Results 11 to 20 of about 4,746 (287)
Ancient Evolutionary Origin of Intrinsically Disordered Cancer Risk Regions [PDF]
Cancer is a heterogeneous genetic disease that alters the proper functioning of proteins involved in key regulatory processes such as cell cycle, DNA repair, survival, or apoptosis.
Mátyás Pajkos +2 more
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Functions of Intrinsically Disordered Regions
Intrinsically disordered regions (IDRs), defined as protein segments lacking stable tertiary structures, are ubiquitously present in the human proteome and enriched with disease-associated mutations. IDRs harbor molecular recognition features (MoRFs) and
Linhu Xiao, Kun Xia
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Phosphorylation of Intrinsically Disordered Regions in Remorin Proteins [PDF]
Plant-specific remorin proteins reside in subdomains of plasma membranes, originally termed membrane rafts. They probably facilitate cellular signal transduction by direct interaction with signalling proteins such as receptor-like kinases (RLKs) and may ...
Macarena eMarín, Thomas eOtt
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Background Intrinsically unstructured or disordered proteins function via interacting with other molecules. Annotation of these binding sites is the first step for mapping functional impact of genetic variants in coding regions of human and other genomes,
Jia-Feng Yu +8 more
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Decoding intrinsically disordered regions in biomolecular condensates
Biomolecular condensates comprise a diverse array of molecular entities, with intrinsically disordered regions (IDRs) receiving mounting attention due to their pivotal roles. In recent years, significant progress has been made in understanding the linear
Minglei Shi +3 more
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Entropy and Information within Intrinsically Disordered Protein Regions [PDF]
Bioinformatics and biophysical studies of intrinsically disordered proteins and regions (IDRs) note the high entropy at individual sequence positions and in conformations sampled in solution.
Iva Pritišanac +3 more
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Analysis of Structured and Intrinsically Disordered Regions of Transmembrane Proteins [PDF]
Integral membrane proteins display two major types of transmembrane structure, helical bundles and beta barrels. The main functional roles of transmembraneproteins are the transport of small molecules and cell signaling, and sometimes these two roles are
Uversky, Vladimir N. +4 more
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Janus-like behavior of intrinsically disordered regions in reticulophagy [PDF]
Intrinsically disordered regions (IDRs) are crucial to homeostatic and organellar remodeling pathways. In reticulophagy/ER-phagy, long cytosolic IDR-containing receptors (e.g. RETREG1/FAM134B) house the LC3-interacting region (LIR) motif to recruit the phagophore.
Sergio Alejandro Poveda Cuevas +5 more
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Functional Segments on Intrinsically Disordered Regions in Disease-Related Proteins [PDF]
One of the unique characteristics of intrinsically disordered proteins (IPDs) is the existence of functional segments in intrinsically disordered regions (IDRs).
Hiroto Anbo +3 more
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Many-to-one binding by intrinsically disordered protein regions [PDF]
Disordered binding regions (DBRs), which are embedded within intrinsically disordered proteins or regions (IDPs or IDRs), enable IDPs or IDRs to mediate multiple protein-protein interactions.
Andrzej Kloczkowski +19 more
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