Intrinsically disordered protein.

By A. Keith Dunker, J. David Lawson, C. Brown, Ryan M. Williams, Pedro Romero, J. Oh, Christopher J. Oldfield, Andrew Campen, Catherine M Ratliff, K. W. Hipps and 10 more. 2001

1,652 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

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Citations in the corpus

Exceptionally abundant exceptions: comprehensive characterization of intrinsic disorder in all domains of life (2014, background): “The concept of protein intrinsic disorder became an important part of modern structural biology and proteomic studies [1, 2, 22].”
Intrinsically disordered proteins and structured proteins with intrinsically disordered regions have different functional roles in the cell (2019, background): “In 88 this context, the lack of a well-defined 3D-structure represents a major functional advantage for 89 IDPs, allowing them to interact with a broad range of substrates with relatively high-specificity and 90 low-affinity, often undergoing a disorder-to-order transition upon binding [2,8,26,37,38”
Intrinsic Disorder Is a Common Feature of Hub Proteins from Four Eukaryotic Interactomes (2006, background): “Proline is a strong promoter of intrinsic disorder [26], and it is likely that this region is intrinsically disordered (as correctly predicted by PONDR VL-XT), but it undergoes a disorder-to-order transition upon binding to SH3 domain.”
p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure–Function Continuum Concept (2016, background): “The increased amount of disorder in eukaryotes may be related to the increase in their cellular signaling [4].”
EffectorP 3.0: prediction of apoplastic and cytoplasmic effectors in fungi and oomycetes (2021, background): “sequence; 10) frequency of polar amino acids (D, E, H, K, N, Q, R, S, T, Z) in the sequence; 11) average disorder propensity of amino acids in the sequence (Dunker et al., 2001); 12) average bulkiness of amino acids in the sequence (Zimmerman et al.”
Prediction of protein disorder based on IUPred (2018, background): “15 It was suggested that the longer disordered segments, such as those collected in the Disprot database, which were largely studied for their biological importance, represent a different flavor of disorder compared to shorter segments that dominate IDRs collected from the PDB. 3 However, these data”
AlphaFold predictions are valuable hypotheses and accelerate but do not replace experimental structure determination (2023, neutral): “The accuracy of a prediction is typically assessed by how closely it matches a structure in the Protein Data Bank 18 (PDB) with the same sequence, and there are many ways to make such a comparison 4 .”
The continuing conundrum of the LEA proteins (2007, background): “com) suggest that 27–41% of all eukaryotic proteins contain unstructured regions ≥50 residues long, and that 6–17% of polypeptides are wholly disordered (Dunker et al. 2001); therefore, many proteins are natively unfolded or have natively unfolded domains.”
Comprehensive comparative assessment of in-silico predictors of disordered regions. (2012, background): “, partially folded or molten/pre-molten globule-like, domains with poorly packed side chains [[2],[3]].”