Understanding eukaryotic linear motifs and their role in cell signaling and regulation.
By Francesca Diella, Niall J. Haslam, Claudia Chica, Aidan Budd, S. Michael, N. P. Brown, G. Travé, Toby J. Gibson. Frontiers in Bioscience, 2008
334 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/4976cf464aa0228d717626c86af866350e887e37
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Molecular Biology
- Alexandre M. J. J. Bonvin
- João P. G. L. M. Rodrigues
- Toby J. Gibson
- Adrien S. J. Melquiond
- Mikael E. Trellet
- Francesca Diella
- Cunliang Geng
- Aidan Budd
Citations in the corpus
- ELM—the database of eukaryotic linear motifs (2011, background): “SLiMs play an important role for many regulatory processes such as signal transduction, protein trafficking and post-translational modification (3,4).”
- Intrinsically disordered proteins: regulation and disease. (2011, background): “Therefore, they are likely to bind to each others’ physiological targets if their concentration is increased [7 ,15].”
- A Unified Conformational Selection and Induced Fit Approach to Protein-Peptide Docking (2013, positive): “The only change compared to bound/unbound (3 conformation) docking protocol is that the structure of the protein receptor in its unbound form was used, as downloaded from the Protein Data Bank.”
- ELM 2016—data update and new functionality of the eukaryotic linear motif resource (2015, background): “Relevance of linear motifs is well known in signaling pathways (32).”
- Motif switches: decision-making in cell regulation. (2012, background): “The majority of disordered interfaces characterised to date are associated with a subset of compact, degenerate and convergently evolvable interaction modules known as short linear motifs (SLiMs) [9].”
- Information-Driven, Ensemble Flexible Peptide Docking Using HADDOCK. (2017, background): “…an ensemble of starting conformations for the peptide (alpha-helix, polyproline-II, and extended) that represent “ideal” conformational states of a given peptide and have been shown to feature in a large fraction of the protein-peptide interactions deposited in the Protein Data Bank (PDB) [10].”
- The eukaryotic linear motif resource ELM: 10 years and counting (2013, background): “SLiMs are represented by a limited number of constrained affinity- and specificity-determining residues within peptides that are typically between 3 and 11 amino acids in length (5,7,8).”