Disruption of the crossover helix impairs dihydrofolate reductase activity in the bifunctional enzyme TS-DHFR from Cryptosporidium hominis.
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Exploring novel strategies for AIDS protozoal pathogens: α-helix mimetics targeting a key allosteric protein–protein interaction in C. hominis thymidylate synthase-dihydrofolate reductase (TS-DHFR)Insights into the role of the junctional region of Plasmodium falciparum dihydrofolate reductase-thymidylate synthase.Understanding the molecular mechanism of substrate channeling and domain communication in protozoal bifunctional TS-DHFR.Selective peptide inhibitors of bifunctional thymidylate synthase-dihydrofolate reductase from Toxoplasma gondii provide insights into domain-domain communication and allosteric regulation.
P2860
Disruption of the crossover helix impairs dihydrofolate reductase activity in the bifunctional enzyme TS-DHFR from Cryptosporidium hominis.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on February 2009
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vedecký článok
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Disruption of the crossover he ...... from Cryptosporidium hominis.
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Disruption of the crossover he ...... from Cryptosporidium hominis.
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type
label
Disruption of the crossover he ...... from Cryptosporidium hominis.
@en
Disruption of the crossover he ...... from Cryptosporidium hominis.
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prefLabel
Disruption of the crossover he ...... from Cryptosporidium hominis.
@en
Disruption of the crossover he ...... from Cryptosporidium hominis.
@nl
P2093
P2860
P356
P1433
P1476
Disruption of the crossover he ...... from Cryptosporidium hominis.
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P2093
Karen S Anderson
Melissa A Vargo
W Edward Martucci
P2860
P304
P356
10.1042/BJ20081247
P407
P577
2009-02-01T00:00:00Z