King Tuo Yip
Ruhr University Bochum
8 Papers
19 Citations
King Tuo Yip is an academic researcher from Ruhr University Bochum. The author has contributed to research in topics: Melanoma inhibitory activity & RHEB. The author has an hindex of 3, co-authored 8 publications.
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Papers
Bisphenol A binds to Ras proteins and competes with guanine nucleotide exchange: implications for GTPase-selective antagonists.
Miriam Schöpel,Katharina F. G. Jockers,Peter M. Düppe,Jasmin Autzen,Veena Nambiar Potheraveedu,Semra Ince,King Tuo Yip,Rolf Heumann,Christian Herrmann,Jürgen Scherkenbeck,Raphael Stoll +10 more
TL;DR: The results propose a new mode of action for bisphenol A (10) that advocates a reduced exposure to this compound in the authors' environment and may lay the foundation for the future design of GTPase-selective antagonists with higher affinity to benefit of the treatment of cancer.
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Small Molecules Antagonise the MIA-Fibronectin Interaction in Malignant Melanoma
King Tuo Yip,Xue Yin Zhong,Nadia Seibel,Stefanie Pütz,Jasmin Autzen,Raphael Gasper,Eckhard Hofmann,Jürgen Scherkenbeck,Raphael Stoll +8 more
TL;DR: This work describes for the first time the discovery of small molecules that are able to disrupt the MIA-FN complex by selectively binding to a new druggable pocket, which could identify on MIA by structural analysis and fragment-based screening.
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A Blocking Group Scan Using a Spherical Organometallic Complex Identifies an Unprecedented Binding Mode with Potent Activity In Vitro and In Vivo for the Opioid Peptide Dermorphin
Martin Strack,Andrea Bedini,King Tuo Yip,Sara Lombardi,Daniel Siegmund,Raphael Stoll,Santi Spampinato,Nils Metzler-Nolte +7 more
TL;DR: In silico docking studies support receptor activation by both dermorphin binding modes and suggest a biological relevance for der Morphin itself, which is in line with previous protein mutation studies.
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Human melanoma inhibitory protein binds to the FN12-14 Hep II domain of fibronectin
TL;DR: The authors have identified the type III modules 12 to 14 of fibronectin's Hep II as the major MIA binding sites and provide a new target protein-protein binding interface for the discovery of novel antimetastatic agents against malignant melanoma in the future.
Molecular Basis of Class III Ligand Recognition by PDZ3 in Murine Protein Tyrosine Phosphatase PTPN13.
Gerd Kock,Markus Dicks,King Tuo Yip,Bastian Kohl,Stefanie Pütz,Rolf Heumann,Kai S. Erdmann,Raphael Stoll +7 more
TL;DR: In this article, the solution structures of the extended murine PTPN13 PDZ3 domain in its apo form and in complex with its physiological ligand, the carboxy-terminus of protein kinase C-related kinase-2 (PRK2), determined by multidimensional NMR spectroscopy were reported.
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