{'fraction_non_alphanumeric': 0.0374251497005988, 'fraction_numerical': 0.020958083832335328, 'mean_word_length': 6.271739130434782, '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}}
Increased interaction between heat shock protein 27 and mitogen‐activated protein kinase (p38 and extracellular signal‐regulated kinase) in pre‐eclamptic placentas

Aims:  Heat shock protein 27 (Hsp27) is a well‐known stress response protein that is characterized by its phosphorylative capacity. Hsp27 becomes phosphorylated in response to various stimuli through interaction with several different kinases. The purpose of this study was to evaluate the interaction between Hsp27 and mitogen‐activated protein kinase (MAPK) (p38, extracellular signal‐regulated kinase [ERK], and c‐Jun N‐terminal kinase) in the human placenta derived from patients with pre‐eclampsia.