Results 11 to 20 of about 2,744,502 (279)
Phosphorylation of Intrinsically Disordered Regions in Remorin Proteins [PDF]
Frontiers in Plant Science, 2012 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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Proteome-wide signatures of function in highly diverged intrinsically disordered regions
eLife, 2019 Intrinsically disordered regions make up a large part of the proteome, but the sequence-to-function relationship in these regions is poorly understood, in part because the primary amino acid sequences of these regions are poorly conserved in alignments ...
Taraneh Zarin +5 more
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DisBind: A database of classified functional binding sites in disordered and structured regions of intrinsically disordered proteins [PDF]
BMC Bioinformatics, 2017 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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Entropy and Information within Intrinsically Disordered Protein Regions [PDF]
Entropy, 2019 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]
Molecular BioSystems, 2009 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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Biomolecular Concepts, 2019 We define the disordered boundary of the cell (DBC) as the system formed by membrane tethered intrinsically disordered protein regions, dynamically coupled to the underlying membrane.
Mohammad Irrem-Laareb +2 more
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Structural and functional studies of intrinsically disordered fibronectin-binding proteins [PDF]
, 2009 Bacterial fibronectin-binding proteins (FnBPs) mediate adhesion of bacteria to host tissues through binding to the human protein fibronectin (Fn). FnBPs are predicted to contain a series of intrinsically disordered Fn-binding repeats (FnBRs), which ...
Norris, Nicole Catherine
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Intrinsically disordered regions in the rodent hepevirus proteome [PDF]
Bioinformation, 2022 Hepatitis E virus (HEV) is the causative agent of Hepatitis E infections across the world. Intrinsically disordered protein regions (IDPRs) or intrinsically disordered proteins (IDPs) are regions or proteins that are characterized by lack of definite structure.
Shafat, Zoya +4 more
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Intrinsically disordered regions in autophagy proteins [PDF]
Proteins: Structure, Function, and Bioinformatics, 2013 ABSTRACTAutophagy is an essential eukaryotic pathway required for cellular homeostasis. Numerous key autophagy effectors and regulators have been identified, but the mechanism by which they carry out their function in autophagy is not fully understood.
Yang, Mei +5 more
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Multifunctional Intrinsically Disordered Regions in Transcription Factors
Chemistry – A European Journal, 2023 Abstract Eukaryotic transcription factors (TFs) are the final integrators of a complex molecular feedback mechanism that interfaces with the genome, consolidating information for transcriptional regulation. TFs consist of both structured DNA‐binding domains and long intrinsically disordered regions (IDRs) embedded with motifs linked ...
Matti Már +2 more
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