Triosephosphate isomerase from Plasmodium falciparum:. the crystal structure provides insights into antimalarial drug design (Q27741899)

DOI

https://api.crossref.org/works/10.1016/S0969-2126(97)00230-X

triosephosphate isomerase

11 November 2024

main subject

crystal structure

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Plasmodium falciparum

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12 September 2018

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25 September 2018

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15 December 2018

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19 December 2018

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20 December 2018

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20 December 2018

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20 December 2018

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20 December 2018

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author name string

S. S. Velanker

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S. S. Ray

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R. S. Gokhale

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S. Suma

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H. Balaram

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P. Balaram

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M. R. Murthy

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language of work or name

English

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National Center for Biotechnology Information

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full work available at URL

11 November 2024

publication date

15 June 1997

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http://www.cell.com/article/S096921269700230X/pdf

file format

Portable Document Format

online access status

open access

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https://api.elsevier.com/content/article/PII:S096921269700230X?httpAccept=text/xml

11 November 2024

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DOI

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https://api.elsevier.com/content/article/PII:S096921269700230X?httpAccept=text/plain

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DOI

https://api.crossref.org/works/10.1016/S0969-2126(97)00230-X

11 November 2024

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751-61

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Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: implications for the reaction mechanism

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Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interacti

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Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme

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Crystallographic binding studies with triosephosphate isomerases: Conformational changes induced by substrate and substrate-analogues

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Dynamics of the flexible loop of triosephosphate isomerase: the loop motion is not ligand gated

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Structure of the complex between trypanosomal triosephosphate isomerase and N‐hydroxy‐4‐phosphono‐butanamide: Binding at the active site despite an “open” flexible loop conformation

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Structure-based design of lipophilic quinazoline inhibitors of thymidylate synthase

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Species-specific inhibition of homologous enzymes by modification of nonconserved amino acids residues. The cysteine residues of triosephosphate isomerase

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