{'fraction_non_alphanumeric': 0.023305084745762712, 'fraction_numerical': 0.03177966101694915, 'mean_word_length': 5.472602739726027, '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}}
Membrane topology of peripheral myelin protein 22

Peripheral myelin protein 22 (PMP22) is a structural component of compact peripheral nerve myelin and is likely to play a role in the modulation of cell proliferation and cell spreading. Molecular genetics revealed that mutations affecting the PMP22 gene are responsible for the most common forms of hereditary motor and sensory neuropathies in humans. Computer analysis predicts a tetraspan‐membrane structure for the PMP22 protein. We have assessed the topology of PMP22 experimentally using chimeric proteins consisting of different PMP22 domains fused to reporter genes and internally tagged molecules. Based on in vitro transcription/translation assays and immunohistochemical analysis of transfected cells, we propose that PMP22 can adopt a non‐tetraspan topology that has functional implications in normal and disease processes. J. Neurosci. Res. 62:15–27, 2000. © 2000 Wiley‐Liss, Inc.