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Dr. Kuen-Phon  Wu
Assistant Research Fellow
Room 112-1, Institute of Biological Chemistry, Academia Sinica
128, Academia Road Sec. 2, Nankang, Taipei 115, Taiwan
TEL: +886-2-27855696 ext. 1161
FAX: +886-2-27889759

Post-translational modifications (PTMs) are important biological process related to numerous cellular molecular events such as cell division, signaling and protein turnover. Ubiquitination is one of the post-translational modifications which employs a 76-residue small protein called ubiquitin to modify substrate proteins. Nearly half of human proteins are involved in the ubiquitination proteasome system and (mis-)regulated ubiquitinations are frequently correlated with human diseases. My research focuses on the molecular mechanism of HERC5 E3-mediated ubiquitination in innate immune responses. HERC5 utilizes a ubiquitin-like molecular called ISG15 to modify and promote degradation of viral or bacterial proteins as an important defending responses.

To fully unveil the HERC5-mediated innate immune response, structural biology provides great tools to discover details of protein-protein interactions. I will combine solution nuclear magnetic resonance (NMR) X-ray crystallography and cryo-electron micropscopy (cryoEM) to characterize dynamic and transient reactions, allosteric activation and complex structures. The outcome will provide chances in advanced drug design for antiviral response.

2004,09 - 2010,01 Ph.D., Chemistry and Chemical Biology, Rutgers, the State University of New Jersey, USA
2000,09 - 2002,06 M.S., Life Sciences, National Tsing Hua University, Taiwan
1996,09 - 2000,06 B.S., Life Sciences, National Tsing Hua University, Taiwan

2018,11 - present Assistant Research Fellow, Institute of Biological Chemistry, Academia Sinica, Taiwan
2018,01 - 2018,10 Visiting Assistant Professor, Institute of Biological Chemistry, Academia Sinica, Taiwan
2017,08 - 2018,10 Assistant research fellow, MOST
2012 - 2017 Postdoc, Department of Structural Biology, St Jude Children’s Research Hospital, USA
2010 - 2012 Postdoc, Center for Advanced Biotechnology and Medicine, Rutgers, the State University of New Jersey, USA

    Publications List
A cascading activity-based probe sequentially targets E1-E2-E3 ubiquitin enzymes.
Mulder MP, Witting K, Berlin I, Pruneda JN, Wu KP, Chang JG, Merkx R, Bialas J, Groettrup M, Vertegaal AC, Schulman BA, Komander D, Neefjes J, El Oualid F, Ovaa H Nature Chemical Biology (2016)
Dual RING E3 Architectures Regulate Multiubiquitination and Ubiquitin Chain Elongation by APC/C.
Brown NG, VanderLinden R, Watson ER, Weissmann F, Ordureau A, Wu KP, Zhang W, Yu S, Mercredi PY, Harrison JS, Davidson IF, Qiao R, Lu Y, Dube P, Brunner MR, Grace CRR, Miller DJ, Haselbach D, Jarvis MA, Yamaguchi M, Yanishevski D, Petzold G, Sidhu SS, Kuhlman B, Kirschner MW, Harper JW, Peters JM, Stark H, Schulman BA Cell (2016)
System-Wide Modulation of HECT E3 Ligases with Selective Ubiquitin Variant Probes.
Zhang W, Wu KP, Sartori MA, Kamadurai HB, Ordureau A, Jiang C, Mercredi PY, Murchie R, Hu J, Persaud A, Mukherjee M, Li N, Doye A, Walker JR, Sheng Y, Hao Z, Li Y, Brown KR, Lemichez E, Chen J, Tong Y, Harper JW, Moffat J, Rotin D, Schulman BA, Sidhu SS Molecular Cell (2016)
Unveiling transient protein-protein interactions that modulate inhibition of alpha-synuclein aggregation by beta-synuclein, a pre-synaptic protein that co-localizes with alpha-synuclein.
Janowska MK, Wu KP, Baum J Scientific Reports (2015)
Fast hydrogen exchange affects 15N relaxation measurements in intrinsically disordered proteins.
Kim S, Wu KP, Baum J Journal of Biomolecular NMR (2013)
Detection of transient interchain interactions in the intrinsically disordered protein alpha-synuclein by NMR paramagnetic relaxation enhancement.
Wu KP, Baum J Journal of American Chemistry Society (2010)
Structural reorganization of alpha-synuclein at low pH observed by NMR and REMD simulations.
Wu KP, Weinstock DS, Narayanan C, Levy RM, Baum J Journal of Molecular Biology (2009)

Updated 2018.08.01

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