Dieter Langosch mainly investigates Biochemistry, Biophysics, Transmembrane domain, Transmembrane protein and Glycine receptor. His work deals with themes such as Amyloid precursor protein secretase and Förster resonance energy transfer, which intersect with Biochemistry. His work in Biophysics covers topics such as Protein structure which are related to areas like Glycophorin and Cell membrane.
The Transmembrane domain study combines topics in areas such as Lipid bilayer, Beta and Membrane protein. The concepts of his Transmembrane protein study are interwoven with issues in Crystallography, Synaptobrevin, Amyloid precursor protein and Syntaxin. His work on Gephyrin as part of general Glycine receptor research is often related to ATP synthase alpha/beta subunits, thus linking different fields of science.
His primary areas of study are Transmembrane domain, Biophysics, Biochemistry, Transmembrane protein and Membrane. His biological study spans a wide range of topics, including Integral membrane protein, Membrane protein, Lipid bilayer and Helix. His studies deal with areas such as Cleavage, Lipid bilayer fusion, Amyloid precursor protein, Protein structure and Peptide as well as Biophysics.
Dieter Langosch has included themes like Protein primary structure and Heptad repeat in his Biochemistry study. His study explores the link between Transmembrane protein and topics such as Cell biology that cross with problems in Ectodomain. The various areas that Dieter Langosch examines in his Membrane study include Crystallography, Nuclear magnetic resonance spectroscopy and Function.
His primary scientific interests are in Biophysics, Transmembrane domain, Cleavage, Amyloid precursor protein and Lipid bilayer. Dieter Langosch has researched Biophysics in several fields, including Peptide bond, Membrane, Lipid bilayer fusion and Protein structure. His Transmembrane domain research incorporates elements of Helix, Active site, Transmembrane protein, Stereochemistry and Membrane protein.
His research investigates the connection between Helix and topics such as Cell biology that intersect with problems in Presenilin, Specific activity and Ectodomain. Within one scientific family, Dieter Langosch focuses on topics pertaining to Protein–protein interaction under Membrane protein, and may sometimes address concerns connected to Crystallography, Fluorophore, Fusion protein and Protein primary structure. He works mostly in the field of Cleavage, limiting it down to topics relating to Intramembrane protease and, in certain cases, Protease and Nuclear magnetic resonance spectroscopy.
Biophysics, Transmembrane domain, Cleavage, Lipid bilayer and Amyloid precursor protein are his primary areas of study. Dieter Langosch connects Biophysics with Hinge in his study. Dieter Langosch interconnects Lipid bilayer fusion, Helix, Active site, Peptide bond and Membrane protein in the investigation of issues within Transmembrane domain.
His Lipid bilayer fusion study combines topics from a wide range of disciplines, such as Liposome, Bilayer, Phosphatidylserine, Phosphatidylethanolamine and Biological membrane. Dieter Langosch focuses mostly in the field of Peptide library, narrowing it down to matters related to Integral membrane protein and, in some cases, Protein structure. The study incorporates disciplines such as Signal peptide peptidase and Regulated Intramembrane Proteolysis, Transmembrane protein in addition to Unfolded protein response.
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Identification of a gephyrin binding motif on the glycine receptor β subunit
Guido Meyer;Joachim Kirsch;Heinrich Betz;Dieter Langosch.
Conserved quaternary structure of ligand-gated ion channels: the postsynaptic glycine receptor is a pentamer.
Dieter Langosch;Leo Thomas;Heinrich Betz.
Proceedings of the National Academy of Sciences of the United States of America (1988)
The atypical M2 segment of the beta subunit confers picrotoxinin resistance to inhibitory glycine receptor channels.
I. Pribilla;T. Takagi;D. Langosch;J. Bormann.
The EMBO Journal (1992)
Identification of synaptophysin as a hexameric channel protein of the synaptic vesicle membrane.
Leo Thomas;Klaus Hartung;Dieter Langosch;Hubert Rehm.
Primary structure and alternative splice variants of gephyrin, a putative glycine receptor-tubulin linker protein
P. Prior;B. Schmitt;G. Grenningloh;I. Pribilla.
GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Aβ42
Lisa-Marie Munter;Philipp Voigt;Anja Harmeier;Daniela Kaden.
The EMBO Journal (2007)
The 93-kDa glycine receptor-associated protein binds to tubulin.
J. Kirsch;D. Langosch;P. Prior;U.Z. Littauer.
Journal of Biological Chemistry (1991)
Dimerisation of the Glycophorin A Transmembrane Segment in Membranes Probed with the ToxR Transcription Activator
Dieter Langosch;Bettina Brosig;Harald Kolmar;Hans-Joachim Fritz.
Journal of Molecular Biology (1996)
Residues within transmembrane segment M2 determine chloride conductance of glycine receptor homo- and hetero-oligomers.
J Bormann;N Rundström;H Betz;D Langosch.
The EMBO Journal (1993)
The dimerization motif of the glycophorin A transmembrane segment in membranes: importance of glycine residues.
Bettina Brosig;Dieter Langosch.
Protein Science (1998)
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