{'fraction_non_alphanumeric': 0.05410821643286573, 'fraction_numerical': 0.03006012024048096, 'mean_word_length': 5.578947368421052, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Convergent synthesis of arisugacin skeletons and their acetylcholinesterase inhibitory activity.

In the course of our screening of microbial metabolites that inhibit the activity of acetylcholinesterase (AchE), we isolated potent and selective inhibitors of AchE, arisugacin A (1) and B (2) from the culture broth of Penicillium sp. FO-42591~4^ together with the structurally related known compound, territrem B (3) (Fig. 1)5'6). Interestingly, structures 1-3 resemble the pyripyropene A (4), which