Papers

3

Total Citations

31

H-Index

3

About

Timothy McPhillips is a structural biologist whose work has centered on elucidating the three-dimensional architecture of key enzymes from thermophilic organisms, particularly *Thermotoga maritima*. His research primarily focuses on the structural characterization of proteins involved in amino acid biosynthesis and carbohydrate metabolism. Among his most notable contributions is the determination of the crystal structure of γ-glutamyl phosphate reductase (TM0293), an enzyme catalyzing the second step of proline biosynthesis, solved at 2.0 Å resolution. This work provided critical insights into the NADPH-dependent reduction mechanism of L-γ-glutamyl phosphate. McPhillips also resolved the structure of uronate isomerase (TM0064) at 2.85 Å, advancing understanding of uronate catabolic pathways. Beyond individual structures, he contributed to the development of a system for the rapid and systematic characterization of protein crystals, part of a structural genomics initiative targeting *E. coli* proteins. While his citation counts (18 and 10 for his top papers) reflect a focused impact, his structural determinations have provided foundational knowledge for enzymology and metabolic pathway engineering. His work exemplifies the value of structural genomics in revealing the molecular machinery of life.

Research Focus

Key Achievements

3
H-Index
3
Papers
31
Total Citations
10
Avg Citations/Paper
🏆 Most Cited Paper
Crystal structure of γ‐glutamyl phosphate reductase (TM0293) from <i>Thermotoga maritima</i> at 2.0 Å resolution
18 citations · 2003
📈 Most Prolific Year: 2003 (2 Papers)
🤝 Key Collaborators: 50
🏛 Institutions: Joint Center for Structural Genomics, Stanford University, Biotechnology Research Institute

Top Papers

  1. 1
  2. 2
  3. 3

Key Collaborators

Contact & Links

Available for collaboration
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