Results 271 to 280 of about 165,231 (306)

Recognition of Proline-Rich Motifs by Protein-Protein-Interaction Domains

Angewandte Chemie - International Edition, 2005
AbstractFor Abstract see ChemInform Abstract in Full Text.
Linda J Ball   +2 more
exaly   +3 more sources

Sequence Motifs in MADS Transcription Factors Responsible for Specificity and Diversification of Protein-Protein Interaction [PDF]

open access: yesPLoS Computational Biology, 2010
Protein sequences encompass tertiary structures and contain information about specific molecular interactions, which in turn determine biological functions of proteins.
Richard Immink   +2 more
exaly   +2 more sources

Yeast protein–protein interaction binding sites: prediction from the motif–motif, motif–domain and domain–domain levels

Molecular BioSystems, 2010
Abstract Interacting proteins can contact with each other at three different levels: by a domain binding to another domain, by a domain binding to a short protein motif, or by a motif binding to another motif. In our previous work, we proposed an approach to predict motif–motif binding sites for the yeast interactome by contrasting ...
Erli, Pang, Kui, Lin
openaire   +2 more sources

Discovering Interacting Domains and Motifs in Protein–Protein Interactions

2012
Many important biological processes, such as the signaling pathways, require protein-protein interactions (PPIs) that are designed for fast response to stimuli. These interactions are usually transient, easily formed, and disrupted, yet specific. Many of these transient interactions involve the binding of a protein domain to a short stretch (3-10) of ...
Hugo, W., Sung, W.-K., Ng, S.-K.
openaire   +2 more sources

D-SLIMMER: Domain–SLiM Interaction Motifs Miner for Sequence Based Protein–Protein Interaction Data

Journal of Proteome Research, 2011
Many biologically important protein-protein interactions (PPIs) have been found to be mediated by short linear motifs (SLiMs). These interactions are mediated by the binding of a protein domain, often with a nonlinear interaction interface, to a SLiM.
Hugo, W., Ng, S.-K., Sung, W.-K.
openaire   +2 more sources

A conserved motif in Argonaute-interacting proteins mediates functional interactions through the Argonaute PIWI domain

Nature Structural & Molecular Biology, 2007
Argonaute (Ago) proteins mediate silencing of nucleic acid targets by small RNAs. In fission yeast, Ago1, Tas3 and Chp1 assemble into a RITS complex, which silences transcription near centromeres. Here we describe a repetitive motif within Tas3, termed the 'Argonaute hook', that is conserved from yeast to humans and binds Ago proteins through their ...
Susanne, Till   +8 more
openaire   +2 more sources

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