title: Protein misfolding and aggregation research: some thoughts on improving quality and utility.
abstract: Once misfolded and aggregated proteins were as interesting as yesterday's trash, just a bothersome byproduct of productive activities. Today, they attract sustained interest from both basic researchers and practicing engineers. In the burgeoning biopharmaceutical industry, protein misfolding and aggregation pose significant challenges to the economic manufacture of safe and effective protein products. In the clinic, protein aggregates are believed to be pathological agents in a number of serious neurodegenerative disorders, such as Alzheimer's and Parkinson's. Over the past few years, the quantity of research into biotechnological aspects of protein misfolding and aggregation has skyrocketed. However, the quality of the published work is quite variable. In this brief opinion piece, we describe what we believe are some key features of high-quality publications in protein aggregation. We focus on experimental studies that may also have a kinetic modeling component.
authors.affiliation: Dept. of Chemical and Biological Engineering, University of Wisconsin, Madison, WI.
authors.forename: Regina M
authors.initials: RM
authors.lastname: Murphy
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Roberts
mesh_terms: D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D008823:Micelles; D018625:Microscopy, Atomic Force; D046529:Microscopy, Electron, Transmission; D008970:Molecular Weight; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared
chemical_list: D008823:Micelles; D011506:Proteins
keywords: kinetic models of aggregation; protein aggregation; protein misfolding