2004 B.S., Biological Sciences, California State University,
2006 M.S., Biological Sciences, California State University,
2006- Ph.D., Chemistry and Molecular Biology, University of
2011 California, Los Angeles, California
2011- Postdoc, Physical and Theoretical Chemistry,
2014 University of Oxford, Oxford, UK
Dr. Laganowsky’s most notable achievement as a graduate student was the determination of the X-ray structure of a toxic amyloid oligomer that exhibits properties of other amyloids, such as Alzheimer’s and Parkinson’s disease. His recent work led to the University of Oxford to learn cutting-edge native ion mobility mass spectrometry of soluble and membrane protein complexes in the laboratory of Professor Dame Carol V. Robinson. Ion mobility mass spectrometry is an established analytical technique and an emerging biophysical approach that is set to become an important component of the structural biology toolkit. Dr. Laganowsky has pioneered novel ion mobility mass spectrometry approaches to study membrane proteins and their interactions with lipid/drug molecules. His latest work was recently published in Nature with his artwork featured on the cover of the journal.
Dr. Laganowsky’s long standing ambition has been to start a research laboratory focused on training and mentoring scientists to solve biomedical problems. He would like to continue to work at the interface between ion mobility mass spectrometry and X-ray crystallography.
1. Laganowsky A, Reading E, Allison TM, Ulmschneider MB, Degiacomi MT, Baldwin AJ, Robinson CV. Membrane proteins bind lipids selectively to modulate their structure and function. Nature 2014, in press. (Cover Article).
2. Laganowsky A, Reading E, Hopper J, Robinson CV. Mass spectrometry of intact membrane protein complexes. Nature Protocols 2013, 8:639-51 (Cover Article).
3. Laganowsky A, Lui C, Sawaya MR, Whitelegge JP, Park J, Zhao M, Pensalfini A, Soriaga A, Landau M, Teng PK, Cascio D, Glabe C, Eisenberg D. Atomic view of a toxic amyloid small oligomer. Science 2012.
4. Colletier J-P§, Laganowsky A§, Landau M, Zhao ML, Soriaga AB, Goldschmidt L, Flot D, Cascio D, Sawaya MR, Eisenberg D. Molecular basis for amyloid-beta polymorphism. PNAS. 2011, 108(41): 16938-43. §Equal authorship.
5. Laganowsky A, Zhao M, Soriaga AB, Sawaya MR, Cascio D, Yeates TO. An approach to crystallizing proteins by metal-mediated synthetic symmetrization. Protein Science 2011, 20(11):1876-90. Ranked “must read” in Faculty of 1000.
6. Landau M, Sawaya MR, Faull KF, Laganowsky A, Jiang L, Sievers SA, Barrio JR, Eisenberg D. Towards a pharmacophore for amyloid. PLoS Biol 2011, 9(6): e1001080. doi:10.1371/journal.pbio.1001080.
7. Laganowsky A, Eisenberg D. Non-3D domain swapped crystal structure of truncated Zebrafish alphaA crystallin. Protein Science 2010, 19(10):1978-1984.
8. Laganowsky A, Benesch J LP, Landau M, Ding L, Sawaya M, Cascio D, Huang Q, Robinson CV, Horwitz J, Eisenberg D. Crystal structures of truncated AlphaA and AlphaB crystallin reveal structural mechanisms of polydispersity important for eye lens transparency. Protein Science 2010, 19(5):1031-43. (Cover Article).
9. Hochberg GK, Ecroyd H, Liu C, Cox D, Cascio D, Sawaya MR, Collier MP, Stroud J, Carver JA, Baldwin AJ, Robinson CV, Eisenberg DS, Benesch JL, Laganowsky A. The structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicity. PNAS. 2014, 111(16): E1562-70.