2026 Roland Riek: Biology and Biochemistry Researcher – H-Index, Publications & Awards

D-Index & Metrics

Discipline name	D-Index	World Ranking	Current World Ranking	National Ranking	Current National Ranking	Publications	Citations
Chemistry	82	3029	2731	72	63	305	36585
Biology and Biochemistry	88	2643	2428	57	53	321	40275

Discipline name

D-Index

World Ranking

Current World Ranking

National Ranking

Current National Ranking

Publications

Citations

Chemistry

3029

2731

305

36585

Biology and Biochemistry

2643

2428

321

40275

Chemistry

D-Index

Citations

36585

World Ranking

3029

National Ranking

Biology and Biochemistry

D-Index

Citations

40275

World Ranking

2643

National Ranking

Research.com Recognitions

2023 - Research.com Biology and Biochemistry in Switzerland Leader Award

Overview

Roland Riek is affiliated with ETH Zurich in Switzerland and has a significant research profile in biochemistry, genetics, and molecular biology, with a strong emphasis on medicine. Their work spans several subfields including molecular biology, physiology, neurology, spectroscopy, and materials chemistry.

The scientist's research focuses on protein structure and dynamics, with particular attention to neurodegenerative diseases such as Alzheimer's and Parkinson's. Key topics covered in their publications include enzyme structure and function, advanced nuclear magnetic resonance (NMR) techniques, prion diseases and protein misfolding, as well as origins and evolution of life.

Roland Riek has published extensively in well-known scientific venues. Frequent publication outlets include:

bioRxiv (Cold Spring Harbor Laboratory)
Angewandte Chemie International Edition
Angewandte Chemie
Nature Communications
Journal of the American Chemical Society

Their collaboration network features several frequent co-authors, including:

Peter Güntert
Juan Gerez
Dhiman Ghosh
Harindranath Kadavath
Jason Greenwald

Recent notable papers authored or co-authored by Roland Riek include:

α-Synuclein aggregation nucleates through liquid-liquid phase separation (2020, Nature Chemistry)
Half a century of amyloids: past, present and future (2020, Chemical Society Reviews)
The expanding amyloid family: Structure, stability, function, and pathogenesis (2021, Cell)
Modulating α-Synuclein Liquid-Liquid Phase Separation (2021, Biochemistry)
Structural insights into α-synuclein monomer-fibril interactions (2021, Proceedings of the National Academy of Sciences)

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

3525
Citations
3D structure of Alzheimer's amyloid-β(1–42) fibrils

Thorsten Lührs;Christiane Ritter;Marc Adrian;Dominique Riek-Loher

2417
Citations
In vivo demonstration that alpha-synuclein oligomers are toxic.

Beate Winner;Roberto Jappelli;Samir K. Maji;Paula A. Desplats

1702
Citations
NMR structure of the mouse prion protein domain PrP(121–231)

Roland Riek;Simone Hornemann;Gerhard Wider;Martin Billeter

1632
Citations
NMR Solution Structure of the Human Prion Protein

Ralph Zahn;Aizhuo Liu;Thorsten Lührs;Roland Riek

1408
Citations
Functional Amyloids as Natural Storage of Peptide Hormones in Pituitary Secretory Granules

Samir K. Maji;Marilyn H. Perrin;Michael R. Sawaya;Sebastian Jessberger

1171
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

1091
Citations
NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231).

Roland Riek;Simone Hornemann;Gerhard Wider;Rudi Glockshuber

1068
Citations
Identifying the amylome, proteins capable of forming amyloid-like fibrils

Lukasz Goldschmidt;Poh K. Teng;Roland Riek;David Eisenberg

918
Citations
Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

Marielle Aulikki Wälti;Francesco Ravotti;Hiromi Arai;Charles G. Glabe

865
Citations
α-Synuclein aggregation nucleates through liquid-liquid phase separation.

Soumik Ray;Nitu Singh;Rakesh Kumar;Komal Patel

845
Citations
Prion (PrPSc)-specific epitope defined by a monoclonal antibody.

Carsten Korth;Beat Stierli;Peter Streit;Markus Moser

791
Citations
Quantitative mass imaging of single biological macromolecules

Gavin Young;Nikolas Hundt;Daniel Cole;Adam Fineberg

784
Citations
Biology of Amyloid: Structure, Function, and Regulation

Jason Greenwald;Roland Riek

761
Citations
The fold of alpha-synuclein fibrils

Marçal Vilar;Hui-Ting Chou;Thorsten Lührs;Samir K. Maji

745
Citations
Cryo-EM structure of alpha-synuclein fibrils.

Ricardo Cesar Guerrero-Ferreira;Nicholas M.I. Taylor;Daniel Mona;Philippe Ringler

604
Citations
Half a century of amyloids: past, present and future

Pu Chun Ke;Pu Chun Ke;Ruhong Zhou;Ruhong Zhou;Louise C. Serpell;Roland Riek

541
Citations
NMR structure of the bovine prion protein

Francisco López García;Ralph Zahn;Roland Riek;Kurt Wüthrich

538
Citations
Correlation of structural elements and infectivity of the HET-s prion.

Christiane Ritter;Marie-Lise Maddelein;Ansgar B. Siemer;Thorsten Lührs

528
Citations
The activities of amyloids from a structural perspective

Roland Riek;David S. Eisenberg;David S. Eisenberg

425
Citations
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

Unknown

32
Citations