Protein folding and misfolding

By Christopher M. Dobson. 2003

4,685 citations recorded by the source corpus.

Subfields: Cell Biology, Materials Chemistry, Molecular Biology

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

In Materials Chemistry

In Molecular Biology

Citations in the corpus

The s2D method: simultaneous sequence-based prediction of the statistical populations of ordered and disordered regions in proteins. (2015, background): “In the course of their lifetimes, most proteins populate partially or fully disordered states, which are often crucial in determining their functional or dysfunctional behaviors [7–13].”
Cellular strategies for controlling protein aggregation (2010, background): “As the energy barriers that separate native and non-native conformations are usually small, even native proteins are at permanent risk of unfolding, especially under environmental stress condition”
Experimental free-energy measurements of kinetic molecular states using fluctuation theorems (2012, methodology): “We applied equation (1) to extract free-energy differences of kinetic states from mechanical unfolding/folding experiments performed on DNA hairpins, which are model systems easy to design and synthesize.”
Mechanisms of diabetic complications. (2013, background): “Indeed, stoichiometry leads the way, where the chain of amino acids fluctuates through many conformations to identify a structure that is the most energetically efficient (153).”
Phase Transition of a Disordered Nuage Protein Generates Environmentally Responsive Membraneless Organelles (2015, background): “Ddx4 Organelle Formation Is Distinct from Amyloid Formation It is interesting to compare phase separation of Ddx4 proteins into organelles with the aggregation of proteins more generally into the amyloid fibrils that are associated with misfolding conditions, including Alzheimer’s and Parkinson’s di”
The amyloid state and its association with protein misfolding diseases (2014, background): “Paired betasheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy.”
Molecular Simulations of Cotranslational Protein Folding: Fragment Stabilities, Folding Cooperativity, and Trapping in the Ribosome (2006, neutral): “than folding in vitro for a number of reasons [1].”
Molecular Mechanism of Thioflavin-T Binding to Amyloid Fibrils (2010, background): “Amyloidfibrils are insoluble proteinaceousmaterials found in awide range of protein-misfolding diseases, including Alzheimer's and prion diseases as well as several types of systemic amyloidoses [1,2].”