T
Thomas G. Consler
Researcher at Saint Louis University
Publications - 11
Citations - 387
Thomas G. Consler is an academic researcher from Saint Louis University. The author has contributed to research in topics: Pyruvate kinase & Allosteric regulation. The author has an hindex of 9, co-authored 11 publications receiving 386 citations. Previous affiliations of Thomas G. Consler include University of California, Los Angeles.
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Journal ArticleDOI
Properties and purification of an active biotinylated lactose permease from Escherichia coli.
Thomas G. Consler,Bengt Persson,Heinrich Jung,Zen Kh,Kirsten Jung,Gilbert G. Privé,G. Verner,H R Kaback +7 more
TL;DR: A simplified approach for purification of functional lactose permease from Escherichia coli is described that is based on the construction of chimeras between the permease and a 100-amino acid residue polypeptide containing the biotin acceptor domain from the oxaloacetate decarboxylase of Klebsiella pneumoniae.
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Role of proline residues in the structure and function of a membrane transport protein.
TL;DR: None of the alterations in permease activity is due to inability of the mutant proteins to insert into the membrane or to diminished lifetimes after insertion, since the concentration of each mutant permease in the membrane is comparable to that of wild-type permease as judged by immunological analyses.
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In vitro phosphorylation of the epidermal growth factor receptor autophosphorylation domain by c-src: identification of phosphorylation sites and c-src SH2 domain binding sites.
TL;DR: The identification of c- src phosphorylation sequences on EGFR as c-src SH2 binding sites supports the notion that this interaction plays a significant role in the regulation of growth factor receptor function and signal transduction.
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Effects of primary sequence differences on the global structure and function of an enzyme: a study of pyruvate kinase isozymes.
TL;DR: In this article, Noguchi et al. used phase-modulation measurements of the fluorescence lifetime of tryptophan residues under a variety of experimental conditions to provide insights into the effects of localized sequence change on the global structural and functional behavior of the enzyme.
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Domain interaction in rabbit muscle pyruvate kinase. II. Small angle neutron scattering and computer simulation.
TL;DR: The effects of ligands on the structure of rabbit muscle pyruvate kinase were studied by small angle neutron scattering, and results indicate a "contraction" and "expansion" of the enzyme when it transforms between its active and inactive forms.