Intrinsically unstructured proteins.

By Peter Tompa. TIBS -Trends in Biochemical Sciences. Regular ed, 2002

2,035 citations recorded by the source corpus.

Subfields: Cell Biology, Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/6501c069f49eb2dc2f46c63b3c4c266d9ceef355

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Citations in the corpus

Protein disorder prediction: implications for structural proteomics. (2003, methodology): “Russell1 (1)EMBL It is becoming increasingly clear that many functionally important protein segments occur outside of globuBiocomputing Unit Meyerhofstr 1 lar domains (Wright and Dyson, 1999; Dunker et al., 2002).”
Conformational constraints for amyloid fibrillation: the importance of being unfolded. (2004, neutral): “unstructured) proteins [7–15].”
The interplay between structure and function in intrinsically unstructured proteins (2005, background): “IUPs can be classified in terms of their functional modes into six broad categories, as put forward in [9,17].”
A decade and a half of protein intrinsic disorder: Biology still waits for physics (2013, background): “Functionally, IDPs/IDPRs were grouped in at least six broad classes based on the mode of action.(14,136) These broad classes included protein”
What’s in a name? Why these proteins are intrinsically disordered (2013, background): “In addition there is another class of functional proteins and protein regions that contain smaller or larger highly dynamic fragments, and some proteins are even characterized by a complete or almost complete lack of ordered structure under physiological conditions (at least in vitro) which appears ”
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].”
G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits (2016, background): “Prion-like, low complexity (LC), and intrinsically unstructured/intrinsically disordered (ID) protein regions mediate protein aggregation (Tompa, 2002), and the SG protein TIA-1 contains a prion-like domain that forms insoluble aggregates when expressed alone (Gilks et al., 2004).”
Improved Disorder Prediction by Combination of Orthogonal Approaches (2009, background): “Many techniques monitor properties such as distances between atoms, hydrodynamic features, and local or global changes in the environment of the atoms [4,5,6].”
Induced fit, conformational selection and independent dynamic segments: an extended view of binding events (2010, positive): “Importantly, a purely induced fit type binding mechanism is not characteristic even in these cases, because IDPs also have a broad fluctuating conformational ensemble, and conformational selection can take place [49-51].”
The pairwise energy content estimated from amino acid composition discriminates between folded and intrinsically unstructured proteins. (2005, background): “Estimated pairwise interaction energies of globular proteins and IUPs.”
Natively unfolded proteins. (2005, background): “It has been argued that, because disordered proteins are common to the majority, if not all, species, they should be recognized as a separate functional and structural category of protein structure [8].”
EGCG redirects amyloidogenic polypeptides into unstructured, off-pathway oligomers (2008, background): “On the basis of these results, we propose that EGCG should also influence the aggregation cascade of other natively unfolded polypeptides and proteins, such as islet amyloid polypeptide, tau or the prion protein [2, 49 ].”