Systematic profiling and identification of the peptide‐mediated interactions between human Yes‐associated protein and its partners in esophageal cancer

• Published in: Journal of molecular recognition Vol. 35; no. 3; pp. e2947 - n/a
• Main Authors: Chen, Fei, Wang, Qifei, Mu, Yushu, Sun, Shibin, Yuan, Xulong, Shang, Pan, Ji, Bo
• Format: Journal Article
• Language: English
• Published: England Wiley Subscription Services, Inc 01.03.2022
• Subjects: Affinity; Amino Acid Motifs; Binding; Bonding strength; Cancer; Chemical compounds; Dishevelled protein; Esophageal cancer; Esophageal Neoplasms; Esophagus; Fluorescence; Fluorescence spectroscopy; Gastric cancer; Gene expression; Humans; Hydrogen bonding; Hydrogen bonds; peptide; Peptides; Peptides - chemistry; peptide‐mediated interaction; Pharmacology; Proline; proline‐rich motif; Protein Binding; Protein Structure, Tertiary; Proteins; Recognition; recognition site; Segments; Selectivity; Signal transduction; Transcription factors; Transcription Factors - metabolism; WW domain; YAP-Signaling Proteins - metabolism; Yes-associated protein; Yes-associated protein; proline-rich motif; selectivity; peptide; esophageal cancer; peptide-mediated interaction; WW domain; recognition site; affinity

Human Yes‐associated protein (YAP) is involved in the Hippo signaling pathway and serves as a coactivator to modulate gene expression, which contains a transactivation domain (TD) responsible for binding to the downstream TEA domain family (TEAD) of transcription factors and two WW1/2 domains that r...