ELM server: a new resource for investigating short functional sites in modular eukaryotic proteins

By P. Puntervoll, Rune Linding, Christine Gemünd, Sophie Chabanis-Davidson, M. Mattingsdal, S. Cameron, David M. A. Martin, G. Ausiello, Barbara Brannetti, A. Costantini and 17 more. Nucleic Acids Res., 2003

636 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/0913a258b4744b6679072b9fb44a47cd76e62c86

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Citations in the corpus

The eukaryotic linear motif resource ELM: 10 years and counting (2013, methodology): “The ELM resource was established in 2003 with the mission to collect, annotate, classify and detect short linear motifs (18).”
GlobPlot: exploring protein sequences for globularity and disorder (2003, background): “org) (8), available for finding globular domains (e.”
Discovering Sequence Motifs with Arbitrary Insertions and Deletions (2008, methodology): “This is illustrated well by the ELM server, which uses protein motifs as a first step in predicting functional sites, and filters the predictions by criteria such as cell compartment and globular domain clash [15].”
Intrinsic disorder and functional proteomics. (2007, background): “The discovered function-associated motifs are often short sequences, which are called eukaryotic linear motifs (ELMs) by one research group (127), and these function-associated motifs resemble in many ways the functional regions found to reside within long ID regions.”
Understanding eukaryotic linear motifs and their role in cell signaling and regulation. (2008, background): “Upstream or downstream of the hydrophobic motif, negatively charged amino acids are common and may be required (see the ELM entry TRG_NES_CRM1_1).”
Improved Disorder Prediction by Combination of Orthogonal Approaches (2009, background): “It has been estimated that ,85% of the linear motifs from Eukaryotic Linear Motif (ELM) database are located within disordered regions [34,35].”
Systematic discovery of in vivo phosphorylation networks. (2007, methodology): “…the development of computational methods to predict the substrate speciﬁcities of protein kinases, based on experimental identiﬁcation of the consensus sequence motifs recognized by the active site of kinase catalytic domains (Hjerrild et al., 2004; Obenauer et al., 2003; Puntervoll et al., 2003).”
DisProt: the Database of Disordered Proteins (2006, methodology): “Another approach, based on sequence comparison rather than analysis of structures in PDB, has been used to systematically identify short, linear motifs that bind to protein partners (20,21,36).”
ELM—the database of eukaryotic linear motifs (2011, methodology): “It was established as the first manually annotated collection of SLiM classes and as a tool for discovering linear motif instances in proteins (13).”
Assessing protein disorder and induced folding (2005, background): “ELMs are short linear peptide motifs essentially acting independently of protein tertiary structure and are used for various cellular functions, ranging from cell compartment targeting, posttranslational modifications, and protein–protein interactions.(237) The ELM server (http://elm.”
Protein disorder prediction: implications for structural proteomics. (2003, neutral): “(Cornilescu et al., 1999).”
Flexible nets: disorder and induced fit in the associations of p53 and 14-3-3 with their partners (2008, background): “Others developed a sequence-based approach to identify short, conserved recognition sites, called eukaryotic linear motifs (ELMs) [132,132-134].”