Results 51 to 60 of about 7,902,914 (332)
Expanded Interactome of the Intrinsically Disordered Protein Dss1
Cell Reports, 2018 Summary: Dss1 (also known as Sem1) is a conserved, intrinsically disordered protein with a remarkably broad functional diversity. It is a proteasome subunit but also associates with the BRCA2, RPA, Csn12-Thp1, and TREX-2 complexes.
Signe M. Schenstrøm +7 more
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Genes, 2023 Intrinsically Disordered Proteins (IDPs) and Regions (IDRs) exist widely. Although without well-defined structures, they participate in many important biological processes.
Bingqing Han +4 more
semanticscholar +1 more source
Many-to-one binding by intrinsically disordered protein regions
Biocomputing 2020, 2019 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. DBR-protein complexes were collected from the Protein Data Bank for which two or more DBRs having different amino acid sequences bind to the same (100% sequence ...
Alterovitz, Wei-Lun +9 more
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Fuzzy regions in an intrinsically disordered protein impair protein–protein interactions [PDF]
The FEBS Journal, 2016 Despite the partial disorder‐to‐order transition that intrinsically disordered proteins often undergo upon binding to their partners, a considerable amount of residual disorder may be retained in the bound form, resulting in a fuzzy complex.
Gruet, Antoine +10 more
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Cryptic amyloidogenic regions in intrinsically disordered proteins
Computational and Structural Biotechnology Journal, 2021 The amyloid conformation is considered a fundamental state of proteins and the propensity to populate it a generic property of polypeptides. Multiple proteome-wide analyses addressed the presence of amyloidogenic regions in proteins, nurturing our understanding of their nature and biological implications.
Santos Suárez, Jaime|| +3 more
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Order, Disorder, and Everything in Between
Molecules, 2016 In addition to the “traditional” proteins characterized by the unique crystal-like structures needed for unique functions, it is increasingly recognized that many proteins or protein regions (collectively known as intrinsically disordered proteins (IDPs)
Shelly DeForte, Vladimir N. Uversky
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Multi-Level Analysis of Intrinsically Disordered Protein Docking Methods
Methods, 2022 Intrinsically Disordered Proteins (IDPs) are a class of proteins in which at least some region of the protein does not possess any stable structure in solution in the physiological condition but may adopt an ordered structure upon binding to a globular ...
Jacob Verburgt, Zi-Cong Zhang, D. Kihara
semanticscholar +1 more source
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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