Jordan P Volpato

Publications10
h-index6
Citations143
Highly Influential Citations5
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Multiple Conformers in Active Site of Human Dihydrofolate Reductase F31R/Q35E Double Mutant Suggest Structural Basis for Methotrexate Resistance*
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
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2-Tier Bacterial and In Vitro Selection of Active and Methotrexate-Resistant Variants of Human Dihydrofolate Reductase
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
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Novel crystallization conditions for tandem variant R67 DHFR yield a wild-type crystal structure.
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
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Combinatorial active‐site variants confer sustained clavulanate resistance in BlaC β‐lactamase from Mycobacterium tuberculosis
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
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Selectively weakened binding of methotrexate by human dihydrofolate reductase allows rapid ex vivo selection of mammalian cells
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
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Increasing methotrexate resistance by combination of active-site mutations in human dihydrofolate reductase.
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
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Mutational 'hot-spots' in mammalian, bacterial and protozoal dihydrofolate reductases associated with antifolate resistance: sequence and structural comparison.
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
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Asymmetric mutations in the tetrameric R67 dihydrofolate reductase reveal high tolerance to active‐site substitutions
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
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Mutagénèse semi-aléatoire au site actif de la DHFR humaine : création et caractérisation de variantes hautement résistantes au MTX
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