Explaining an Unusually Fast Parasitic Enzyme: Folate Tail-Binding Residues Dictate Substrate Positioning and Catalysis in Cryptosporidium hominis Thymidylate Synthase † ‡ - Test2 - elhamkhani - TriplyDB

Explaining an Unusually Fast Parasitic Enzyme: Folate Tail-Binding Residues Dictate Substrate Positioning and Catalysis in Cryptosporidium hominis Thymidylate Synthase † ‡

Explaining an Unusually Fast Parasitic Enzyme: Folate Tail-Binding Residues Dictate Substrate Positioning and Catalysis in Cryptosporidium hominis Thymidylate Synthase † ‡

http://www.wikidata.org/entity/Q27651391

about

Mg 2+ Binds to the Surface of Thymidylate Synthase and Affects Hydride Transfer at the Interior Active Site First Three-Dimensional Structure of Toxoplasma gondii Thymidylate Synthase–Dihydrofolate Reductase: Insights for Catalysis, Interdomain Interactions, and Substrate Channeling 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)Cryptosporidium: genomic and biochemical features Structural studies provide clues for analog design of specific inhibitors of Cryptosporidium hominis thymidylate synthase-dihydrofolate reductase.

P2860

Q27677524-99A268C4-7191-4B16-801C-48DE3407ACCD Q27680002-DD1202E5-81B5-4C19-84BE-D5E538572752 Q27680861-E6D14135-1274-4473-8E9D-1C7B49A9C284 Q33641940-B9DFA6AB-3BEC-4779-88B3-BD1BE5F38936 Q40524360-1DEBDFD5-4EC5-4C87-85AE-CBBB2825F5A3

P2860

Explaining an Unusually Fast Parasitic Enzyme: Folate Tail-Binding Residues Dictate Substrate Positioning and Catalysis in Cryptosporidium hominis Thymidylate Synthase † ‡

http://www.wikidata.org/entity/Q27651391

description

2008 nî lūn-bûn

@nan

2008 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

name

Explaining an Unusually Fast P ...... minis Thymidylate Synthase † ‡

@ast

Explaining an Unusually Fast P ...... minis Thymidylate Synthase † ‡

@en

Explaining an Unusually Fast P ...... minis Thymidylate Synthase † ‡

@nl

type

label

Explaining an Unusually Fast P ...... minis Thymidylate Synthase † ‡

@ast

Explaining an Unusually Fast P ...... minis Thymidylate Synthase † ‡

@en

Explaining an Unusually Fast P ...... minis Thymidylate Synthase † ‡

@nl

prefLabel

Explaining an Unusually Fast P ...... minis Thymidylate Synthase † ‡

@ast

Explaining an Unusually Fast P ...... minis Thymidylate Synthase † ‡

@en

Explaining an Unusually Fast P ...... minis Thymidylate Synthase † ‡

@nl

P1433

Q27651391-D5104EB2-5575-4847-BAB4-DF711A9805BD

P1476

Q27651391-664E7EAD-EC50-4033-9C84-616CA60037E5

P2093

Q27651391-35E295BD-F201-430A-B357-0E6B1384D569

Q27651391-4E744D3F-E7D7-43FB-A227-E62E920BECB0

Q27651391-B0F347C3-B90C-40C4-B9E7-116F5B819EBC

P2860

Q27651391-00C58DD4-8D4C-44BD-B6B4-A5F2E9ADB98E

Q27651391-0289D3B7-852A-4BC9-B5D2-A81559785897

Q27651391-11D85B0E-4D80-45E6-B2A7-F5978B13B55F

Q27651391-11F5930E-D20F-42C4-ADA6-7951769EEB7F

Q27651391-135ED641-072B-44D3-B155-68383509CFD2

Q27651391-1A66B0C5-320B-4165-8310-9A7B00DA6A38

Q27651391-26234029-8F3C-4CAD-8675-DB62561A2F46

Q27651391-26D9FD2D-067C-48B7-8ACD-45F3A74E944B

Q27651391-2F9D65FB-3838-4F09-9EB9-16E9A546C8BA

Q27651391-3B71528D-BAF8-406A-B6ED-44B0F6457432

P304

Q27651391-5B8551F8-663E-4040-9395-953F1059B942

P31

Q27651391-225C3A77-8529-4B62-8DA8-09CDF5541EBA

P356

Q27651391-FD2C64B5-C794-48C9-924D-D987BDF0E6F1

P407

Q27651391-8B4C4276-7C3A-468F-AD97-9F5B4B8F33C7

P433

Q27651391-B8E099D4-499B-4FCC-90B2-6E8C6857C62C

P478

Q27651391-403067A4-E331-4E61-9831-E6F7DEE0C068

P577

Q27651391-C1D95644-2813-43A6-8419-461856C88560

P5875

Q27651391-D08F3E02-9334-482E-B765-B6558B956B2F

P698

Q27651391-69BC01DD-CD00-42E9-B57E-624E36A04D52

P932

Q27651391-A59DD6C9-A74A-4BE2-B60A-C326BB4119AB

P356

P1433

P1476

Explaining an Unusually Fast P ...... minis Thymidylate Synthase † ‡

@en

P2093

Karen S Anderson

http://www.w3.org/2001/XMLSchema#string

Melissa A Vargo

http://www.w3.org/2001/XMLSchema#string

W Edward Martucci

http://www.w3.org/2001/XMLSchema#string

P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

The structural mechanism for half-the-sites reactivity in an enzyme, thymidylate synthase, involves a relay of changes between subunits

Crystal structure of a deletion mutant of human thymidylate synthase Δ (7-29) and its ternary complex with Tomudex and dUMP

Approaches to solving the rigid receptor problem by identifying a minimal set of flexible residues during ligand docking

Tryptophan 80 and leucine 143 are critical for the hydride transfer step of thymidylate synthase by controlling active site access

The only active mutant of thymidylate synthase D169, a residue far from the site of methyl transfer, demonstrates the exquisite nature of enzyme specificity

Phylogenetic classification of protozoa based on the structure of the linker domain in the bifunctional enzyme, dihydrofolate reductase-thymidylate synthase

Nonconserved residues Ala287 and Ser290 of the Cryptosporidium hominis thymidylate synthase domain facilitate its rapid rate of catalysis

Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding

P304

8902-11

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1021/BI800466Z

http://www.w3.org/2001/XMLSchema#string

P407

P433

34

http://www.w3.org/2001/XMLSchema#string

P478

47

http://www.w3.org/2001/XMLSchema#string

P577

2008-08-26T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

23143047

http://www.w3.org/2001/XMLSchema#string

P698

18672899

http://www.w3.org/2001/XMLSchema#string

P932

2613286

http://www.w3.org/2001/XMLSchema#string