The graduate program in Biochemistry and Molecular Biology described here was established in 1987 by the faculty from seven different departments within Robert Wood Johnson Medical School and Rutgers University. The first NIH training grant was awarded in 1991 to support 3 trainees per year. In this application, we request continued support for 4 trainees per year over the next 5 years. The training program was established at this most rapidly expanding life-science community at Piscataway Campus, where Robert Wood Johnson Medical School and Rutgers University, although independent, share not only physical hut also intellectual facilities forming a single life-science community. During the past five years, there were a number of notable developments which further enforce the present multidisciplinary training program consisting of 19 faculty from the medical school and 11 faculty from Rutgers University. These include two Howard Hughes professors (D. Reinberg and A. Stock) and the addition of four junior faculty (C. Abate, S. Brill, M. Driscoll and S. Peltz), a new research building of 60,000 square feet in the Center for Advanced Biotechnology and Medicine where 9 of the training faculty reside, the facility for structural molecular biology (E. Arnold, G. Montelione, and A. Stock) including 500 and 600 mHz NMR spectroscopes, and state-of-the- art X-ray diffraction equipment, as well as the establishment of the Division of Nucleic Acid Enzymology (D. Reinberg, T.W. Wong, and M. Hampsey). The annual research finding by these faculty is now more than $12.7 million. In this enriched life-science environment, students will perform research from mammalian genetics, signal transduction, regulation of DNA replication, transcription and translation, macromolecular interactions in living systems, protein structure and function, oncogenes, retroviruses, plant molecular biology, cell cycle and differentiation. Most significantly, a completely novel approach for recruiting trainees will be takIng place in 1996. All five graduate programs (2 from RWJMS and 3 from Rutgers) has been recently reorganized to form the consolidated Graduate Programs in Molecular Biosciences in order to jointly recruit and admit a first year class of outstanding graduate students and minority students. Now, more than 50% of our recruits are American. These students who choose the faculty of our graduate program after their second year as advisers will be members of this trainee program in which their performance will be monitored under the program.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Institutional National Research Service Award (T32)
Project #
5T32GM008360-08
Application #
2654834
Study Section
National Institute of General Medical Sciences Initial Review Group (BRT)
Project Start
1991-07-01
Project End
2001-06-30
Budget Start
1998-07-01
Budget End
1999-06-30
Support Year
8
Fiscal Year
1998
Total Cost
Indirect Cost
Name
University of Medicine & Dentistry of NJ
Department
Biochemistry
Type
Schools of Medicine
DUNS #
622146454
City
Piscataway
State
NJ
Country
United States
Zip Code
08854
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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