Pages that link to "Q27743024"
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The following pages link to Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform (Q27743024):
Displaying 50 items.
- Prion Protein Biology (Q21972822) (← links)
- The molecular biology of prion propagation. (Q24522314) (← links)
- Prions (Q24633319) (← links)
- Cellular prion protein conformation and function (Q24634850) (← links)
- Hot spots in prion protein for pathogenic conversion (Q24670553) (← links)
- Trans-dominant inhibition of prion propagation in vitro is not mediated by an accessory cofactor (Q27316451) (← links)
- Antibody binding defines a structure for an epitope that participates in the PrPC-->PrPSc conformational change (Q27620158) (← links)
- NMR solution structure of the human prion protein (Q27620845) (← links)
- NMR structure of the bovine prion protein (Q27625390) (← links)
- NMR structures of three single-residue variants of the human prion protein (Q27625393) (← links)
- Two different neurodegenerative diseases caused by proteins with similar structures (Q27630179) (← links)
- NMR structure of the human doppel protein (Q27640537) (← links)
- NMR structure of the bank vole prion protein at 20 degrees C contains a structured loop of residues 165-171 (Q27652004) (← links)
- Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the beta2-alpha2 loop is modulated by long-range sequence effects (Q27655231) (← links)
- Unique quadruplex structure and interaction of an RNA aptamer against bovine prion protein (Q27656952) (← links)
- Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein (Q27661489) (← links)
- Unique Structural Characteristics of the Rabbit Prion Protein (Q27663561) (← links)
- Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein (Q27665069) (← links)
- The prion protein binds thiamine (Q27671805) (← links)
- Prion protein mPrP[F175A](121-231): structure and stability in solution (Q27682040) (← links)
- Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel (Q28145970) (← links)
- Familial and sporadic fatal insomnia (Q28185765) (← links)
- Rapid folding of the prion protein captured by pressure-jump (Q28236967) (← links)
- Formation of amyloid fibrils from β-amylase (Q28586287) (← links)
- Generic amyloidogenicity of mammalian prion proteins from species susceptible and resistant to prions (Q28607285) (← links)
- Prion protein: evolution caught en route (Q28776299) (← links)
- Eight prion strains have PrP(Sc) molecules with different conformations (Q29617277) (← links)
- Mammalian prion proteins. (Q30326201) (← links)
- Protein structure elucidation from NMR proton densities. (Q30330309) (← links)
- Comparative analysis of the human and chicken prion protein copper binding regions at pH 6.5. (Q30350094) (← links)
- Protein structure elucidation from minimal NMR data: the CLOUDS approach. (Q30350477) (← links)
- Enhanced stability of human prion proteins with two disulfide bridges. (Q30354790) (← links)
- Use of proteinase K nonspecific digestion for selective and comprehensive identification of interpeptide cross-links: application to prion proteins (Q30414522) (← links)
- Mammalian prions: tolerance to sequence changes-how far? (Q30424667) (← links)
- The polybasic N-terminal region of the prion protein controls the physical properties of both the cellular and fibrillar forms of PrP. (Q30485085) (← links)
- Copper binding to the prion protein: structural implications of four identical cooperative binding sites (Q30558995) (← links)
- Determination of solution conformations of PrP106-126, a neurotoxic fragment of prion protein, by 1H NMR and restrained molecular dynamics. (Q30585001) (← links)
- Utilizing NMR and EPR spectroscopy to probe the role of copper in prion diseases. (Q30593594) (← links)
- Molecular dynamics simulation of human prion protein including both N-linked oligosaccharides and the GPI anchor. (Q30616807) (← links)
- Mapping the early steps in the pH-induced conformational conversion of the prion protein (Q30638581) (← links)
- Solid-state NMR studies of the secondary structure of a mutant prion protein fragment of 55 residues that induces neurodegeneration (Q30660780) (← links)
- Glycosylation differences between the normal and pathogenic prion protein isoforms (Q30810971) (← links)
- Biochemistry and structure of PrPC and PrPSc (Q30881419) (← links)
- NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126. (Q30885520) (← links)
- Characterization of 2'-fluoro-RNA aptamers that bind preferentially to disease-associated conformations of prion protein and inhibit conversion. (Q31151988) (← links)
- Prion protein fragments spanning helix 1 and both strands of beta sheet (residues 125-170) show evidence for predominantly helical propensity by CD and NMR. (Q31979097) (← links)
- Mapping the prion protein using recombinant antibodies (Q32003051) (← links)
- Observation of intermediate states of the human prion protein by high pressure NMR spectroscopy (Q33250429) (← links)
- Probing structural differences in prion protein isoforms by tyrosine nitration (Q33280623) (← links)
- Reversible monomer-oligomer transition in human prion protein (Q33401483) (← links)