Ser and Thr Residues Modulate the Conformation of Pro-Kinked Transmembrane α-Helices

By X. Deupí, M. Olivella, C. Govaerts, J. Ballesteros, M. Campillo, L. Pardo. 2004

84 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/300fb3b8524de60f47f98af87cb5a877d49706bf

How researchers see this paper

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In Molecular Biology

1. Gerd Krause
2. Catherine L. Worth
3. Annika Kreuchwig
4. Gunnar Kleinau
5. Johanna K. S. Tiemann
6. Peter Werner Hildebrand
7. Michele Ritschel
8. Franziska Kreuchwig

Citations in the corpus

• GPCR-SSFE 2.0—a fragment-based molecular modeling web tool for Class A G-protein coupled receptors (2017, background): “These features must correlate with a corresponding sequence pattern (fingerprint) such as proline distortions (22,23), serine/threonine residues modifying proline-induced -helical kinks by forming side chain hydrogen bonds with the helix backbone (24,25), glycine patterns, conserved motifs, lack of ”