Iron transport and storage proteins.
- P. Aisen, I. Listowsky
- Chemistry, BiologyAnnual Review of Biochemistry
The iron binding affinities of the sites, and the two-domain hypothesis of tronsfemn structure, are described.
Subunit diversity and tissue distribution of human glutathione S-transferases: interpretations based on electrospray ionization-MS and peptide sequence-specific antisera.
- J. Rowe, E. Nieves, I. Listowsky
- BiologyBiochemical Journal
- 15 July 1997
Subunit profiles were distinct and characteristic of the particular tissue type, and this tissue specificity in GST expression was evident even in organs from different individuals.
Intracellular binding and transport of hormones and xenobiotics by glutathione-S-transferases.
- I. Listowsky, M. Abramovitz, H. Homma, Y. Niitsu
- Biology, MedicineDrug metabolism reviews (Softcover ed.)
The present study focused on the binding and transport of Hormones and Xenobiotics by Glutathiones-Transferases, a type of “cell reprograming”, which has shown promise in understanding the mechanism behind drug resistance.
Nomenclature for mammalian soluble glutathione transferases.
- B. Mannervik, P. Board, J. Hayes, I. Listowsky, W. Pearson
- BiologyMethods in Enzymology
Selective expression of a unique glutathione S-transferase Yb3 gene in rat brain.
- M. Abramovitz, I. Listowsky
- BiologyJournal of Biological Chemistry
- 5 June 1987
Differential Localization of Glutathione‐S‐Transferase Yp and Yb Subunits in Oligodendrocytes and Astrocytes of Rat Brain
- W. Cammer, F. Tansey, M. Abramovitz, S. Ishigaki, I. Listowsky
- BiologyJournal of Neurochemistry
- 1 March 1989
The finding of glutathione‐S‐transferases in ependymal cells and astrocytes in the brain also suggests that this enzyme could be a first line of defense against toxic substances.
Transition state model and mechanism of nucleophilic aromatic substitution reactions catalyzed by human glutathione S-transferase M1a-1a.
- Y. Patskovsky, L. Patskovska, S. Almo, I. Listowsky
- Chemistry, BiologyBiochemistry
- 28 March 2006
Transition states in which Tyr115, Tyr6, and His107 side chains are involved in the stabilization of the Meisenheimer complex via interactions with the ortho nitro group of CDNB or FDNB and provide insight into the means by which GSTs adapt to accommodate different substrates are provided.
Reaction mechanisms of allicin and allyl-mixed disulfides with proteins and small thiol molecules.
- T. Miron, I. Listowsky, M. Wilchek
- Chemistry, BiologyEuropean journal of medicinal chemistry
- 1 May 2010
Distinctive structure of the human GSTM3 gene-inverted orientation relative to the mu class glutathione transferase gene cluster.
- Y. Patskovsky, M. Huang, T. Takayama, I. Listowsky, W. Pearson
- BiologyArchives of Biochemistry and Biophysics
The sequence and exon-intron structure of the human class mu GSTM3 glutathione transferase gene and its orientation with respect to the remainder of the human class mu GSTM gene cluster were…
An asparagine-phenylalanine substitution accounts for catalytic differences between hGSTM3-3 and other human class mu glutathione S-transferases.
- Y. Patskovsky, L. Patskovska, I. Listowsky
- 7 December 1999
It was determined that a Y119F mutation considerably enhanced the turnover rate of the enzyme for nucleophilic aromatic substitution reactions, and a polar Asn212 in place of a Phe residue found in the cognate position of other mu class glutathione S-transferases has a marked influence on catalysis by hGSTM3-3.