Profile-based short linear protein motif discovery [PDF]
Background Short linear protein motifs are attracting increasing attention as functionally independent sites, typically 3–10 amino acids in length that are enriched in disordered regions of proteins.
Haslam Niall J, Shields Denis C
doaj +6 more sources
iELM--a web server to explore short linear motif-mediated interactions. [PDF]
The recent expansion in our knowledge of protein-protein interactions (PPIs) has allowed the annotation and prediction of hundreds of thousands of interactions. However, the function of many of these interactions remains elusive. The interactions of Eukaryotic Linear Motif (iELM) web server provides a resource for predicting the function and positional
Weatheritt RJ +3 more
europepmc +8 more sources
A correlated motif approach for finding short linear motifs from protein interaction networks [PDF]
Background An important class of interaction switches for biological circuits and disease pathways are short binding motifs. However, the biological experiments to find these binding motifs are often laborious and expensive.
Hugo Willy +3 more
doaj +4 more sources
QSLiMFinder: improved short linear motif prediction using specific query protein data. [PDF]
Abstract Motivation: The sensitivity of de novo short linear motif (SLiM) prediction is limited by the number of patterns (the motif space) being assessed for enrichment. QSLiMFinder uses specific query protein information to restrict the motif space and thereby increase the sensitivity and specificity of predictions ...
Palopoli N, Lythgow KT, Edwards RJ.
europepmc +8 more sources
The eukaryotic linear motif resource - 2018 update. [PDF]
Short linear motifs (SLiMs) are protein binding modules that play major roles in almost all cellular processes. SLiMs are short, often highly degenerate, difficult to characterize and hard to detect.
Gouw, Marc +5 more
core +3 more sources
SLiMDisc: short, linear motif discovery, correcting for common evolutionary descent [PDF]
Many important interactions of proteins are facilitated by short, linear motifs (SLiMs) within a protein's primary sequence. Our aim was to establish robust methods for discovering putative functional motifs. The strongest evidence for such motifs is obtained when the same motifs occur in unrelated proteins, evolving by convergence.
Davey, Norman E. +2 more
openaire +5 more sources
SLiMSearch 2.0: biological context for short linear motifs in proteins [PDF]
Short, linear motifs (SLiMs) play a critical role in many biological processes. The SLiMSearch 2.0 (Short, Linear Motif Search) web server allows researchers to identify occurrences of a user-defined SLiM in a proteome, using conservation and protein disorder context statistics to rank occurrences.
Davey, Norman E. +3 more
openaire +6 more sources
HH-MOTiF: de novo detection of short linear motifs in proteins by Hidden Markov Model comparisons [PDF]
Short linear motifs (SLiMs) in proteins are self-sufficient functional sequences that specify interaction sites for other molecules and thus mediate a multitude of functions. Computational, as well as experimental biological research would significantly benefit, if SLiMs in proteins could be correctly predicted de novo with high sensitivity.
Roman Prytuliak +3 more
exaly +11 more sources
Resources to Discover and Use Short Linear Motifs in Viral Proteins [PDF]
Viral proteins evade host immune function by molecular mimicry, often achieved by short linear motifs (SLiMs) of three to ten consecutive amino acids (AAs). Motif mimicry tolerates mutations, evolves quickly to modify interactions with the host, and enables modular interactions with protein complexes.
Peter Hraber +6 more
openaire +4 more sources
Short Linear Sequence Motif LxxPTPh Targets Diverse Proteins to Growing Microtubule Ends [PDF]
Microtubule plus-end tracking proteins (+TIPs) are involved in virtually all microtubule-based processes. End-binding (EB) proteins are considered master regulators of +TIP interaction networks, since they autonomously track growing microtubule ends and recruit a plethora of proteins to this location.
Kumar, Anil +11 more
openaire +6 more sources

