Intrinsically Disordered Proteins in Human Diseases: Introducing the D2Concept
Top Cited Papers
- 1 June 2008
- journal article
- review article
- Published by Annual Reviews in Annual Review of Biophysics
- Vol. 37 (1), 215-246
- https://doi.org/10.1146/annurev.biophys.37.032807.125924
Abstract
Intrinsically disordered proteins (IDPs) lack stable tertiary and/or secondary structures under physiological conditions in vitro. They are highly abundant in nature and their functional repertoire...Keywords
This publication has 157 references indexed in Scilit:
- Alternative splicing in cancer: Noise, functional, or systematic?The International Journal of Biochemistry & Cell Biology, 2007
- Disorder and Sequence Repeats in Hub Proteins and Their Implications for Network EvolutionJournal of Proteome Research, 2006
- Abundance of Intrinsic Disorder in Protein Associated with Cardiovascular DiseaseBiochemistry, 2006
- Coupled Folding and Binding with α-Helix-Forming Molecular Recognition ElementsBiochemistry, 2005
- Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signalingJournal of Molecular Recognition, 2005
- p53 Activation by Small Molecules: Application in OncologyJournal of Medicinal Chemistry, 2005
- Comparing and Combining Predictors of Mostly Disordered ProteinsBiochemistry, 2005
- Protein folding revisited. A polypeptide chain at the folding ? misfolding ? nonfolding cross-roads: which way to go?Cellular and Molecular Life Sciences, 2003
- Conformational properties of α-synuclein in its free and lipid-associated states 1 1Edited by P. E. WrightJournal of Molecular Biology, 2001
- NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively UnfoldedBiochemistry, 1996