Roland Riek

Molecular Biology · 2000–2020

A researcher in the Science corpus: 9 papers; trusts 2 researchers and is trusted by 0 researchers here, as inferred from the citation graph.

Subfields

• Molecular Biology — 61 citations into it
• Materials Chemistry — 11 citations into it
• Computational Biology & Bioinformatics — 5 citations into it

Whom Roland Riek trusts overall

Their strongest outbound trust, strongest first, inferred from their citations.

1. Brian Kuhlman

Papers from Roland Riek's perspective

Ordered by how strongly the researchers Roland Riek trusts endorse each paper. Same corpus, a different order for every researcher.

1. A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR. (Proceedings of the National Academy of Sciences of the United States of America)
2. Structural conversion of neurotoxic amyloid-β(1–42) oligomers to fibrils (Nature Structural &Molecular Biology)
3. Native protein sequences are close to optimal for their structures.
4. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins (Nature Biotechnology)
5. Amyloid Fibrils of the HET-s(218–289) Prion Form a β Solenoid with a Triangular Hydrophobic Core (Science)
6. Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host (Science)
7. Combined automated NOE assignment and structure calculation with CYANA
8. Aβ(1–42) Fibril Structure Illuminates Self-recognition and Replication of Amyloid in Alzheimer’s (Nature Structural &Molecular Biology)
9. 13C–1H dipolar-driven 13C–13C recoupling without 13C rf irradiation in nuclear magnetic resonance of rotating solids
10. The amyloid hypothesis of Alzheimer's disease at 25 years (EMBO Molecular Medicine)

Their papers

• Identifying the amylome, proteins capable of forming amyloid-like fibrils (2010) — 792 citations
• Amyloid Fibrils of the HET-s(218–289) Prion Form a β Solenoid with a Triangular Hydrophobic Core (2008) — 968 citations
• Functional Amyloids as Natural Storage of Peptide Hormones in Pituitary Secretory Granules (2009) — 934 citations
• NMR solution structure of the human prion protein. (2000) — 1,081 citations
• α-Synuclein aggregation nucleates through liquid–liquid phase separation (2020) — 666 citations
• Quantitative mass imaging of single molecules (2018) — 615 citations
• Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril (2016) — 742 citations
• In vivo demonstration that α-synuclein oligomers are toxic (2011) — 1,193 citations
• 3D structure of Alzheimer's amyloid-β(1–42) fibrils (2005) — 1,866 citations