Nonconserved residues Ala287 and Ser290 of the Cryptosporidium hominis thymidylate synthase domain facilitate its rapid rate of catalysis
about
Explaining an Unusually Fast Parasitic Enzyme: Folate Tail-Binding Residues Dictate Substrate Positioning and Catalysis in Cryptosporidium hominis Thymidylate Synthase † ‡Inhibitor-bound complexes of dihydrofolate reductase-thymidylate synthase from Babesia bovisMg 2+ Binds to the Surface of Thymidylate Synthase and Affects Hydride Transfer at the Interior Active SiteSubstituted pyrrolo[2,3-d]pyrimidines as Cryptosporidium hominis thymidylate synthase inhibitorsFirst Three-Dimensional Structure of Toxoplasma gondii Thymidylate Synthase–Dihydrofolate Reductase: Insights for Catalysis, Interdomain Interactions, and Substrate ChannelingExploring 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)Cryptosporidium: genomic and biochemical featuresTopoisomerase I expression is associated with prognosis in postoperative non-small cell lung cancer patientsNovel non-active site inhibitor of Cryptosporidium hominis TS-DHFR identified by a virtual screenProbing the role of parasite-specific, distant structural regions on communication and catalysis in the bifunctional thymidylate synthase-dihydrofolate reductase from Plasmodium falciparumStructural studies provide clues for analog design of specific inhibitors of Cryptosporidium hominis thymidylate synthase-dihydrofolate reductase.Selective peptide inhibitors of bifunctional thymidylate synthase-dihydrofolate reductase from Toxoplasma gondii provide insights into domain-domain communication and allosteric regulation.
P2860
Q27651391-26D9FD2D-067C-48B7-8ACD-45F3A74E944BQ27673544-03CA7D0E-60EF-466E-A171-E4C27216508FQ27677524-271F06FC-3CCB-459F-882E-EC498DE0B5D5Q27679459-A39EBAC7-B058-44F1-AA96-5D88299F09CFQ27680002-4AEDF9C3-B927-4321-B00A-61BBD8313480Q27680861-5A34BD55-A0CC-4154-8E63-344A0919DA2AQ33641940-A4BCDB1B-344E-4BC1-BF33-3C944EBBFC54Q37060409-741A8753-8DB9-4793-87D2-34BD339A586DQ37117303-701176DB-AAD8-4AF5-9D7D-2254F3ED9675Q37136020-DD502D97-A995-470E-8DAD-4E3A43CEAF64Q40524360-D8C9871F-691C-49C6-8BAF-778F09B21303Q42632086-3D909A7B-627A-4AEC-90DC-826E61A23C31
P2860
Nonconserved residues Ala287 and Ser290 of the Cryptosporidium hominis thymidylate synthase domain facilitate its rapid rate of catalysis
description
2007 nî lūn-bûn
@nan
2007 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Nonconserved residues Ala287 a ...... te its rapid rate of catalysis
@ast
Nonconserved residues Ala287 a ...... te its rapid rate of catalysis
@en
Nonconserved residues Ala287 a ...... te its rapid rate of catalysis
@nl
type
label
Nonconserved residues Ala287 a ...... te its rapid rate of catalysis
@ast
Nonconserved residues Ala287 a ...... te its rapid rate of catalysis
@en
Nonconserved residues Ala287 a ...... te its rapid rate of catalysis
@nl
prefLabel
Nonconserved residues Ala287 a ...... te its rapid rate of catalysis
@ast
Nonconserved residues Ala287 a ...... te its rapid rate of catalysis
@en
Nonconserved residues Ala287 a ...... te its rapid rate of catalysis
@nl
P2093
P3181
P356
P1433
P1476
Nonconserved residues Ala287 a ...... te its rapid rate of catalysis
@en
P2093
Chloé E Atreya
Karen S Anderson
Lanxuan T Doan
Melissa A Vargo
W Edward Martucci
P304
P3181
P356
10.1021/BI700531R
P407
P577
2007-07-17T00:00:00Z