Results 41 to 50 of about 29,414 (258)
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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PhosIDP: a web tool to visualize the location of phosphorylation sites in disordered regions
Scientific Reports, 2021 Charge is a key determinant of intrinsically disordered protein (IDP) and intrinsically disordered region (IDR) properties. IDPs and IDRs are enriched in sites of phosphorylation, which alters charge.
Sonia T. Nicolaou +4 more
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FEBS Open Bio, 2022 Acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis (TTE0866) has an N‐terminal region (NTR; residues 23–135) between the signal sequence (residues 1–22) and the catalytic domain (residues 136–324), which is of unknown function ...
Kohei Sasamoto +6 more
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Frontiers in Plant Science, 2022 Intrinsically disorder regions or proteins (IDRs or IDPs) constitute a large subset of the eukaryotic proteome, which challenges the protein structure–function paradigm.
Nishu Gandass, Kajal, Prafull Salvi
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DARUMA: a gateway to fast and easy prediction of intrinsically disordered regions [PDF]
PeerJ Computer ScienceBackground Intrinsically disordered proteins (IDPs) are proteins that contain intrinsically disordered regions (IDRs), which lack stable three-dimensional structures under physiological conditions.
Itsuki Shimizu +4 more
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OPAL: prediction of MoRF regions in intrinsically disordered protein sequences [PDF]
Bioinformatics, 2018 AbstractMotivationIntrinsically disordered proteins lack stable 3-dimensional structure and play a crucial role in performing various biological functions. Key to their biological function are the molecular recognition features (MoRFs) located within long disordered regions. Computationally identifying these MoRFs from disordered protein sequences is a
Ronesh Sharma +4 more
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PLOS ONE, 2019 Abstract Many studies about classification and the functional annotation of intrinsically disordered proteins (IDPs) are based on either the occurrence of long disordered regions or the fraction of disordered residues in the sequence.
Deiana, Antonio +3 more
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Protein Expansion Is Primarily due to Indels in Intrinsically Disordered Regions [PDF]
Molecular Biology and Evolution, 2013 Proteins evolve not only through point mutations but also by insertion and deletion events, which affect the length of the protein. It is well known that such indel events most frequently occur in surface-exposed loops. However, detailed analysis of indel events in distantly related and fast-evolving proteins is hampered by the difficulty involved in ...
Light S +4 more
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The molecular basis for cellular function of intrinsically disordered protein regions
Nature Reviews Molecular Cell Biology, 2023 Intrinsically disordered protein regions exist in a collection of dynamic interconverting conformations that lack a stable 3D structure. These regions are structurally heterogeneous, ubiquitous and found across all kingdoms of life. Despite the absence of a defined 3D structure, disordered regions are essential for cellular processes ranging from ...
Alex S. Holehouse, Birthe B. Kragelund
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Intrinsic disorder and protein multibinding in domain, terminal, and linker regions [PDF]
Molecular BioSystems, 2010 Abstract Intrinsic disorder is believed to contribute to the ability of some proteins to interact with multiple partners which is important for protein functional promiscuity and regulation of the cross-talk between pathways.
Jessica H, Fong, Anna R, Panchenko
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