S. Rasmussen

Molecular Biology · Nature · 2001–2018

A researcher in the Science corpus: 13 papers; trusts 1 researcher and is trusted by 4 researchers here, as inferred from the citation graph.

Subfields

• Molecular Biology — 97 citations into it; #9,166 of 17,773 by trust here, #1,038 by citations
• Cellular and Molecular Neuroscience — 57 citations into it; #1,522 of 2,998 by trust here, #48 by citations

Whom S. Rasmussen trusts overall

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

1. A. McCoy
2. Vadim Cherezov
3. Brian K. Kobilka

Who trusts S. Rasmussen overall

1. Roderick E. Hubbard
2. William I. Weis
3. Brian K. Kobilka
4. A. Manglik
5. Yigong Shi
6. Vsevolod Katritch
7. Brian K. Shoichet
8. Vadim Cherezov
9. Raymond C. Stevens
10. D. Rosenbaum

Papers from S. Rasmussen's perspective

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

1. Crystal structure of opsin in its G-protein-interacting conformation (Nature)
2. Roles of G‐protein‐coupled receptor dimerization (EMBO Reports)
3. Conformational complexity of G-protein-coupled receptors. (TIPS - Trends in Pharmacological Sciences)
4. Regulation of GPCRs by endocytic membrane trafficking and its potential implications. (Annual Review of Pharmacology and Toxicology)
5. Crystallizing Membrane Proteins Using Lipidic Mesophases (Nature Protocols)
6. Allosteric modulators of GPCRs: a novel approach for the treatment of CNS disorders (Nature reviews. Drug discovery)
7. Crystal structure of metarhodopsin II (Nature)
8. Dark adaptation and the retinoid cycle of vision. (Progress in retinal and eye research)
9. Crystal structure of the ligand-free G-protein-coupled receptor opsin (Nature)
10. Refinement of macromolecular structures by the maximum-likelihood method.

Their papers

• Crystal structure of the human β2 adrenergic G-protein-coupled receptor (2007) — 1,633 citations
• High-Resolution Crystal Structure of an Engineered Human β2-Adrenergic G Protein–Coupled Receptor (2007) — 2,512 citations
• Activation of the β2-Adrenergic Receptor Involves Disruption of an Ionic Lock between the Cytoplasmic Ends of Transmembrane Segments 3 and 6* (2001) — 607 citations
• Yeast surface display platform for rapid discovery of conformationally selective nanobodies (2018) — 467 citations
• Crystal Structure of the β2Adrenergic Receptor-Gs protein complex (2011) — 2,924 citations
• GPCR Engineering Yields High-Resolution Structural Insights into β2-Adrenergic Receptor Function (2007) — 1,308 citations
• Structure and Function of an Irreversible Agonist-β2 Adrenoceptor complex (2011) — 766 citations
• Structure of a nanobody-stabilized active state of the β2 adrenoceptor (2011) — 1,689 citations
• A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein (2007) — 691 citations
• Conformational biosensors reveal adrenoceptor signalling from endosomes (2013) — 798 citations
• A general protocol for the generation of Nanobodies for structural biology (2014) — 750 citations
• The structure and function of G-protein-coupled receptors (2009) — 1,548 citations
• High-resolution crystal structure of an engineered human beta2-adrenergic G protein-coupled receptor. (2007) — 727 citations