ABSTRACT
Information about the impact of interactions between amyloid proteins on their fibrillization propensity is scattered among many experimental articles and presented in unstructured form. We manually curated information located in almost 200 publications (selected out of 562 initially considered), obtaining details of 883 experimentally studied interactions between 46 amyloid proteins or peptides. We also proposed a novel standardized terminology for the description of amyloid-amyloid interactions, which is included in our database, covering all currently known types of such a cross-talk, including inhibition of fibrillization, cross-seeding and other phenomena. The new approach allows for more specific studies on amyloids and their interactions, by providing very well-defined data. AmyloGraph, an online database presenting information on amyloid-amyloid interactions, is available at (http://AmyloGraph.com/). Its functionalities are also accessible as the R package (https://github.com/KotulskaLab/AmyloGraph). AmyloGraph is the only publicly available repository for experimentally determined amyloid-amyloid interactions.
Subject(s)
Amyloid , Amyloidogenic Proteins , Amyloidogenic Proteins/metabolism , Peptides , Databases, ProteinABSTRACT
In this paper, we have proposed a statistical procedure for detecting transitions of the mean-square-displacement exponent value within a single trajectory. With this procedure, we have identified three regimes of proteins dynamics on a cell membrane, namely, subdiffusion, free diffusion, and immobility. The fourth considered dynamics type, namely, superdiffusion was not detected. We show that the analyzed protein trajectories are not stationary and not ergodic. Moreover, classification of the dynamics type performed without prior detection of transitions may lead to the overestimation of the proportion of subdiffusive trajectories.
