Cadences of the collective: conspecific stimulation patterns interact with endogenous rhythms to cue socially mediated response shifts. [PDF]
Larter LC, Cushing CW, Ryan MJ.
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Nanopore-Based, Real-Time Single-Molecule Probing of i-Motif Structural Dynamics and Targeted PNA Disruption. [PDF]
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Circularization of 23S rRNA but not 16S rRNA within archaeal ribosomes. [PDF]
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Machine and Deep Learning Reveal Sequence Determinants Encoding Bivalent Histone Modifications. [PDF]
Zhao X +6 more
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Drosophila melanogaster miPEP8 Regulates Cell Size Through its Interaction With ref(2)P/p62. [PDF]
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Attributes of short linear motifs
Mol. BioSyst., 2012Traditionally, protein-protein interactions were thought to be mediated by large, structured domains. However, it has become clear that the interactome comprises a wide range of binding interfaces with varying degrees of flexibility, ranging from rigid globular domains to disordered regions that natively lack structure.
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How to Annotate and Submit a Short Linear Motif to the Eukaryotic Linear Motif Resource
2020Over the past few years, it has become apparent that approximately 35% of the human proteome consists of intrinsically disordered regions. Many of these disordered regions are rich in short linear motifs (SLiMs) which mediate protein-protein interactions. Although these motifs are short and often partially conserved, they are involved in many important
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How viral proteins bind short linear motifs and intrinsically disordered domains
Essays in Biochemistry, 2022Abstract Viruses are the obligate intracellular parasites that exploit the host cellular machinery to replicate their genome. During the viral life cycle viruses manipulate the host cell through interactions with host proteins. Many of these protein–protein interactions are mediated through the recognition of host globular domains by ...
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Screening Intrinsically Disordered Regions for Short Linear Binding Motifs
2020The intrinsically disordered regions of the proteome are enriched in short linear motifs (SLiMs) that serve as binding sites for peptide binding proteins. These interactions are often of low-to-mid micromolar affinities and are challenging to screen for experimentally.
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