The Graduate Program in Biochemistry and Molecular Biology involves seven departments in Robert Wood Johnson Medical School (RWJMS) and Rutgers University (RU). Graduate Training is currently supported by five training awards from the NIH. Continued support for these 5 traineeships is requested. RWJMS and RU represent the primary facilities for research and graduate (and undergraduate) training in the State of New Jersey. The Busch Campus in Piscataway is home to RWJMS and RU, as well as the Center for Advanced Biotechnology and Medicine (CABM), The Waksman Institute, Rutgers School of Pharmacy, The School of Public Health, and the Environmental and Occupational Health Sciences Institute (EOHSI). This concentration of research capital has fostered strong links between the various institutes, and among the faculty. The Joint Program in Molecular Biosciences (MolBioSci) took advantage of this resource to form a collective program to recruit graduate students, with the specific objective of enhancing their training potential. The Program in Biochemistry and Molecular Biology is administered by the Department of Biochemistry (RWJMS). The quality of incoming graduate students is excellent, as is the retention and graduation rate. A significant pool of candidates is available, since approximately 50% of the incoming class represents American citizens, and 25% are underrepresented minority students. Trainees are supported for two years during their third and fourth years of training. The number of participating faculty is currently 33, with 23 members from RWJMS and 10 from RU. The campus retains notable strengths in structural biology, enzymology of DNA replication, biochemistry of transcription and DMA repair, and regulation of development. Various model systems are explored, including rodent, fly, nematode, frog, plant, yeast and bacterial systems. Graduate training in the Program is accompanied by significant oversight, as formal mechanisms are in place to closely monitor the progress of the student, to remediate deficiencies, and insure completion of the dissertation. Similarly, the Program is itself subject to evaluation, to provide the strongest environment for graduate education and training.

National Institute of Health (NIH)
National Institute of General Medical Sciences (NIGMS)
Institutional National Research Service Award (T32)
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Special Emphasis Panel (ZGM1-BRT-5 (CG))
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Gindhart, Joseph G
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University of Medicine & Dentistry of NJ
Schools of Medicine
United States
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Schneider, William M; Brzezinski, Jonathon D; Aiyer, Sriram et al. (2013) Viral DNA tethering domains complement replication-defective mutations in the p12 protein of MuLV Gag. Proc Natl Acad Sci U S A 110:9487-92
Mazari, Peter M; Argaw, Takele; Valdivieso, Leonardo et al. (2012) Comparison of the convergent receptor utilization of a retargeted feline leukemia virus envelope with a naturally-occurring porcine endogenous retrovirus A. Virology 427:118-26
Schneider, William M; Wu, Dai-tze; Amin, Vaibhav et al. (2012) MuLV IN mutants responsive to HDAC inhibitors enhance transcription from unintegrated retroviral DNA. Virology 426:188-96
Leonard, Paul G; Bezar, Ian F; Sidote, David J et al. (2012) Identification of a hydrophobic cleft in the LytTR domain of AgrA as a locus for small molecule interactions that inhibit DNA binding. Biochemistry 51:10035-43
Cheng, Haiming; Rashid, Shayan; Yu, Zhuoxin et al. (2011) Location of glycine mutations within a bacterial collagen protein affects degree of disruption of triple-helix folding and conformation. J Biol Chem 286:2041-6
Schneider, William M; Tang, Yuefeng; Vaiphei, S Thangminlal et al. (2010) Efficient condensed-phase production of perdeuterated soluble and membrane proteins. J Struct Funct Genomics 11:143-154
Hwang, Eileen S; Thiagarajan, Geetha; Parmar, Avanish S et al. (2010) Interruptions in the collagen repeating tripeptide pattern can promote supramolecular association. Protein Sci 19:1053-64
Tang, Yuefeng; Schneider, William M; Shen, Yang et al. (2010) Fully automated high-quality NMR structure determination of small (2)H-enriched proteins. J Struct Funct Genomics 11:223-32
Schneider, William M; Inouye, Masayori; Montelione, Gaetano T et al. (2009) Independently inducible system of gene expression for condensed single protein production (cSPP) suitable for high efficiency isotope enrichment. J Struct Funct Genomics 10:219-25
Simmons, M J; Fan, G; Zong, W-X et al. (2008) Bfl-1/A1 functions, similar to Mcl-1, as a selective tBid and Bak antagonist. Oncogene 27:1421-8

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