Continued support is requested for an ongoing program of graduate research training in molecular biology and biophysics at the University of Oregon. This training activity is centered in the Institute of Molecular Biology, and also involves additional research groups with related scientific interests. The Institute is a center for research and research instruction in areas where understanding of biological phenomena can be found in the properties of biological macromolecules. Current research includes studies of the molecular bases of genetic mechanisms in viruses, bacteria, yeast, and cells of higher organisms; control of gene expression, including initiation, elongation, and termination mechanisms in DNA replication, transcription, and translation; enzyme structure and function; interactions of proteins and nucleic acids; and certain aspects of developmental biology and differentiation. Over the last decade the research programs have expanded, in part as a consequence of a major grant from the Markey Trust. In addition, available research space has increased substantially as a consequence of a major building program. Due to careful planning, all molecular biology space is still closely contiguous and interactions between research groups and trainees in different laboratories remain strong. Faculty holds academic appointments in different departments (Biology, Chemistry, and Physics), but are housed in adjacent laboratories to maximize interactions and collaboration. Inter-disciplinary flexibility is promoted by the opportunity to do research under faculty members from any department. An increase in the current number of trainees is requested from 17 to 19.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Institutional National Research Service Award (T32)
Project #
5T32GM007759-23
Application #
6350998
Study Section
National Institute of General Medical Sciences Initial Review Group (BRT)
Program Officer
Cassatt, James
Project Start
1979-07-01
Project End
2004-06-30
Budget Start
2001-07-01
Budget End
2002-06-30
Support Year
23
Fiscal Year
2001
Total Cost
$514,607
Indirect Cost
Name
University of Oregon
Department
Biochemistry
Type
Organized Research Units
DUNS #
948117312
City
Eugene
State
OR
Country
United States
Zip Code
97403
Luan, Qing; Liu, Su-Ling; Helgeson, Luke A et al. (2018) Structure of the nucleation-promoting factor SPIN90 bound to the actin filament nucleator Arp2/3 complex. EMBO J 37:
Duvvuri, Hiranmayi; Wheeler, Lucas C; Harms, Michael J (2018) pytc: Open-Source Python Software for Global Analyses of Isothermal Titration Calorimetry Data. Biochemistry 57:2578-2583
Schlomann, Brandon H; Wiles, Travis J; Wall, Elena S et al. (2018) Bacterial Cohesion Predicts Spatial Distribution in the Larval Zebrafish Intestine. Biophys J 115:2271-2277
Piñas, Germán E; DeSantis, Michael D; Parkinson, John S (2018) Noncritical Signaling Role of a Kinase-Receptor Interaction Surface in the Escherichia coli Chemosensory Core Complex. J Mol Biol 430:1051-1064
Wiles, Travis J; Wall, Elena S; Schlomann, Brandon H et al. (2018) Modernized Tools for Streamlined Genetic Manipulation and Comparative Study of Wild and Diverse Proteobacterial Lineages. MBio 9:
Wheeler, Lucas C; Anderson, Jeremy A; Morrison, Anneliese J et al. (2018) Conservation of Specificity in Two Low-Specificity Proteins. Biochemistry 57:684-695
Balzer, Connor J; Wagner, Andrew R; Helgeson, Luke A et al. (2018) Dip1 Co-opts Features of Branching Nucleation to Create Linear Actin Filaments that Activate WASP-Bound Arp2/3 Complex. Curr Biol 28:3886-3891.e4
Fierro Jr, Javier; Haynes, Dylan R; Washbourne, Philip (2018) 4.1Ba is necessary for glutamatergic synapse formation in the sensorimotor circuit of developing zebrafish. PLoS One 13:e0205255
Schlomann, Brandon H (2018) Stationary moments, diffusion limits, and extinction times for logistic growth with random catastrophes. J Theor Biol 454:154-163
Miranda, Rafael G; McDermott, James J; Barkan, Alice (2018) RNA-binding specificity landscapes of designer pentatricopeptide repeat proteins elucidate principles of PPR-RNA interactions. Nucleic Acids Res 46:2613-2623

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