Hao Wu (Chinese: 吴皓; pinyin: Wú Hào) is a Chinese American biochemist and structural biologist. She is the Asa and Patricia Springer Professor of Structural Biology in the Department of Biological Chemistry and Molecular Pharmacology at Harvard Medical School, and a Senior Investigator in the Program in Cellular and Molecular Medicine at Boston Children's Hospital. Her work focuses on molecular mechanisms of signal transduction in cell death and inflammation in innate immunity. She discovered large, higher-order protein assemblies involved in cell death and immune signaling - structures that, unlike traditional protein complexes, form filaments or circular oligomers and often lack fixed stoichiometry. These assemblies illuminate molecular mechanisms of proximity-driven enzyme activation, threshold behavior, signal amplification, noise reduction, and spatiotemporal regulation of signal transduction. They establish a new paradigm in signaling, and reveal mechanistic links to phase separation and biomolecular condensates. Together with Jon Kagan, she later dubbed these structures as supramolecular organizing centers (SMOCs). As of 2025, Wu has an h-index of 112 and her research has been cited over 50,000 times. She has received the Pew Scholar Award, the Rita Allen Scholar Award, the Margaret Dayhoff Memorial Award, the NYC Mayor's Award for Excellence in Science and Technology, NIH MERIT and Pioneer Awards, and the Purdue University Distinguished Science Alumni Award. She was elected AAAS fellow in 2013, to the National Academy of Sciences in 2015, and to the National Academy of Medicine in 2024.
Early life and education Wu's grandfather, Chengluo Wu (吴承洛), studied chemical engineering in the U.S. at Lehigh University (where he was known as Chenlott C. Wu). He founded and served as the president of the Chinese Chemical Society. Wu's parents were physics professors in Beijing, China, but were often targeted by the anti-intellectualism of the Chinese Cultural Revolution. As a high school junior, Wu was selected to the Chinese preparatory camp for the International Mathematical Olympiad, but declined in order to attend a summer program in biology. Wu was admitted from high school to Peking Union Medical College (PUMC) with the highest entering scores in 1982. She received a two and a half-year pre-medical education at Peking University, followed by clinical studies at PUMC. While at PUMC, she engaged in immunology research and developed a deep interest in basic science. In 1987, she attended a scientific lecture in Beijing by Professor Michael Rossmann, a pioneer in X-ray crystallography. Inspired, she chose not to complete her M.D. degree and instead moved to the U.S. in 1988 to pursue a Ph.D. in biochemistry at Purdue University under Rossmann's supervision. She graduated in 1992 with a thesis study on virus structures in which she developed and applied computational approaches to solve these structures. Wu conducted her postdoctoral training with Professor Wayne Hendrickson at Columbia University, where she solved the crystal structure of the four domain extracellular domain of human CD4 and engaged in software development for a crystallographic phasing method called multi-wavelength anomalous dispersion (MAD).
Career After her postdoctoral work, Wu began her independent academic career in 1997 as an assistant professor in the Department of Biochemistry at Weill Cornell Medical College. She was promoted to associate professor in 2001 and full professor in 2003. She took the risk of establishing a new research direction during her time at Cornell and gained recognition for her work on immune signaling complexes using X-ray crystallography. In 2012, Wu joined Harvard Medical School and Boston Children's Hospital. There, she was named the inaugural Asa and Patricia Springer Professor of Structural Biology, a chair named after the parents of Dr. Timothy Springer, in recognition of her scientific contributions.
Research Early on, Wu's lab focused on immune system signaling domains, including death domains, TNF receptor associated factor (TRAF) domains (also known as meprin and TRAF homology (MATH) domain), and RIP homotypic interaction motifs (RHIMs), as well as caspases and kinases, helped explain how immune receptors are activated. It was through these studies that she discovered a recurrent theme in immune signaling proteins: nonstoichiometric homo and hetero-oligomerization that mediates formation of supramolecular or higher-order molecular complexes, also known as signalosomes. Examples of these complexes include helical assembly of death domains such as in the Myddosome, multivalent interactions in TRAFs, and amyloid assembly of RHIMs. Her group has solved the structures of large protein complexes involved in immune pathways, including TRAFs, the Myddosome, IKK-beta, inflammasomes, gasdermins, and synaptic recombination-activating gene (RAG) complexes. Her work has advanced the concept that signal transduction is mediated by higher-order protein assemblies, which enable proximity-induced enzyme activation, signal amplification, and control of biological noise.
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