Search Results - "Wüthrich, K"

The formation, function and regulation of amyloids: insights from structural biology by Landreh, M., Sawaya, M. R., Hipp, M. S., Eisenberg, D. S., Wüthrich, K., Hartl, F. U.

“…Amyloid diseases are characterized by the accumulation of insoluble, β‐strand‐rich aggregates. The underlying structural conversions are closely associated…”
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Torsion angle dynamics for NMR structure calculation with the new program DYANA by Güntert, P, Mumenthaler, C, Wüthrich, K

“…The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from…”
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The way to NMR structures of proteins by Wüthrich, Kurt

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NMR spectroscopy of large molecules and multimolecular assemblies in solution by Wider, Gerhard, Wüthrich, Kurt

“…New strategies and technical advances in NMR spectroscopy and biochemical methods for isotope labeling have enabled solution NMR studies of biomacromolecular…”
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Prion (PrP Sc )-specific epitope defined by a monoclonal antibody by Korth, C, Oesch, B, Stierli, B, Streit, P, Moser, M, Schaller, O, Fischer, R, Schulz-Schaeffer, W, Kretzschmar, H, Raeber, A, Braun, U, Ehrensperger, F, Hornemann, S, Glockshuber, R, Riek, R, Billeter, M, Wüthrich, K

“…Prions are infectious particles causing transmissible spongiform encephalopathies (TSEs). They consist, at least in part, of an isoform (PrPSc) of the…”
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TROSY in Triple-Resonance Experiments: New Perspectives for Sequential NMR Assignment of Large Proteins by Salzmann, Michael, Pervushin, Konstantin, Wider, Gerhard, Senn, Hans, Wuthrich, Kurt

“…The NMR assignment of13C,15N-labeled proteins with the use of triple resonance experiments is limited to molecular weights below ∼ 25,000 Daltons, mainly…”
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TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution by Riek, Roland, Pervushin, Konstantin, Wüthrich, Kurt

“…TROSY and CRINEPT are new techniques for solution NMR studies of molecular and supramolecular structures. They allow the collection of high-resolution spectra…”
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NMR characterization of the full-length recombinant murine prion protein, mPrP(23–231) by Riek, Roland, Hornemann, Simone, Wider, Gerhard, Glockshuber, Rudi, Wüthrich, Kurt

“…The recombinant murine prion protein, mPrP(23–231), was expressed in E. coli with uniform 15N-labeling. NMR experiments showed that the previously determined…”
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NMR Structure of the Bovine Prion Protein by Garcia, Francisco Lopez, Zahn, Ralph, Riek, Roland, Wuthrich, Kurt

“…The NMR structures of the recombinant 217-residue polypeptide chain of the mature bovine prion protein, bPrP(23-230), and a C-terminal fragment, bPrP(121-230),…”
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Transverse Relaxation-Optimized NMR Spectroscopy with the Outer Membrane Protein OmpX in Dihexanoyl Phosphatidylcholine Micelles by Fernández, César, Adeishvili, Koba, Wüthrich, Kurt

“…The 2H,13C,15N-labeled, 148-residue integral membrane protein OmpX from Escherichia coli was reconstituted with dihexanoyl phosphatidylcholine (DHPC) in mixed…”
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Polarization Transfer by Cross-Correlated Relaxation in Solution NMR with Very Large Molecules by Riek, Roland, Wider, Gerhard, Pervushin, Konstantin, Wüthrich, Kurt

“…In common multidimensional NMR experiments for studies of biological macromolecules in solution, magnetization transfers via spin-spin couplings [insensitive…”
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Metabolic Flux Responses to Pyruvate Kinase Knockout in Escherichia coli by Emmerling, Marcel, Dauner, Michael, Ponti, Aaron, Fiaux, Jocelyne, Hochuli, Michel, Szyperski, Thomas, Wüthrich, Kurt, Bailey, J E, Sauer, Uwe

“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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Improved spectral resolution in COSY (1)H NMR spectra of proteins via double quantum filtering. 1983 by Rance, M, Sørensen, O W, Bodenhausen, G, Wagner, G, Ernst, R R, Wüthrich, K

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Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli by Fernández, César, Hilty, Christian, Bonjour, Sophie, Adeishvili, Koba, Pervushin, Konstantin, Wüthrich, Kurt

“…Membrane proteins are usually solubilized in polar solvents by incorporation into micelles. Even for small membrane proteins these mixed micelles have rather…”
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Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding by Zahn, Ralph, von Schroetter, Christine, Wüthrich, Kurt

“…An efficient method is presented for the production of intact mammalian prion proteins and partial sequences thereof. As an illustration we describe the…”
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Prion Protein NMR Structure and Familial Human Spongiform Encephalopathies by Riek, Roland, Wider, Gerhard, Billeter, Martin, Hornemann, Simone, Glockshuber, Rudi, Wüthrich, Kurt

“…The refined NMR structure of the mouse prion protein domain mPrP(121-231) and the recently reported NMR structure of the complete 208-residue polypeptide chain…”
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Structure comparison of human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein P14a indicates a functional link between the human immune system and a plant defense system by Szyperski, T. (Institut fur Molekularbiologie und Biophysik, Zurich, Switzerland.), Fernandez, C, Mumenthaler, C, Wuthrich, K

“…The human glioma pathogenesis-related protein (GliPR) is highly expressed in the brain tumor glioblastoma multiforme and exhibits 35% amino acid sequence…”
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NMR Structure of the Calreticulin P-Domain by Ellgaard, Lars, Riek, Roland, Herrmann, Torsten, Güntert, Peter, Braun, Daniel, Helenius, Ari, Wüthrich, Kurt

“…The NMR structure of the rat calreticulin P-domain, comprising residues 189-288, CRT(189-288), shows a hairpin fold that involves the entire polypeptide chain,…”
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Molecular cloning, functional expression and characterisation of RCC reductase involved in chlorophyll catabolism by Wüthrich, Karin L., Bovet, Lucien, Hunziker, Peter E., Donnison, Iain S., Hörtensteiner, Stefan

“…Summary Red chlorophyll catabolite (RCC) reductase (RCCR) and pheophorbide (Pheide) a oxygenase (PaO) catalyse the key reaction of chlorophyll catabolism,…”
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NMR characterization of a pH-dependent equilibrium between two folded solution conformations of the pheromone-binding protein from Bombyx mori by DAMBERGER, FRED, NIKONOVA, LARISA, HORST, RETO, PENG, GUIHONG, LEAL, WALTER SOARES, WÜTHRICH, KURT

“…NMR spectroscopic changes as a function of pH in solutions of the pheromone-binding protein of Bombyx mori (BmPBP) show that BmPBP undergoes a conformational…”
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