Stephanie M. Truhlar, Ph.D. - Publications
Affiliations: | 2004 | University of California, San Francisco, San Francisco, CA |
Area:
Structure, function, and folding of proteins, chromosomes, and centrosomes| Year | Citation | Score | |||
|---|---|---|---|---|---|
| 2008 | Truhlar SM, Komives EA. LRR domain folding: just put a cap on it! Structure (London, England : 1993). 16: 655-7. PMID 18462667 DOI: 10.1016/J.Str.2008.04.002 | 0.456 | |||
| 2007 | Ferreiro DU, Cervantes CF, Truhlar SM, Cho SS, Wolynes PG, Komives EA. Stabilizing IkappaBalpha by "consensus" design. Journal of Molecular Biology. 365: 1201-16. PMID 17174335 DOI: 10.1016/J.Jmb.2006.11.044 | 0.384 | |||
| 2005 | Truhlar SM, Agard DA. The folding landscape of an alpha-lytic protease variant reveals the role of a conserved beta-hairpin in the development of kinetic stability. Proteins. 61: 105-14. PMID 16044461 DOI: 10.1002/Prot.20525 | 0.622 | |||
| 2005 | Jaswal SS, Truhlar SM, Dill KA, Agard DA. Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases. Journal of Molecular Biology. 347: 355-66. PMID 15740746 DOI: 10.1016/J.Jmb.2005.01.032 | 0.599 | |||
| 2004 | Truhlar SM, Cunningham EL, Agard DA. The folding landscape of Streptomyces griseus protease B reveals the energetic costs and benefits associated with evolving kinetic stability. Protein Science : a Publication of the Protein Society. 13: 381-90. PMID 14718653 DOI: 10.1110/Ps.03336804 | 0.546 | |||
| 2002 | Cunningham EL, Mau T, Truhlar SM, Agard DA. The pro region N-terminal domain provides specific interactions required for catalysis of alpha-lytic protease folding. Biochemistry. 41: 8860-7. PMID 12102628 DOI: 10.1021/Bi020214O | 0.534 | |||
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