(Q46130535)

19 December 2017

title

Structure of and kinetic channelling in bifunctional dihydrofolate reductase-thymidylate synthase (English)

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19 December 2017

author name string

Knighton DR

1

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19 December 2017

Kan CC

2

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19 December 2017

Howland E

3

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19 December 2017

Janson CA

4

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19 December 2017

Hostomska Z

5

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19 December 2017

Welsh KM

6

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19 December 2017

Matthews DA

7

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19 December 2017

publication date

1 March 1994

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19 December 2017

Nature structural biology

published in

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19 December 2017

volume

1

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19 December 2017

issue

3

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19 December 2017

page(s)

186-194

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19 December 2017

The origin of the bifunctional dihydrofolate reductase-thymidylate synthase isogenes of Arabidopsis thaliana

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Plastic adaptation toward mutations in proteins: structural comparison of thymidylate synthases

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Atomic structure of thymidylate synthase: target for rational drug design

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Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate

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Structures of thymidylate synthase with a C-terminal deletion: role of the C-terminus in alignment of 2'-deoxyuridine 5'-monophosphate and 5,10-methylenetetrahydrofolate

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Physiological significance of metabolic channelling

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The electrostatic potential of B-DNA.

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Bifunctional thymidylate synthase-dihydrofolate reductase in protozoa

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inferred from DOI database lookup

7 January 2021

based on heuristic

Enzyme organization and the direction of metabolic flow: physicochemical considerations

1 reference

https://api.crossref.org/works/10.1038%2FNSB0394-186

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NSB0394-186

1 reference

19 December 2017

1 reference

19 December 2017