
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Structural and functional characterization of the lysosomal peptide transporter TAPL
Functional reconstitution of the human lysosomal peptide transporter TAPL reveals the substrate specificity
Current Methods to Unravel the Functional Properties of Lysosomal Ion Channels and Transporters
XJ single-lipospme based mechanistic studies of peptide translocation by the lysosomal ABC transporter TAPL
Peptide translocation by the lysosomal ABC transporter TAPL is regulated by coupling efficiency and activation energy
Lysosomal and mitochondrial crosstalk: the role of lysosomal signaling on mitochondrial biogenesis and function
The role of CLN3 in the lysosomal-autophagosomal system
Cell-free expression of GPCRs: the endothelin system
Cell-free expression of GPCRs : the endothelin system
Subcellular targeting, stabilization & interaction mediated by the N-terminal TMDO of the lysosomal peptide transporter TAPL
Characterization of the lysosomal targeting of the ABC transporter TAPL
An inventory of lysosomal ABC transporters
Structural and functional characterization of the lysosomal peptide transporter TAPL
Functional reconstitution of the human lysosomal peptide transporter TAPL reveals the substrate specificity
Current Methods to Unravel the Functional Properties of Lysosomal Ion Channels and Transporters
XJ single-lipospme based mechanistic studies of peptide translocation by the lysosomal ABC transporter TAPL
Peptide translocation by the lysosomal ABC transporter TAPL is regulated by coupling efficiency and activation energy
Lysosomal and mitochondrial crosstalk: the role of lysosomal signaling on mitochondrial biogenesis and function
The role of CLN3 in the lysosomal-autophagosomal system
Cell-free expression of GPCRs: the endothelin system
Cell-free expression of GPCRs : the endothelin system
Subcellular targeting, stabilization & interaction mediated by the N-terminal TMDO of the lysosomal peptide transporter TAPL
Characterization of the lysosomal targeting of the ABC transporter TAPL
An inventory of lysosomal ABC transporters
Structural and functional characterization of the lysosomal peptide transporter TAPL
Functional reconstitution of the human lysosomal peptide transporter TAPL reveals the substrate specificity
Current Methods to Unravel the Functional Properties of Lysosomal Ion Channels and Transporters
XJ single-lipospme based mechanistic studies of peptide translocation by the lysosomal ABC transporter TAPL
Peptide translocation by the lysosomal ABC transporter TAPL is regulated by coupling efficiency and activation energy
Lysosomal and mitochondrial crosstalk: the role of lysosomal signaling on mitochondrial biogenesis and function
The role of CLN3 in the lysosomal-autophagosomal system
Cell-free expression of GPCRs: the endothelin system