Signal peptide peptidase functions in ERAD to cleave the unfolded protein response regulator XBP1uSelf-interaction of a SNARE transmembrane domain promotes the hemifusion-to-fusion transition.In vitro selection of self-interacting transmembrane segments--membrane proteins approached from a different perspective.Ionic interactions promote transmembrane helix-helix association depending on sequence context.Tryptophan supports interaction of transmembrane helices.Solid-phase synthesis and purification of a set of uniformly 13C, 15N labelled de novo designed membrane fusogenic peptides.GxxxG motifs within the amyloid precursor protein transmembrane sequence are critical for the etiology of Abeta42.An extended ToxR POSSYCCAT system for positive and negative selection of self-interacting transmembrane domains.Complex patterns of histidine, hydroxylated amino acids and the GxxxG motif mediate high-affinity transmembrane domain interactions.Amyloid beta 42 peptide (Abeta42)-lowering compounds directly bind to Abeta and interfere with amyloid precursor protein (APP) transmembrane dimerization.Homodimerization Protects the Amyloid Precursor Protein C99 Fragment from Cleavage by γ-Secretase.Functions of SNAREs in intracellular membrane fusion and lipid bilayer mixing.Identifying ionic interactions within a membrane using BLaTM, a genetic tool to measure homo- and heterotypic transmembrane helix-helix interactions.Interaction and conformational dynamics of membrane-spanning protein helices.De novo design of conformationally flexible transmembrane peptides driving membrane fusion.Phenylalanine promotes interaction of transmembrane domains via GxxxG motifs.Role of GxxxG Motifs in Transmembrane Domain Interactions.Side-chain to main-chain hydrogen bonding controls the intrinsic backbone dynamics of the amyloid precursor protein transmembrane helixDirect visualization of large and protein-free hemifusion diaphragmsEntrapment of Water at the Transmembrane Helix-Helix Interface of Quiescin Sulfhydryl Oxidase 2.The interface between self-assembling erythropoietin receptor transmembrane segments corresponds to a membrane-spanning leucine zipper.Sequence-specific conformational flexibility of SNARE transmembrane helices probed by hydrogen/deuterium exchange.Stabilization of conformationally dynamic helices by covalently attached acyl chains.Sequence-dependent backbone dynamics of a viral fusogen transmembrane helix.The backbone dynamics of the amyloid precursor protein transmembrane helix provides a rationale for the sequential cleavage mechanism of γ-secretase.The interface of a membrane-spanning leucine zipper mapped by asparagine-scanning mutagenesis.A solid-state NMR study of changes in lipid phase induced by membrane-fusogenic LV-peptides.Synaptobrevin transmembrane domain dimerization-revisited.Structural features of fusogenic model transmembrane domains that differentially regulate inner and outer leaflet mixing in membrane fusion.Is lipid flippase activity of SNARE transmembrane domains required for membrane fusion?Self-interaction of transmembrane helices representing pre-clusters from the human single-span membrane proteins.Solid-phase extraction as a tool to remove impurities and small fragments from synthetic peptides.BLaTM 2.0, a Genetic Tool Revealing Preferred Antiparallel Interaction of Transmembrane Helix 4 of the Dual-Topology Protein EmrE.Substrate processing in intramembrane proteolysis by γ-secretase - the role of protein dynamics.Gas-phase behavior of noncovalent transmembrane segment complexes.The cleavage domain of the amyloid precursor protein transmembrane helix does not exhibit above-average backbone dynamics.Increased H-Bond Stability Relates to Altered ε-Cleavage Efficiency and Aβ Levels in the I45T Familial Alzheimer's Disease Mutant of APP
P50
Q24304271-51726073-6C14-468B-A9F8-0CB8E4F6DD63Q27936090-D61B9E00-CFAD-4F0B-99E3-06D14C54F91DQ30875805-EDB34E82-5F8E-4BC7-B930-1C5E49F41BAEQ30955497-62924BC1-6DF9-46C2-B27D-20604E8D5BCAQ33226928-4B045F04-1077-4E52-9DC6-9B32613FA8EDQ33264392-5EC2BD57-A2A0-442D-A8BE-4E85187049F0Q33276402-F183987B-9663-42E7-9B67-81F6BEE6F443Q33277473-AB6107B2-0C81-4F25-8FE6-085AC859D6AFQ33384330-0BAFD10A-687E-4BDE-8CE7-EDCEC80D8277Q34093329-6CD324E6-4E33-4E1D-8B4F-BDFE3730AC28Q35787111-E195275C-1583-422B-8195-3C1644C223D7Q36243923-CCCF02FD-CD90-4B44-A2CC-1E601E4E6487Q36299114-DDF2653F-3B98-46EC-AEFB-65762FF5A209Q37520862-A9377776-BB42-44FD-B7B4-4ABE6F4E5CAFQ37571104-0D1422E2-5C90-462F-A675-55042610042EQ38297192-73C3F09E-C240-44F9-A881-23C2CD4EFE29Q38561235-B5BB25CF-EDD1-49CD-A261-469E830F4772Q38725946-7CBF915F-FB75-4A73-86F1-093AF5FC9DA0Q39887494-817AA45C-EC17-440C-8DA3-8930CD46CBA3Q39984816-F88B21A9-F238-4478-B997-76A5D6565E95Q40619204-E180430D-4307-4F2F-8A12-6DE202F8D856Q40769084-D75128FB-9E3A-4FD1-833C-F0D4DAF16DFBQ41818340-0D59443A-2CBF-4723-B68F-F800F15BADC3Q41890205-DA4CDE61-3AA7-47E4-9009-A03E5C300B3AQ42092456-3BE6CD07-BCAD-42E6-9756-E8C93EA58802Q43105230-66F7D25D-A2F2-44DE-B812-4C350EA5DBAEQ43251266-054DB320-CEC3-4D6C-9C4F-8FA5D35BA34CQ44861325-D198127B-71EB-414A-9E93-DDC5D44D47EBQ45237236-08ED151F-D8C8-4BA5-8701-AD226CCA2332Q45328916-96313499-8CC1-482B-99C9-BAB1BFD1DF5EQ45838200-B0FC9702-0706-4030-B757-70DAF99CBE9CQ46615456-481063A8-7274-490D-A44D-093E5235AF79Q51041058-42BC46AD-41E9-4005-9C41-AFD51728FCA8Q51326618-4EC7E60F-5C43-44F5-89A3-8E4C6487C64BQ51960497-512653A3-7B95-44FA-92EF-8F347174515CQ53087150-8BC796A5-0FAB-4FE6-B9BA-4BBF47A6E60EQ59480081-C496DAD5-1BAA-44E6-82D6-73FA76789538
P50
description
Duits biochemicus
@nl
German biochemist
@en
bithchemiceoir Gearmánach
@ga
chimiste allemand
@fr
deutscher Biochemiker und Hochschullehrer
@de
professor académico alemão
@pt
tysk professor
@da
tysk professor
@sv
name
Dieter Langosch
@ast
Dieter Langosch
@ca
Dieter Langosch
@da
Dieter Langosch
@de
Dieter Langosch
@en
Dieter Langosch
@es
Dieter Langosch
@fr
Dieter Langosch
@it
Dieter Langosch
@nds
Dieter Langosch
@nl
type
label
Dieter Langosch
@ast
Dieter Langosch
@ca
Dieter Langosch
@da
Dieter Langosch
@de
Dieter Langosch
@en
Dieter Langosch
@es
Dieter Langosch
@fr
Dieter Langosch
@it
Dieter Langosch
@nds
Dieter Langosch
@nl
prefLabel
Dieter Langosch
@ast
Dieter Langosch
@ca
Dieter Langosch
@da
Dieter Langosch
@de
Dieter Langosch
@en
Dieter Langosch
@es
Dieter Langosch
@fr
Dieter Langosch
@it
Dieter Langosch
@nds
Dieter Langosch
@nl
P106
P214
P227
P1412
P1559
Dieter Langosch
@de
P19
P21
P214
P227
1207481556
P31
P569
1958-01-31T00:00:00Z