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|Alternative name||Short Linear Motif Predictor|
|Interface||Web user interface|
|Restrictions to use||None|
Publication for Short Linear Motif Predictor
Intrinsic disorder within AKAP79 fine tunes anchored phosphatase activity toward substrates and drug sensitivity
[…] as the C-terminal portion of the anchoring protein is more ordered (). This is consistent with evidence showing that the C-terminal region encompasses the PKA-binding helix (blue; ; ). The ANCHOR and SLiMPred programs identify regions that are predicted to adopt static conformations upon association with protein binding partners (; ). These include known binding sites within AKAP79 for protein kin […]
Predicting MoRFs in protein sequences using HMM profiles
[…] ibed as disordered domains.Several predictors have been developed to identify SLiMs and MoRFs in disordered protein sequences [, ], namely, MoRFpred , ANCHOR [, ], MFSPSSMpred , γ-MoRF-PredII , SliMpred , SLiMDis  and SliMFinder . Considering all of the above predictors, the methods for identifying SLiMs and MoRFs are different even though SLiMs and MoRFs interact within IDRs. With the […]
Design and Evaluation of Antimalarial Peptides Derived from Prediction of Short Linear Motifs in Proteins Related to Erythrocyte Invasion
[…] sequences with a predicted TM domain because SLiMs have been shown to be enriched on the cytoplasmic side of TM proteins  and palmitoylated peptides can be targeted to membranes [, ]. We then used SLiMPred  to predict SLiM like regions in these sequences. We filtered the predictions keeping only those where at least five residues in a row had a predicted probability of being in a SLiM of 0.5 […]
Mutations in Gamma Adducin are Associated With Inherited Cerebral Palsy
[…] Short linear protein-binding motifs (SLiMs) were predicted using SLiMPred (http://bioware.ucd.ie/∼compass/biowareweb/). Protein intrinsic disorder was predicted with IUPred (http://iupred.enzim.hu/). Three-class protein secondary structure (helix, strand, and coil) […]
Evaluating Caveolin Interactions: Do Proteins Interact with the Caveolin Scaffolding Domain through a Widespread Aromatic Residue Rich Motif?
[…] kelihood to undergo order-disorder transitions , . It is therefore possible to computationally predict regions where motifs are likely to occur from a protein's primary sequence. We therefore applied SLiMPred, a recent de novo web-based programme designed to predict SLiMs from both ordered and disordered protein sequences independently of experimentally defined homologues and interactors , to see […]
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