Gender	Male
E-mail	rong.wang@mssm.edu
Education and Training	Ph.D., Johns Hopkins University School of Medicine

E-mail: rong.wang@mssm.edu
Tel: (212) 659-6759
Fax: (212) 828-5515

Mailing Address: 1425 Madison Avenue, Box 1498, New York, NY 10029

Education and Training	Ph.D., Johns Hopkins University School of Medicine

Biological mass spectrometry, proteomics, metabolomics and systems biology
Research in my laboratory is focused on biological mass spectrometry and mass spectrometry based proteomics and metabolomics.  We develop and utilize mass spectrometry technology to probe the protein interactions and protein processing mechanisms of the amyloid beta-protein in Alzheimer's disease. We are continuously developing new mass spectrometric methodologies in conjunction with protein purification technologies in order to increase protein detection sensitivity, enhance identification and characterization of protein post-translational modifications and perform quantification of particular protein sets (also known as proteome). This methodological development has been extensively applied to (1) the study of proteomics of hepatocellular carcinoma; (2) the study of proteomics of cellular vesicle trafficking; (3) the study of protein secretion, trafficking and degradation; (4) the plasma proteomics of Alzheimer's disease as well as (5) metabolomics.  It is our goal to continue to use biological mass spectrometry as an analytical tool to further our understanding of the molecular mechanisms of Alzheimer's disease, neuron degenerative diseases and cancer.

We are currently conducting researches in the following four general areas:

-Proteomics and metabolomics studies of neurodegenerative disease, cancer and other human diseases. Proteins and metabolites from different stages of disease are systematically analyzed using mass spectrometry to discover disease specific biomarkers as well as to understand disease pathological mechanisms.  Currently we are conducing plasma proteomics of Alzheimer's disease and tissue proteomics of hepatocellular carcinoma.  Based on the protein profile changes, we will modeling how metabolic pathways are altered in pathological conditions and further conducting metabolomics studies for comprehensively understand disease mechanisms.

-Proteomics study of intracellular vesicle trafficking.  Two cellular processes, endocytosis and exocytosis, are investigated by proteomics approaches.  The newly developed subcellular fractionation methodologies and mass spectrometry allow us to study these dynamic processes in great detail.  Currently, we are investigating the endocytosis pathways by applying magnetic nano-particles and stable isotope labeling techniques together with mass spectrometry.  

-Investigation of biological processes involving the synthesis, modification, and degradation of biological peptides and proteins using modern mass spectrometric methods. In recent years there has been a great amount of interest in investigating the biochemical events involved in the regulation of protein processing and metabolism as well as the disruption of these processes, for example, the processing of beta-amyloid precursor protein and metabolism of amyloid beta-peptide in Alzheimer's disease.

-Study of protein posttranslational modifications and their role in human diseases using mass spectrometry. We are focusing on developing more sensitive methods using mass spectrometry to identify the type, the number and the site of protein posttranslational modifications, for examples phosphorylation.

Wang R, Sweeney D , Gandy SE, Sisodia SS. The profile of soluble amyloid beta protein in cultured cell media. Detection and quantification of amyloid beta protein and variants by immunoprecipitation-mass spectrometry. J Biol Chem 1996 Dec; 271(50): 31894-31902.

Murphy MP, Uljon SN, Golde TE, Wang R. FAD-linked mutations in presenilin 1 alter the length of Abeta peptides derived from betaAPP transmembrane domain mutants. Biochim Biophys Acta 2002 Mar; 1586(2): 199-209.

Dias DC, Dolios G , Wang R, Pan ZQ. CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex. Proc Natl Acad Sci USA 2002 Dec; 99(26): 16601-16606.

Ikeuchi T, Dolios G , Kim SH, Wang R, Sisodia SS. Familial Alzheimer disease-linked presenilin 1 variants enhance production of both Abeta 1-40 and Abeta 1-42 peptides that are only partially sensitive to a potent aspartyl protease transition state inhibitor of 'gamma-secretase'. J Biol Chem 2003 Feb; 278(9): 7010-7018.

Wu K, Yamoah K , Dolios G , Gan-Erdene T , Tan P , Chen A , Lee CG, Wei N , Wilkinson KD, Wang R, Pan ZQ. DEN1 is a dual function protease capable of processing the C terminus of Nedd8 and deconjugating hyper-neddylated CUL1. J Biol Chem 2003 Aug; 278(31): 28882-28891.

Schoenfeld AR, Apgar S , Dolios G , Wang R, Aaronson SA. BRCA2 Is Ubiquitinated In Vivo and Interacts with USP11, a Deubiquitinating Enzyme That Exhibits Prosurvival Function in the Cellular Response to DNA Damage. Mol Cell Biol 2004 Sep; 24(17): 7444-7455.