title: Why and how protein aggregation has to be studied in vivo.
abstract: The understanding of protein aggregation is a central issue in different fields of protein science, from the heterologous protein production in biotechnology to amyloid aggregation in several neurodegenerative and systemic diseases. To this goal, it became more and more evident the crucial relevance of studying protein aggregation in the complex cellular environment, since it allows to take into account the cellular components affecting protein aggregation, such as chaperones, proteases, and molecular crowding. Here, we discuss the use of several biochemical and biophysical approaches that can be employed to monitor protein aggregation within intact cells, focusing in particular on bacteria that are widely employed as microbial cell factories.
authors: Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126, Milano, Italy. silviamaria.doglia@unimib.it
authors: Diletta
authors: D
authors: Ami
authors: Antonino
authors: A
authors: Natalello
authors: Marina
authors: M
authors: Lotti
authors: Silvia Maria
authors: SM
authors: Doglia
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000378:metabolism; D052160:Benzothiazoles; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D018832:Molecular Chaperones / Q000378:metabolism; D019636:Neurodegenerative Diseases / Q000378:metabolism / Q000473:pathology; D010447:Peptide Hydrolases / Q000378:metabolism; D011506:Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D017550:Spectroscopy, Fourier Transform Infrared; D013844:Thiazoles / Q000737:chemistry
chemical_list: D000682:Amyloid; D052160:Benzothiazoles; D018832:Molecular Chaperones; D011506:Proteins; D011993:Recombinant Fusion Proteins; D013844:Thiazoles; C009462:thioflavin T; D010447:Peptide Hydrolases