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Vladimir N. Uversky

Researcher at University of South Florida

Publications -  1099
Citations -  87547

Vladimir N. Uversky is an academic researcher from University of South Florida. The author has contributed to research in topics: Intrinsically disordered proteins & Protein structure. The author has an hindex of 131, co-authored 959 publications receiving 75342 citations. Previous affiliations of Vladimir N. Uversky include Indiana University – Purdue University Indianapolis & University of California, Santa Cruz.

Papers
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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
Journal ArticleDOI

Why are "natively unfolded" proteins unstructured under physiologic conditions?

Vladimir N. Uversky, +3 more
- 15 Nov 2000 - 
TL;DR: 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.
Journal ArticleDOI

Natively unfolded proteins: a point where biology waits for physics.

Vladimir N. Uversky
- 01 Apr 2002 - 
TL;DR: 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.
Book

Intrinsically Disordered Proteins

Vladimir N. Uversky, +2 more
TL;DR: The sequence-structure relationships indicate that disorder is an encoded property, and the predictions strongly suggest that proteins in nature are much richer in intrinsic disorder than are those in the Protein Data Bank.
Journal ArticleDOI

Classification of intrinsically disordered regions and proteins.

Robin van der Lee, +20 more
- 09 Jul 2014 - 
TL;DR: 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.