Quyen Hoang, Ph.D.
Department of Biochemistry and Molecular Biology,
Stark Neurosciences Research Institute
Indiana University School of Medicine
635 Barnhill Drive, Room MS0013C
Indianapolis, Indiana 46202-5126
Phone: (317) 274-4371
Facsimile: (317) 274-4686
B.S., 1997, McMaster University, Ontario, Canada
Ph.D., 2003, McMaster University, Ontario, Canada
Post Doc., 2009, Brandeis University, Waltham, MA
Area of Study
Structural biology of neurodegenerative disease and structure-based drug design. More details...
Selected Recent Publications
Hoang QQ, Sicheri F, Howard AJ, Yang DSC. Bone recognition mechanism of porcine osteocalcin from crystal structure. Nature. 425: 977-980 (2003)
Das C*, Hoang QQ*, Kreinbring CA, Luchansky SJ, Meray RK, Ray SS, Lansbury PT, Ringe D, Petsko GA. Structural Basis for Conformational Plasticity of the Parkinson's Disease-Associated Ubiquitin Hydrolase UCH-L1. Proc Natl Acad Sci U S A. 103(12): 4675-80 (2006) (* Co-first author)
Pau VP, Zhu Y, Yuchi Z, Hoang QQ, Yang DS. Characterization of the C-terminal domain of a potassium channel from Streptomyces lividans (KcsA) J Biol Chem. 282(40): 29163-9 (2007)
Liu D, Thomas PW, Momb J, Hoang QQ, Petsko GA, Ringe D, Fast W. Structure and specificity of a quorum-quenching lactonase (AiiB) from Agrobacterium tumefaciens. Biochemistry. 46(42): 11789-99 (2007)
Ataie N, Hoang QQ, Dybig M, Milne A, Petsko GA and Ringe D. Zinc Coordination Geometry and Ligand Binding Affinity: The Structual and Kinetics Analysis of the Second-Shell Serine 228 Residue and the Methionine 180 Residue of the Aminopeptidase from Vibrio proteolyticus. Biochemistry. 47(29): 7673-83 (2008)
Landon MR, Lieberman RL, Hoang QQ, Ju S, Caaveiro JMM, Orwig SD, Kozakov D, Brenke R, Chuang GY, Beglov D, Vajda S, Petsko GA, Dagmar Ringe D. Detection of ligand binding hot spots on protein surfaces via fragment-based methods: Application to DJ-1 and Glucocerebrosidase. J. Comput Aided Mol Des. 23:491-500 (2009)
Wang W, Perovic I, Chittuluru J, Kagnanovich A, Nguyen LTT, Liao J, Auclair JR, Johnson D, Landeru A, Simorellis AK, Ju S, Cookson M, Asturias FJ, Agar JN, Webb BN, Kang CH, Ringe D, Gregory Petsko GA, Pochapsky TC, and Hoang QQ. A soluble alpha-Synuclein construct forms an ordered tetramer. Proc Natl Acad Sci U S A. 108(43): 17797-802 (2011)
Zhang Q, Xiao H, Chai SC, Hoang QQ, Lu H. Hydrophilic residues are crucial for RPL11 interaction with the zinc finger domain of mdm2 and P53 activation. J Biol Chem. 286(44): 38264-74 (2011)
Wu R, Edayathumangalam R, Wang Y, Garcia R, Wang W, Kreinbring S, Liao J, Stone T, Hoang QQ, Boris Belitsky, Gregory A Petsko, Ringe D, Dali Liu. Crystal structure of Bacillius subtilis GabR, an autorepressor and transcription activator of gabT. Proc Natl Acad Sci U S A. 110(44): 17820-5 (2013)
Liao J, Wu C, Burlak C, Zhang S, Sahm H, Wang M, Zhang ZY, Vogel KW, Federici M, Riddle SM, Nichols RJ, Liu D, Cookson MR, Stone TA, Hoang QQ. The Parkinson’s disease-associated mutation R1441H in LRRK2 prolongs the ‘active-state’ of its GTPase domain. Proc Natl Acad Sci U S A. 111(11): 4055-60 (2014)
Hoang QQ. Pathway for Parkinson’s disease. Proc Natl Acad Sci U S A. 111(17): 2402-3 (2014)
Tashiro A, Caaveiro JM, Wu CX, Hoang QQ, Tsumoto K. Thermodynamic and structural characterization of the specific binding of Zn(II) to Human DJ-1. Biochemistry. 53(14): 2218-20 (2014)
Oh M, Lee JH, Wang W, Lee HS, Lee WS, Burlak C, Im W, Hoang QQ*, and Hyun-Suk Lim*. Pharmacological Chaperones Targeting Cancer-Associated MCL-1 and Parkinson’s Disease-Associated α-Synuclein. Proc Natl Acad Sci U S A. 1111(30):11007-12 (2014) (* corresponding authors)
Burlak C, Hoang QQ. Xenotransplantation literature update, May-June 2014. Xenotransplantation. 21(4):392-5 (2014)
Recently, the World Health Organization (WHO) released a report entitled "Neurological Disorders, public health challenges" dedicated specially to the global burden of neurological disorders, highlighting the enormity of the problem and its burden on societies around the world. The report placed neurological disorders among the worse diseases and suggested that the need for a solution to alter the course of neurological disorders is of highest priority. There is a sense of urgency because of the rapid growth of the aging population, which is entering the ages of high-risk for neurological disorders. The biggest components of the age-dependent neurological disorders are neurodegenerative diseases. The top two neurodegenerative diseases are Alzheimer's disease and Parkinson's disease. Collectively they affect about 6.2 million people in the United States alone and costs the American society about $175 billion per year in direct and indirect costs associated with patient care [www.alz.org, www.parkinson.org]. These numbers are expected to triple by the year 2050 as the population is rapidly aging. Therefore, if effective treatments or preventive strategies for neurodegenerative diseases are not discovered in the near future, the costs and suffering caused by these diseases will be staggering.
Focus of our research
Parkinson's disease was characterized and treated more than 3000 years ago and James Parkinson formalized the disease nearly 200 years ago, yet the root causes of the disease remain elusive and there is currently no way to alter the course of disease progression. The Parkinson's disease research field had experienced an explosion of knowledge in the recent decade ignited by the discovery of genetic causative factors. Genetic studies in the past decade have identified 8 genes (α-synuclein, Parkin, UCH-L1, PINK1, DJ-1, LRRK2, Omi/HtrA2, and ATP13A2) implicated in the pathology of PD. Mutations in these genes are both causative and susceptibility factors for PD due to impairment of vesicular transport, proteosome function, mitochondria integrity and/or oxidative stress. Our research focuses on unraveling the molecular etiology of the disease and development of therapeutics. Our goals are to understand the biochemical functions of the disease associated proteins and the biological pathways in which they function. In parallel, are investigating ways to interfere the pathological function of these proteins with pharmacological agents as therapeutic strategies for people affected by Parkinson Disease.
Our research approaches
Unraveling these complex pathways will likely require the amalgamation of data from many different disciplines, and that is precisely the approach that we take in tackling these problems. We will go where the science takes us. The core of our research technique is structural biology (protein X-ray crystallography) and structure-based drug design. But we use techniques that range from atoms to human cellular models.