Hochschulschrift
Molecular identification and electrophysiological characterization of the volume-regulated anion channel VRAC
- Weitere Titel
-
Molekulare Identifikation und elektrophysiologische Charakterisierung des volumenregulierten Anionenkanals VRAC
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
-
Online-Ressource
- Sprache
-
Englisch
- Anmerkungen
-
Berlin, Freie Universität Berlin, Dissertation, 2017
- Klassifikation
-
Biowissenschaften, Biologie
- Ereignis
-
Veröffentlichung
- (wo)
-
Berlin
- (wer)
-
Freie Universität Berlin
- (wann)
-
2017
- Urheber
-
Ullrich, Florian
- URN
-
urn:nbn:de:kobv:188-fudissthesis000000103931-4
- Rechteinformation
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
25.03.2025, 13:54 MEZ
Datenpartner
Dieses Objekt wird bereitgestellt von:
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Objekttyp
- Hochschulschrift
Beteiligte
- Ullrich, Florian
- Freie Universität Berlin
Entstanden
- 2017
Ähnliche Objekte (12)
Molecular identification of the volume-regulated anion channel VRAC by a genome-wide siRNA screen
The role of the volume-regulated anion channel VRAC/LRRC8 in myoblast differentiation
Identification and electrophysiological characterization of NpHV1: a new voltage-gated proton channel
Importance of volume-regulated anion channel subunit LRRC8A for hypotonic stress response and differentiation of human keratinocytes
Investigation of the LRRC8 subunit composition and the activating signal transduction of the volume-regulated anion channel (VRAC)
Voltage dependent anion channel: Interaction with lipid membranes
Voltage dependent anion channel: interaction with lipid membranes
Investigation of the activation mechanism of the volume-regulated anion channel VRAC and its role in cell proliferation and migration
Inactivation and anion selectivity of volume-regulated anion channels depend on C-terminal residues of the first extracellular loop
Light-Regulated Transcription of a Mitochondrial-Targeted K⁺ Channel
Structural basis of the mitochondrial voltage-dependent anion channel VDAC I
Time-resolved spectroscopic and electrophysiological data reveal insights in the gating mechanism of anion channelrhodopsin
Molecular identification of the volume-regulated anion channel VRAC by a genome-wide siRNA screen
The role of the volume-regulated anion channel VRAC/LRRC8 in myoblast differentiation
Identification and electrophysiological characterization of NpHV1: a new voltage-gated proton channel
Importance of volume-regulated anion channel subunit LRRC8A for hypotonic stress response and differentiation of human keratinocytes
Investigation of the LRRC8 subunit composition and the activating signal transduction of the volume-regulated anion channel (VRAC)
Voltage dependent anion channel: Interaction with lipid membranes
Voltage dependent anion channel: interaction with lipid membranes
Investigation of the activation mechanism of the volume-regulated anion channel VRAC and its role in cell proliferation and migration
Inactivation and anion selectivity of volume-regulated anion channels depend on C-terminal residues of the first extracellular loop
Light-Regulated Transcription of a Mitochondrial-Targeted K⁺ Channel
Structural basis of the mitochondrial voltage-dependent anion channel VDAC I
Time-resolved spectroscopic and electrophysiological data reveal insights in the gating mechanism of anion channelrhodopsin
Molecular identification of the volume-regulated anion channel VRAC by a genome-wide siRNA screen
The role of the volume-regulated anion channel VRAC/LRRC8 in myoblast differentiation
Identification and electrophysiological characterization of NpHV1: a new voltage-gated proton channel
Importance of volume-regulated anion channel subunit LRRC8A for hypotonic stress response and differentiation of human keratinocytes
Investigation of the LRRC8 subunit composition and the activating signal transduction of the volume-regulated anion channel (VRAC)
Voltage dependent anion channel: Interaction with lipid membranes
Voltage dependent anion channel: interaction with lipid membranes
Investigation of the activation mechanism of the volume-regulated anion channel VRAC and its role in cell proliferation and migration
Inactivation and anion selectivity of volume-regulated anion channels depend on C-terminal residues of the first extracellular loop
Light-Regulated Transcription of a Mitochondrial-Targeted K⁺ Channel
Structural basis of the mitochondrial voltage-dependent anion channel VDAC I