The Conserved N-capping Box in the Hydrophobic Core of GlutathioneS-Transferase P1–1 Is Essential for Refolding (Q57081183)

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scientific article published in Journal of Biological Chemistry

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English	The Conserved N-capping Box in the Hydrophobic Core of GlutathioneS-Transferase P1–1 Is Essential for Refolding	scientific article published in Journal of Biological Chemistry

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9325266 AND SRC:MED&resulttype=core&format=json

6 November 2019

The conserved N-capping box in the hydrophobic core of glutathione S-transferase P1-1 is essential for refolding. Identification of a buried and conserved hydrogen bond important for protein stability (English)

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9325266 AND SRC:MED&resulttype=core&format=json

6 November 2019

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Sonia Michaela Melino

3

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9325266 AND SRC:MED&resulttype=core&format=json

6 November 2019

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B Dragani

1

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9325266 AND SRC:MED&resulttype=core&format=json

6 November 2019

G Stenberg

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9325266 AND SRC:MED&resulttype=core&format=json

6 November 2019

R Petruzzelli

4

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6 November 2019

B Mannervik

5

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9325266 AND SRC:MED&resulttype=core&format=json

6 November 2019

A Aceto

6

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6 November 2019

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1 October 1997

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9325266 AND SRC:MED&resulttype=core&format=json

6 November 2019

Journal of Biological Chemistry

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9325266 AND SRC:MED&resulttype=core&format=json

6 November 2019

272

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6 November 2019

41

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6 November 2019

25518-25523

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6 November 2019

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

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-A resolution

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

Eukaryotic translation elongation factor 1 gamma contains a glutathione transferase domain--study of a diverse, ancient protein superfamily using motif search and structural modeling

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

Identification of an N-capping box that affects the alpha 6-helix propensity in glutathione S-transferase superfamily proteins: a role for an invariant aspartic residue.

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

Hydrogen bonding in globular proteins

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

High-Level Bacterial Expression of Human Glutathione Transferase P1-1 Encoded by Semisynthetic DNA

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

DNA sequencing with chain-terminating inhibitors

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

Dissociation and unfolding of Pi-class glutathione transferase. Evidence for a monomeric inactive intermediate

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

Differential activity of human, rat, mouse and bacteria glutathione transferase isoenzymes towards 4-nitroquinoline 1-oxide.

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

Sequence determinants of the capping box, a stabilizing motif at the N-termini of alpha-helices

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

The hydrophobic-staple motif and a role for loop-residues in α-helix stability and protein folding

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

Helix signals in proteins

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

Conserved residues and the mechanism of protein folding

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

In vitro absorption of inorganic phosphate and other electrolytes in the carp intestine

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

Site-directed mutagenesis study on the roles of evolutionally conserved aspartic acid residues in human glutathione S-transferase P1-1

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

Helix stop signals in proteins and peptides: the capping box

1 reference

https://api.crossref.org/works/10.1074/JBC.272.41.25518

21 January 2018

Identifiers

10.1074/JBC.272.41.25518

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9325266 AND SRC:MED&resulttype=core&format=json

6 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9325266 AND SRC:MED&resulttype=core&format=json

6 November 2019

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