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Journal article

Naturally occurring Phe151Leu substitution near a conserved folding module lowers stability of glutathione transferase P1-1

HJ Lin, AS Johansson, G Stenberg, AM Materi, JM Park, AH Dai, HY Zhou, JSY Gim, IH Kau, SI Hardy, MW Parker, B Mannervik

Biochimica et Biophysica Acta-Proteins and Proteomics | ELSEVIER SCIENCE BV | Published : 2003

DOI: 10.1016/S1570-9639(03)00149-3

University of Melbourne Researchers

Michael Parker's Profile Picture
Michael Parker Author Biochemistry and Pharmacology

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Citation metrics

11Web of Science
14Scopus
11Dimensions

Keywords

Polymorphism, Genetic
Glutathione Transferase
Glutathione S-Transferase Pi
African Continental Ancestry Group
Human-Placenta
Models, Molecular
Colorectal-Cancer
Amino Acid Substitution
Breast-Cancer
Leucine
S-Transferase
Protein Folding
Biophysics
Sensitive Gel-Electrophoresis
Dinitrochlorobenzene
Genetic Variation
Kinetics
N-Capping Box
Biochemistry & Molecular Biology
Pi
Folding Module
Chemical Hepatocarcinogenesis
Humans
Life Sciences & Biomedicine
Hydrophobic-Staple Motif
Half-Life
Hydrophobic and Hydrophilic Interactions
Gst Motif Ii
Isoenzymes
Science & Technology
Enzyme Stability
Gstp1 Variant
Phenylalanine
Gene
Amino Acid Motifs

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