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Author Details

Bernd Reif
Technische Universitat Munchen (TUM)
1996
145
49
Andrej Sali (CM4AI)
PMIDPaper TitleJournal TitlePublished Year
36682493Liquid-liquid phase separation of amyloid-β oligomers modulates amyloid fibrils formation.J Biol Chem2023
37904859Performance of the cross-polarization experiment in conditions of radiofrequency field inhomogeneity and slow to ultrafast magic angle spinning (MAS).Magn Reson (Gott)2023
37353525Mechanistic insights into the aggregation pathway of the patient-derived immunoglobulin light chain variable domain protein FOR005.Nat Commun2023
34870415Deuteration for High-Resolution Detection of Protons in Protein Magic Angle Spinning (MAS) Solid-State NMR.Chem Rev2022
35753394Structural insights into the interaction of antifungal peptides and ergosterol containing fungal membrane.Biochim Biophys Acta Biomembr2022
36074981Sensitivity-Enhanced Multidimensional Solid-State NMR Spectroscopy by Optimal-Control-Based Transverse Mixing Sequences.J Am Chem Soc2022
35924280SAA fibrils involved in AA amyloidosis are similar in bulk and by single particle reconstitution: A MAS solid-state NMR study.J Struct Biol X2022
36113917Field and magic angle spinning frequency dependence of proton resonances in rotating solids.Prog Nucl Magn Reson Spectrosc2022
34883118Conformational Tuning of Amylin by Charged Styrene-Maleic-Acid Copolymers.J Mol Biol2022
32946005Solid state NMR assignments of a human λ-III immunoglobulin light chain amyloid fibril.Biomol NMR Assign2021
34644121Maximizing efficiency of dipolar recoupling in solid-state NMR using optimal control sequences.Sci Adv2021
34795272Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.Nat Commun2021
34338090Protease resistance of <i>ex vivo</i> amyloid fibrils implies the proteolytic selection of disease-associated fibril morphologies.Amyloid2021
34368784Solid-state NMR spectroscopy.Nat Rev Methods Primers2021
31539802Cysteine oxidation triggers amyloid fibril formation of the tumor suppressor p16[INK4A].Redox Biol2020
31863711Structural Insight into IAPP-Derived Amyloid Inhibitors and Their Mechanism of Action.Angew Chem Int Ed Engl2020
33058870Domain Interactions Determine the Amyloidogenicity of Antibody Light Chain Mutants.J Mol Biol2020
33093170Seeded fibrils of the germline variant of human λ-III immunoglobulin light chain FOR005 have a similar core as patient fibrils with reduced stability.J Biol Chem2020
33006345Small molecule induced toxic human-IAPP species characterized by NMR.Chem Commun (Camb)2020
32291951Mapping the Binding Interface of PET Tracer Molecules and Alzheimer Disease Aβ Fibrils by Using MAS Solid-State NMR Spectroscopy.Chembiochem2020
30694593Accurate Determination of <sup>1</sup> H-<sup>15</sup> N Dipolar Couplings Using Inaccurate Settings of the Magic Angle in Solid-State NMR Spectroscopy.Angew Chem Int Ed Engl2019
31685894Accessing Methyl Groups in Proteins via <sup>1</sup>H-detected MAS Solid-state NMR Spectroscopy Employing Random Protonation.Sci Rep2019
31792453The structure and oxidation of the eye lens chaperone αA-crystallin.Nat Struct Mol Biol2019
31407204Determination of methyl order parameters using solid state NMR under off magic angle spinning.J Biomol NMR2019
31515660MAS dependent sensitivity of different isotopomers in selectively methyl protonated protein samples in solid state NMR.J Biomol NMR2019
30917192Probing transient non-native states in amyloid beta fiber elongation by NMR.Chem Commun (Camb)2019
29348618Epigallocatechin gallate (EGCG) reduces the intensity of pancreatic amyloid fibrils in human islet amyloid polypeptide (hIAPP) transgenic mice.Sci Rep2018
29989288Overcoming Volume Selectivity of Dipolar Recoupling in Biological Solid-State NMR Spectroscopy.Angew Chem Int Ed Engl2018
29963623The neuronal S100B protein is a calcium-tuned suppressor of amyloid-β aggregation.Sci Adv2018
30228183A single residue switch reveals principles of antibody domain integrity.J Biol Chem2018
30414962The Antibody Light-Chain Linker Regulates Domain Orientation and Amyloidogenicity.J Mol Biol2018
29745410hIAPP forms toxic oligomers in plasma.Chem Commun (Camb)2018
29605910Reconstitution of Isotopically Labeled Ribosomal Protein L29 in the 50S Large Ribosomal Subunit for Solution-State and Solid-State NMR.Methods Mol Biol2018
29453354Physical basis of amyloid fibril polymorphism.Nat Commun2018
28019720Solid- and solution-state nuclear magnetic resonance spectroscopic studies on antibody light chain amyloid formation and interactions with epigallocatechin gallate.Amyloid2017
28128355Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains.Sci Rep2017
28287098The redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes.Sci Rep2017
29148426Stabilization and structural analysis of a membrane-associated hIAPP aggregation intermediate.Elife2017
28946058Radiofrequency fields in MAS solid state NMR probes.J Magn Reson2017
28785098Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins.Sci Rep2017
28746363MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors.PLoS One2017
28841025Comparative Study of REDOR and CPPI Derived Order Parameters by <sup>1</sup>H-Detected MAS NMR and MD Simulations.J Phys Chem B2017
26900939Sulindac Sulfide Induces the Formation of Large Oligomeric Aggregates of the Alzheimer's Disease Amyloid-β Peptide Which Exhibit Reduced Neurotoxicity.Biochemistry2016
27017576Immobilization of soluble protein complexes in MAS solid-state NMR: Sedimentation versus viscosity.Solid State Nucl Magn Reson2016
26827727A Stable Mutant Predisposes Antibody Domains to Amyloid Formation through Specific Non-Native Interactions.J Mol Biol2016
25564702Access to Cα backbone dynamics of biological solids by 13C T1 relaxation and molecular dynamics simulation.J Am Chem Soc2015
26408269The Antibody Light-Chain Linker Is Important for Domain Stability and Amyloid Formation.J Mol Biol2015
26458046The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.Nat Struct Mol Biol2015
26641130Restoring Resolution in Biological Solid-State NMR under Conditions of Off-Magic-Angle Spinning.J Phys Chem Lett2015
26416887Structural Mechanism of the Interaction of Alzheimer Disease Aβ Fibrils with the Non-steroidal Anti-inflammatory Drug (NSAID) Sulindac Sulfide.J Biol Chem2015
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Collaborators

Hartmut Oschkinat
Leibniz-Forschungsinstitut fur Molekulare Pharmakologie
Co-authored papers 11
Martin Zacharias
Co-authored papers 5
Tobias Madl
Gottfried Schatz Research Center, Medical University of Graz
Co-authored papers 4
Oliver F Lange
Center for Integrated Protein Science, Technische Universitat Munchen
Co-authored papers 3
Martin Hrab?? de Angelis
German Center for Diabetes Research (DZD e.V.)
Co-authored papers 3
Lewis E Kay
University of Toronto
Co-authored papers 2
Michael Sattler
Technical University of Munich, Institute of Structural Biology
Co-authored papers 2
Udo Heinemann
Max-Delbruck-Center for Molecular Medicine in the Helmholtz Association (MDC)
Co-authored papers 2
Horst Kessler
Institute for Advanced Study, Technical University Munich
Co-authored papers 2
Andrej Sali (CM4AI)
University of California San Francisco
Co-authored papers 1
Josep Rizo
University of Texas Southwestern Medical Center
Co-authored papers 1
Mike P Williamson
The University of Sheffield
Co-authored papers 1
Lu-Yun Lian
Institute of Systems, The University of Liverpool
Co-authored papers 1
Juri Rappsilber
Institute for Biotechnology, Technical University Berlin
Co-authored papers 1
Igor L Barsukov
Institute of Integrative Biology, University of Liverpool
Co-authored papers 1
David E Shaw
Columbia University
Co-authored papers 1
Ad Bax
National Institutes of Health
Co-authored papers 1
Patrick C A van der Wel
Zernike Institute for Advanced Materials, University of Groningen
Co-authored papers 1
David Middleton
Co-authored papers 1
Ioannis Vakonakis
University of Oxford
Co-authored papers 1
Roland Beckmann
University of Munich
Co-authored papers 1
Thomas A Frenkiel
The Medical Research Council Biomedical NMR Centre, The Francis Crick Institute
Co-authored papers 1
Ernest D Laue
University of Cambridge
Co-authored papers 1
Gordon S Rule
Carnegie Mellon University
Co-authored papers 1
Stephen Matthews
Imperial College London
Co-authored papers 1
Chien Ho
Carnegie Mellon University
Co-authored papers 1
Toshimichi Fujiwara
Institute for Protein Research, Osaka University
Co-authored papers 1
Pei Tang
Sichuan University
Co-authored papers 1
Joern Werner
Co-authored papers 1
Paul C Driscoll
The Francis Crick Institute
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Release 1.2