[NMR paper] Backbone NMR assignments of the extensive human and chicken TRPV4 N-terminal intrinsically disordered regions as important players in ion channel regulation
Backbone NMR assignments of the extensive human and chicken TRPV4 N-terminal intrinsically disordered regions as important players in ion channel regulation
Transient receptor potential (TRP) channels are important pharmacological targets due to their ability to act as sensory transducers on the organismic and cellular level, as polymodal signal integrators and because of their role in numerous diseases. However, a detailed molecular understanding of the structural dynamics of TRP channels and their integration into larger cellular signalling networks remains challenging, in part due to the systematic absence of highly dynamic regions pivotal for...
[NMR paper] Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant
Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant
Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative disorders associated with the misfolding and aggregation of the human prion protein (huPrP). Despite efforts into investigating the process of huPrP aggregation, the mechanisms triggering its misfolding remain elusive. A number of TSE-associated mutations of huPrP have been identified, but their role at the onset and progression of prion diseases is unclear. Here we report the NMR assignments of...
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[NMR paper] Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.
Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Backbone NMR assignments of the C-terminal domain of the human prion protein and its disease-associated T183A variant.
Biomol NMR Assign. 2021 Feb 15;:
Authors: Sanz-Hernández M, De Simone A
Abstract
Transmissible spongiform encephalopathies (TSEs) are fatal...
Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion
Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion
Abstract We present the de novo resonance assignments for the crystalline 33 kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly 13C, 15N labeled protein sample, sequential chemical-shift information for 74% of the N, Cα, Cβ triples, and for 80% of further side-chain resonances for these spin systems. We describe the procedures and protocols devised, and discuss possibilities and limitations of the...
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08-04-2011 01:14 AM
Extensive de novo solid-state NMR assignments of the 33*kDa C-terminal domain of the Ure2 prion.
Extensive de novo solid-state NMR assignments of the 33*kDa C-terminal domain of the Ure2 prion.
Extensive de novo solid-state NMR assignments of the 33*kDa C-terminal domain of the Ure2 prion.
J Biomol NMR. 2011 Jul 31;
Authors: Habenstein B, Wasmer C, Bousset L, Sourigues Y, Schütz A, Loquet A, Meier BH, Melki R, Böckmann A
We present the de novo resonance assignments for the crystalline 33*kDa C-terminal domain of the Ure2 prion using an optimized set of five 3D solid-state NMR spectra. We obtained, using a single uniformly (13)C, (15)N labeled...
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08-02-2011 11:40 AM
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Backbone and side chain NMR assignments for the intrinsically disordered cytoplasmic domain of human neuroligin-3.
Biomol NMR Assign. 2011 Jun 7;
Authors: Wood K, Paz A, Dijkstra K, Scheek RM, Otten R, Silman I, Sussman JL, Mulder FA
Neuroligins act as heterophilic adhesion molecules at neuronal synapses. Their cytoplasmic domains interact with synaptic scaffolding proteins, and have been shown to be intrinsically disordered. Here we...