Reference delineations of Area hOc5 (LOC) in individual sections of the BigBrain

This dataset contains cytoarchitectonic maps of area hOc5 (LOC) in the BigBrain. The mappings were created using multivariate statistical image analysis, applied to GLI-images of coronal histological sections of 1 micron resolution. Mappings are available on 21 sections of the occipital lobe of the BigBrain and have been transformed to the 3D reconstructed BigBrain space. For this brain area, a highly detailed 3D map has been computed based on automatic delineations on every histological section from a novel Deep Learning algorithm. This dataset can be accessed here: [Ultrahigh resolution 3D cytoarchitectonic map of Area hOc5 (LOC) created by a Deep-Learning assisted workflow](https://kg.ebrains.eu/search/live/minds/core/dataset/v1.0.0/ea8fb74b-0ecc-4801-9522-b4c2cb2a2a5c) This ultrahigh resolution 3D cytoarchitectonic map of Area hOc5 (LOC) can be explored in the HBP interactive Atlas Viewer

Kinetic binding analysis of aptamers targeting HIV-1 proteins by a combination of a microbalance array and mass spectrometry (MAMS)

An enhanced chip-based detection platform was developed by integrating a surface acoustic wave biosensor of the Love-wave type with protein identification by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-ToF MS). The system was applied to characterize the interaction of aptamers with their cognate HIV-1 proteins. The aptamers, which target two proteins of HIV-1, were identified using an automated in vitro selection platform. For aptamers S66A-C6 and S68B-C5, which target the V3 loop of the HIV-1 envelope protein gp120, KD values of 406 and 791 nM, respectively, were measured. Aptamer S69A-C15 was shown to bind HIV-1 reverse transcriptase (HIV-1 RT) with a KD value of 637 nM when immobilized on the biosensor surface. HIV-1 RT was identified with high significance using MALDI-ToF MS even in crude protein mixtures. The V3-loop of gp120 could be directly identified when using chip-bound purified protein samples. From crude protein mixtures, it could be identified indirectly with high significance via its fusion-partner glutathione-S-transferase (GST). Our data show that the combination of the selectivity of aptamers with a sensitive detection by MS enables the reliable and quantitative analysis of kinetic binding events of protein solutions in real time