Bernd Reif researcher
Reif, Bernd 1968-
VIAF ID: 27900446 (Personal)
Permalink: http://viaf.org/viaf/27900446
Preferred Forms
- 100 0 _ ‡a Bernd Reif ‡c researcher
- 100 1 _ ‡a Reif, Bernd ‡d 1968-
4xx's: Alternate Name Forms (2)
Works
Title | Sources |
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The Conformation ofcyclo(−d-Pro−Ala4−) as a Model for Cyclic Pentapeptides of thedL4Type | |
Cryogenic solid state NMR studies of fibrils of the Alzheimer's disease amyloid-β peptide: perspectives for DNP. | |
Determination of multiple torsion-angle constraints in U-(13)C,(15)N-labeled peptides: 3D (1)H-(15)N-(13)C-(1)H dipolar chemical shift NMR spectroscopy in rotating solids | |
Differentiation of HMBC two- and three-bond correlations: A method to simplify the structure determination of natural products | |
Direct measurement of angles between bond vectors in high-resolution NMR. | |
Dynamische Aspekte der molekularen Chaperone alphaA- und alphaB-Kristallin der menschlichen Augenlinse untersucht mittels NMR Spektroskopie | |
Entwicklung neuer NMR spektroskopischer Methoden zur Bestimmung von Konstitution und Konformation von Biomakromolekülen, Naturstoffen und metallorganischen Komplexen | |
Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains | |
Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice. | |
Experimental Determination of Microsecond Reorientation Correlation Times in Protein Solutions | |
Glycogen synthase kinase 3beta interaction protein functions as an A-kinase anchoring protein | |
Homophilic interactions of the amyloid precursor protein (APP) ectodomain are regulated by the loop region and affect beta-secretase cleavage of APP. | |
A Hot-Segment-Based Approach for the Design of Cross-Amyloid Interaction Surface Mimics as Inhibitors of Amyloid Self-Assembly. | |
Hydrogen bonding involving side chain exchangeable groups stabilizes amyloid quarternary structure. | |
Identification of Hydroxyl Protons, Determination of Their Exchange Dynamics, and Characterization of Hydrogen Bonding in a Microcrystallin Protein | |
Importance of low-oligomeric-weight species for prion propagation in the yeast prion system Sup35/Hsp104. | |
Improvements of MAS solid-state NMR experiments by Optimal Control | |
In support of the BMRB. | |
Internal protein dynamics on ps to μs timescales as studied by multi-frequency (15)N solid-state NMR relaxation | |
Large protein complexes with extreme rotational correlation times investigated in solution by magic-angle-spinning NMR spectroscopy | |
Local Structure and Relaxation in Solid-State NMR: Accurate Measurement of Amide N−H Bond Lengths and H−N−H Bond Angles | |
MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors | |
MAS solid-state NMR studies on the multidrug transporter EmrE. | |
Measurement of 2J(H,C)- and 3J(H,C)-coupling constants by alpha/beta selective HC(C)H-TOCSY. | |
Measurements of residual dipolar couplings in peptide inhibitors weakly aligned by transient binding to peptide amyloid fibrils | |
The mechanism of denaturation and the unfolded state of the α-helical membrane-associated protein Mistic. | |
Method development in solid-state NMR using CPMG-like pulse sequence | |
Methodenentwicklung in der Festkörper NMR mithilfe der CPMG-ähnlichen Pulssequenz | |
Methyl rotation barriers in proteins from 2H relaxation data. Implications for protein structure | |
Microsecond time scale mobility in a solid protein as studied by the 15N R(1rho) site-specific NMR relaxation rates | |
Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in the solid-state. | |
The neuronal S100B protein is a calcium-tuned suppressor of amyloid-β aggregation. | |
NH-NH vector correlation in peptides by solid-state NMR | |
NMR evidence for helix geometry modifications by a G-U wobble base pair in the acceptor arm of E. coli tRNAAla | |
NMR Spectroscopic Determination of Angles α and ζ in RNA from CH-Dipolar Coupling, P-CSA Cross-Correlated Relaxation | |
NMR spectroscopy of soluble protein complexes at one mega-dalton and beyond | |
Optimal (2)H rf Pulses and (2)H-(13)C Cross-Polarization Methods for Solid-State (2)H MAS NMR of Perdeuterated Proteins. | |
Optimal degree of protonation for ¹H detection of aliphatic sites in randomly deuterated proteins as a function of the MAS frequency | |
Periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter is sufficient to bind the maltose binding protein MalE. | |
Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble | |
Probing surface accessibility of proteins using paramagnetic relaxation in solid-state NMR spectroscopy | |
Protein side-chain dynamics observed by solution- and solid-state NMR: comparative analysis of methyl 2H relaxation data | |
Proton-detected solid-state NMR spectroscopy at aliphatic sites: application to crystalline systems | |
Radiofrequency fields in MAS solid state NMR probes. | |
The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes | |
A residue-specific shift in stability and amyloidogenicity of antibody variable domains | |
Resolution enhancement in MAS solid-state NMR by application of 13C homonuclear scalar decoupling during acquisition | |
Restoring Resolution in Biological Solid-State NMR under Conditions of Off-Magic-Angle Spinning | |
Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case | |
Site-specific analysis of heteronuclear Overhauser effects in microcrystalline proteins | |
Site-specific solid-state NMR studies of "trigger factor" in complex with the large ribosomal subunit 50S. | |
Slow motions in microcrystalline proteins as observed by MAS-dependent 15N rotating-frame NMR relaxation | |
Small molecule AKAP-protein kinase A (PKA) interaction disruptors that activate PKA interfere with compartmentalized cAMP signaling in cardiac myocytes | |
Small-molecule conversion of toxic oligomers to nontoxic β-sheet-rich amyloid fibrils | |
Small molecule induced toxic human-IAPP species characterized by NMR | |
Solid- and solution-state nuclear magnetic resonance spectroscopic studies on antibody light chain amyloid formation and interactions with epigallocatechin gallate | |
Solid state NMR assignments of a human λ-III immunoglobulin light chain amyloid fibril | |
Solid-state NMR of proteins sedimented by ultracentrifugation | |
Stabilization and structural analysis of a membrane-associated hIAPP aggregation intermediate | |
A Stable Mutant Predisposes Antibody Domains to Amyloid Formation through Specific Non-Native Interactions. | |
Structural and mechanistic implications of metal binding in the small heat-shock protein αB-crystallin | |
Structural Comparison of Oligoribonucleotides and Their 2′-Deoxy-2′-fluoro Analogs by heteronuclear NMR spectroscopy | |
Structural Insight into IAPP-Derived Amyloid Inhibitors and Their Mechanism of Action | |
Structural investigation of Serum Amyloid A fibrils using solid-state NMR and the effect of Heparin on SAA aggregation | |
Structural Mechanism of the Interaction of Alzheimer Disease Aβ Fibrils with the Non-steroidal Anti-inflammatory Drug (NSAID) Sulindac Sulfide | |
Structural properties of EGCG-induced, nontoxic Alzheimer's disease Aβ oligomers. | |
Structure and orientation of peptide inhibitors bound to beta-amyloid fibrils. | |
The structure and oxidation of the eye lens chaperone αA-crystallin | |
Structure calculation from unambiguous long-range amide and methyl 1H-1H distance restraints for a microcrystalline protein with MAS solid-state NMR spectroscopy | |
Strukturelle Untersuchung von Serum-Amyloid-A-Fibrillen mithilfe der Festkörper-NMR und die Auswirkungen von Heparin auf SAA-Aggregation | |
Substrate transport activation is mediated through second periplasmic loop of transmembrane protein MalF in maltose transport complex of Escherichia coli | |
Sulindac Sulfide Induces the Formation of Large Oligomeric Aggregates of the Alzheimer's Disease Amyloid-β Peptide Which Exhibit Reduced Neurotoxicity | |
Ultrahigh resolution in proton solid-state NMR spectroscopy at high levels of deuteration. | |
Yeast prion-protein, sup35, fibril formation proceeds by addition and substraction of oligomers. |