Results 51 to 60 of about 4,606,382 (149)
Connecting the αα-hubs: same fold, disordered ligands, new functions
Cell Communication and Signaling, 2021 Background Signal fidelity depends on protein–protein interaction–‘hubs’ integrating cues from large interactomes. Recently, and based on a common secondary structure motif, the αα-hubs were defined, which are small α-helical domains of large, modular ...
Lasse Staby +5 more
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Intrinsic Disorder of the C-Terminal Domain of Drosophila Methoprene-Tolerant Protein. [PDF]
PLoS ONE, 2016 Methoprene tolerant protein (Met) has recently been confirmed as the long-sought juvenile hormone (JH) receptor. This protein plays a significant role in the cross-talk of the 20-hydroxyecdysone (20E) and JH signalling pathways, which are important for ...
Marta Kolonko +6 more
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The N-terminal intrinsically disordered domain of mgm101p is localized to the mitochondrial nucleoid. [PDF]
, 2013 The mitochondrial genome maintenance gene, MGM101, is essential for yeasts that depend on mitochondrial DNA replication. Previously, in Saccharomyces cerevisiae, it has been found that the carboxy-terminal two-thirds of Mgm101p has a functional core ...
George Desmond Clark-Walker (281878) +12 more
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Modulation of the disordered conformational ensembles of the p53 transactivation domain by cancer-associated mutations. [PDF]
PLoS Computational Biology, 2015 Intrinsically disordered proteins (IDPs) are frequently associated with human diseases such as cancers, and about one-fourth of disease-associated missense mutations have been mapped into predicted disordered regions.
Debabani Ganguly, Jianhan Chen
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Advanced Sampling Methods for Multiscale Simulation of Disordered Proteins and Dynamic Interactions
Biomolecules, 2021 Intrinsically disordered proteins (IDPs) are highly prevalent and play important roles in biology and human diseases. It is now also recognized that many IDPs remain dynamic even in specific complexes and functional assemblies.
Xiping Gong, Yumeng Zhang, Jianhan Chen
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Expose flexible conformations for intrinsically disordered protein
Current Research in Structural BiologyThe folding conformation of native protein has flexibility in different degrees, which may bring difficulty in presenting the structures, and also it causes complexity in understanding the relationship between structure and functions.
Jiaan Yang +8 more
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Biomolecules, 2022 Intrinsically disordered proteins (IDPs) are ensembles of interconverting conformers whose conformational properties are governed by several physico-chemical factors, including their amino acid composition and the arrangement of oppositely charged ...
Greta Bianchi +6 more
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Globular and disordered – the non-identical twins in protein-protein interactions
Frontiers in Molecular Biosciences, 2015 In biology proteins from different structural classes interact across and within classes in ways that are optimized to achieve balanced functional outputs.
Kaare eTeilum +2 more
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Low-resolution description of the conformational space for intrinsically disordered proteins
Scientific Reports, 2022 Intrinsically disordered proteins (IDP) are at the center of numerous biological processes, and attract consequently extreme interest in structural biology.
Daniel Förster +5 more
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BMC Biology, 2023 Background Intrinsically disordered regions (IDRs) are widely distributed in proteins and related to many important biological functions. Accurately identifying IDRs is of great significance for protein structure and function analysis.
Yi-Jun Tang +4 more
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