Author pages are created from data sourced from our academic publisher partnerships and public sources.
- Publications
- Influence
Multiple Conformers in Active Site of Human Dihydrofolate Reductase F31R/Q35E Double Mutant Suggest Structural Basis for Methotrexate Resistance*
- Jordan P Volpato, B. Yachnin, +5 authors J. Pelletier
- Chemistry, Medicine
- The Journal of Biological Chemistry
- 28 May 2009
Methotrexate is a slow, tight-binding, competitive inhibitor of human dihydrofolate reductase (hDHFR), an enzyme that provides key metabolites for nucleotide biosynthesis. In an effort to better… Expand
2-Tier Bacterial and In Vitro Selection of Active and Methotrexate-Resistant Variants of Human Dihydrofolate Reductase
- E. Fossati, Jordan P Volpato, L. Poulin, Vanessa Guerrero, David-Antoine Dugas, J. Pelletier
- Biology, Medicine
- Journal of biomolecular screening
- 1 July 2008
We report a rapid and reliable 2-tier selection and screen for detection of activity as well as drug-resistance in mutated variants of a clinically-relevant drug-target enzyme. Human dihydrofolate… Expand
Novel crystallization conditions for tandem variant R67 DHFR yield a wild-type crystal structure.
- B. Yachnin, D. Colin, Jordan P Volpato, M. Ebert, J. Pelletier, A. Berghuis
- Biology, Medicine
- Acta crystallographica. Section F, Structural…
- 1 November 2011
Trimethoprim is an antibiotic that targets bacterial dihydrofolate reductase (DHFR). A plasmid-encoded DHFR known as R67 DHFR provides resistance to trimethoprim in bacteria. To better understand the… Expand
Combinatorial active‐site variants confer sustained clavulanate resistance in BlaC β‐lactamase from Mycobacterium tuberculosis
- Philippe Egesborg, Hélène Carlettini, Jordan P Volpato, N. Doucet
- Biology, Medicine
- Protein science : a publication of the Protein…
- 1 April 2015
Bacterial resistance to β‐lactam antibiotics is a global issue threatening the success of infectious disease treatments worldwide. Mycobacterium tuberculosis has been particularly resilient to… Expand
Selectively weakened binding of methotrexate by human dihydrofolate reductase allows rapid ex vivo selection of mammalian cells
- Jordan P Volpato, N. Mayotte, E. Fossati, Vanessa Guerrero, G. Sauvageau, J. Pelletier
- Biology, Medicine
- Journal of molecular recognition : JMR
- 1 March 2011
Ex vivo selection of transduced hematopoietic stem cells (HSC) with drug‐resistance genes offers the possibility to enrich transduced cells prior to engraftment, toward increased reconstitution in… Expand
Increasing methotrexate resistance by combination of active-site mutations in human dihydrofolate reductase.
- Jordan P Volpato, E. Fossati, J. Pelletier
- Biology, Medicine
- Journal of molecular biology
- 26 October 2007
Methotrexate-resistant forms of human dihydrofolate reductase have the potential to protect healthy cells from the toxicity of methotrexate (MTX), to improve prognosis during cancer therapy. It has… Expand
Mutational 'hot-spots' in mammalian, bacterial and protozoal dihydrofolate reductases associated with antifolate resistance: sequence and structural comparison.
- Jordan P Volpato, J. Pelletier
- Biology, Medicine
- Drug resistance updates : reviews and…
- 1 February 2009
Human dihydrofolate reductase (DHFR) is a primary target for antifolate drugs in cancer treatment, while DHFRs from Plasmodium falciparum, Plasmodium vivax and various bacterial species are primary… Expand
Asymmetric mutations in the tetrameric R67 dihydrofolate reductase reveal high tolerance to active‐site substitutions
- Maximilian C. C. J. C. Ebert, Krista L. Morley, Jordan P Volpato, A. Schmitzer, J. Pelletier
- Biology, Medicine
- Protein science : a publication of the Protein…
- 1 April 2015
Type II R67 dihydrofolate reductase (DHFR) is a bacterial plasmid‐encoded enzyme that is intrinsically resistant to the widely‐administered antibiotic trimethoprim. R67 DHFR is genetically and… Expand
Mutagénèse semi-aléatoire au site actif de la DHFR humaine : création et caractérisation de variantes hautement résistantes au MTX
- Jordan P Volpato
- Biology
- 4 June 2009
Human dihydrofolate reductase (hDHFR) is an enzyme that is essential to cell proliferation. It reduces dihydrofolate to tetrahydrofolate, an important cofactor involved in purine and thymidylate… Expand
Modifying Enzyme Specificity by COmbinatorial Active Site Mutations
Recent developments in molecular biology offer new approaches for improving our understanding of enzyme-ligand interactions. The complexity of enzyme catalysis, consisting of ligand recognition and… Expand