D-Index & Metrics Best Publications
Chemistry
Switzerland
2023

D-Index & Metrics D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines.

Discipline name D-index D-index (Discipline H-index) only includes papers and citation values for an examined discipline in contrast to General H-index which accounts for publications across all disciplines. Citations Publications World Ranking National Ranking
Chemistry D-index 72 Citations 26,713 235 World Ranking 3057 National Ranking 82
Biology and Biochemistry D-index 76 Citations 31,041 267 World Ranking 3085 National Ranking 66

Research.com Recognitions

Awards & Achievements

2023 - Research.com Chemistry in Switzerland Leader Award

Overview

What is he best known for?

The fields of study he is best known for:

  • Quantum mechanics
  • Enzyme
  • Amino acid

Roland Riek mostly deals with Protein structure, Biochemistry, Amyloid, Fibril and Nuclear magnetic resonance spectroscopy. His biological study spans a wide range of topics, including Crystallography, Biophysics, Bovine spongiform encephalopathy, Prion protein and Cell biology. His Biochemistry research is multidisciplinary, incorporating elements of Fungal prion, Antiparallel, Fungal protein and Substantia nigra.

His research integrates issues of Protein aggregation, Cooperativity, Beta sheet, Peptide and Alzheimer's disease in his study of Amyloid. His Fibril research incorporates elements of Senile plaques, P3 peptide, Alpha-synuclein and Protein folding. His work in Nuclear magnetic resonance spectroscopy addresses subjects such as Protein secondary structure, which are connected to disciplines such as Scrapie.

His most cited work include:

  • Attenuated T2 relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution (1815 citations)
  • 3D structure of Alzheimer's amyloid-β(1–42) fibrils (1528 citations)
  • NMR structure of the mouse prion protein domain PrP(121–231) (1051 citations)

What are the main themes of his work throughout his whole career to date?

His scientific interests lie mostly in Biochemistry, Biophysics, Crystallography, Protein structure and Amyloid. In Biochemistry, he works on issues like Cell biology, which are connected to Programmed cell death. His Crystallography study integrates concerns from other disciplines, such as Lipid bilayer and Intermolecular force.

His Protein structure research incorporates themes from Nuclear magnetic resonance spectroscopy, Prion protein and Rhodanese. His research investigates the connection between Nuclear magnetic resonance spectroscopy and topics such as Spectroscopy that intersect with issues in Transverse relaxation-optimized spectroscopy. The study incorporates disciplines such as Fibril and Peptide in addition to Amyloid.

He most often published in these fields:

  • Biochemistry (32.99%)
  • Biophysics (26.74%)
  • Crystallography (18.06%)

What were the highlights of his more recent work (between 2016-2021)?

  • Biophysics (26.74%)
  • Amyloid (19.10%)
  • Fibril (16.67%)

In recent papers he was focusing on the following fields of study:

His main research concerns Biophysics, Amyloid, Fibril, Nuclear magnetic resonance spectroscopy and Alpha-synuclein. His study in Biophysics is interdisciplinary in nature, drawing from both Vesicle, Membrane, Membrane protein and Biological membrane. His study on Membrane is covered under Biochemistry.

His Amyloid research includes themes of Amino acid, Stereochemistry and Peptide. His work investigates the relationship between Fibril and topics such as Intermolecular force that intersect with problems in Resolution. His work carried out in the field of Nuclear magnetic resonance spectroscopy brings together such families of science as Protein structure, Gating, Crystallography and Protonation.

Between 2016 and 2021, his most popular works were:

  • Cryo-EM structure of alpha-synuclein fibrils. (187 citations)
  • Quantitative mass imaging of single biological macromolecules (137 citations)
  • Quantitative mass imaging of single biological macromolecules (137 citations)

In his most recent research, the most cited papers focused on:

  • Enzyme
  • Quantum mechanics
  • Amino acid

The scientist’s investigation covers issues in Biophysics, Amyloid, Fibril, Biochemistry and Crystallography. The Biophysics study combines topics in areas such as Helix, Membrane, Protein aggregation and Model lipid bilayer. His Fibril study combines topics from a wide range of disciplines, such as Pharmacophore, Structural biology, Alpha-synuclein and Cryo-electron microscopy.

His Biochemistry research is multidisciplinary, relying on both Amyloid fibril, Amyloid β, Solid-state nuclear magnetic resonance and Antiparallel. His studies in Crystallography integrate themes in fields like Nanodisc, Lipid bilayer, Lipid bilayer phase behavior, NMR spectra database and Nuclear magnetic resonance spectroscopy. His Nuclear magnetic resonance spectroscopy research integrates issues from Protein structure and Cooperativity.

This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.

Best Publications

Attenuated T2 relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Konstantin Pervushin;Roland Riek;Gerhard Wider;Kurt Wüthrich.
Proceedings of the National Academy of Sciences of the United States of America (1997)

3311 Citations

3D structure of Alzheimer's amyloid-β(1–42) fibrils

Thorsten Lührs;Christiane Ritter;Marc Adrian;Dominique Riek-Loher.
Proceedings of the National Academy of Sciences of the United States of America (2005)

2195 Citations

NMR structure of the mouse prion protein domain PrP(121–231)

Roland Riek;Simone Hornemann;Gerhard Wider;Martin Billeter.
Nature (1996)

1534 Citations

In vivo demonstration that alpha-synuclein oligomers are toxic.

Beate Winner;Roberto Jappelli;Samir K. Maji;Paula A. Desplats.
Proceedings of the National Academy of Sciences of the United States of America (2011)

1386 Citations

NMR Solution Structure of the Human Prion Protein

Ralph Zahn;Aizhuo Liu;Thorsten Lührs;Roland Riek.
Proceedings of the National Academy of Sciences of the United States of America (2000)

1340 Citations

NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231).

Roland Riek;Simone Hornemann;Gerhard Wider;Rudi Glockshuber.
FEBS Letters (1997)

1039 Citations

Amyloid fibrils of the HET-s(218–289) prion form a β-solenoid with a triangular hydrophobic core.

Christian Wasmer;Adam Lange;Hélène Van Melckebeke;Ansgar B. Siemer.
Science (2008)

1026 Citations

Functional Amyloids as Natural Storage of Peptide Hormones in Pituitary Secretory Granules

Samir K. Maji;Marilyn H. Perrin;Michael R. Sawaya;Sebastian Jessberger.
Science (2009)

971 Citations

Prion (PrPSc)-specific epitope defined by a monoclonal antibody.

Carsten Korth;Beat Stierli;Peter Streit;Markus Moser.
Nature (1997)

786 Citations

Identifying the amylome, proteins capable of forming amyloid-like fibrils

Lukasz Goldschmidt;Poh K. Teng;Roland Riek;David Eisenberg.
Proceedings of the National Academy of Sciences of the United States of America (2010)

759 Citations

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