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Natively unfolded proteins: A point where biology waits for physics
  • V. Uversky
  • Chemistry, Medicine
  • Protein science : a publication of the Protein…
  • 1 April 2002
TLDR
Results of this analysis showed that intrinsically unstructured proteins do not possess uniform structural properties, as expected for members of a single thermodynamic entity, and the Protein Quartet model, with function arising from four specific conformations (ordered forms, molten globule, premolten globules, and random coils) is discussed. Expand
PONDR-FIT: a meta-predictor of intrinsically disordered amino acids.
TLDR
A consensus artificial neural network (ANN) prediction method, which was developed by combining the outputs of several individual disorder predictors and found to improve the prediction accuracy over a range of 3 to 20% with an average of 11% compared to the single predictors, depending on the datasets being used. Expand
Why are “natively unfolded” proteins unstructured under physiologic conditions?
TLDR
Analysis of amino acid sequences, based on the normalized net charge and mean hydrophobicity, has been applied to two sets of proteins and shows that “natively unfolded” proteins are specifically localized within a unique region of charge‐hydrophobia phase space. Expand
DisProt: the Database of Disordered Proteins
TLDR
The Database of Protein Disorder (DisProt) links structure and function information for intrinsically disordered proteins (IDPs) by collecting and organizing knowledge regarding the experimental characterization and the functional associations of IDPs. Expand
Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism.
TLDR
The results indicated that both nucleation and fibril growth were controlled by hydrophobic and electrostatic interactions. Expand
Evidence for a Partially Folded Intermediate in α-Synuclein Fibril Formation*
TLDR
A model for the fibrillation of α-synuclein is proposed in which the first step is the conformational transformation of the natively unfolded protein into the aggregation-competent partially folded intermediate. Expand
What does it mean to be natively unfolded?
  • V. Uversky
  • Chemistry, Medicine
  • European journal of biochemistry
  • 2002
TLDR
It appeared that natively unfolded proteins are characterized by low overall hydrophobicity and large net charge, and possess hydrodynamic properties typical of random coils in poor solvent, or premolten globule conformation. Expand
Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson's disease and heavy metal exposure.
TLDR
It is indicated that low concentrations of some metals can directly induce alpha-synuclein fibril formation and the potential for ligand bridging by polyvalent metal ions is proposed to be an important factor in the metal-induced conformational changes of alpha- synuclein. Expand
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
TLDR
There continues to be confusion regarding acceptable methods to measure autophagy, especially in multicellular eukaryotes, so it is important to update guidelines for monitoring autophagic activity in different organisms. Expand
Classification of Intrinsically Disordered Regions and Proteins
TLDR
Characterization of unannotated and uncharacterized protein segments is expected to lead to the discovery of novel functions as well as provide important insights into existing biological processes and is likely to shed new light on molecular mechanisms of diseases that are not yet fully understood. Expand
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