ESR Resolves the C Terminus Structure of the Ligand-free Human Glutathione S-Transferase A1-1.

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ESR Resolves the C Terminus Structure of the Ligand-free Human Glutathione S-Transferase A1-1.

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2018 nî lūn-bûn

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2018年の論文

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2018年学术文章

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ESR Resolves the C Terminus St ...... lutathione S-Transferase A1-1.

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ESR Resolves the C Terminus St ...... lutathione S-Transferase A1-1.

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ESR Resolves the C Terminus St ...... lutathione S-Transferase A1-1.

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ESR Resolves the C Terminus St ...... lutathione S-Transferase A1-1.

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ESR Resolves the C Terminus St ...... lutathione S-Transferase A1-1.

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ESR Resolves the C Terminus St ...... lutathione S-Transferase A1-1.

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P1476

ESR Resolves the C Terminus St ...... Glutathione S-Transferase A1-1

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P2093

Frederick Lanni

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Gordon S Rule

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John R Pettersson

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Matthew J Lawless

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P2860

The contribution of the C-terminal sequence to the catalytic activity of GST2, a human alpha-class glutathione transferase

Localization of the C-terminus of rat glutathione S-transferase A1-1: crystal structure of mutants W21F and W21F/F220Y

1.3-A resolution structure of human glutathione S-transferase with S-hexyl glutathione bound reveals possible extended ligandin binding site

Structural origin of weakly ordered nitroxide motion in spin-labeled proteins

Stability of the domain interface contributes towards the catalytic function at the H-site of class alpha glutathione transferase A1-1

The interaction of the chemotherapeutic drug chlorambucil with human glutathione transferase A1-1: kinetic and structural analysis

The C-terminus of glutathione S-transferase A1-1 is required for entropically-driven ligand binding

The catalytic Tyr-9 of glutathione S-transferase A1-1 controls the dynamics of the C terminus

Glutathione transferases

The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance

P304

592-601

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P31

scholarly article

P356

10.1016/J.BPJ.2017.12.016

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P407

English

P433

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P478

114

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P50

Sunil Saxena

P577

2018-02-01T00:00:00Z

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P698

29414705

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P932

5985033

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