PERFORM Publications

The folding capacity of the mature domain of the dual-targeted plant tRNA nucleotidyltransferase influences organelle selection.

Author(s): Leibovitch M, Bublak D, Hanic-Joyce PJ, Tillmann B, Flinner N, Amsel D, Scharf KD, Mirus O, Joyce PB, Schleiff E

Biochem J. 2013 Aug 01;453(3):401-12 Authors: Leibovitch M, Bublak D, Hanic-Joyce PJ, Tillmann B, Flinner N, Amsel D, Scharf KD, Mirus O, Joyce PB, Schleiff E

Article GUID: 23713568

In vitro studies of disease-linked variants of human tRNA nucleotidyltransferase reveal decreased thermal stability and altered catalytic activity.

Author(s): Leibovitch M, Hanic-Joyce PJ, Joyce PBM

Biochim Biophys Acta Proteins Proteom. 2018 Apr;1866(4):527-540 Authors: Leibovitch M, Hanic-Joyce PJ, Joyce PBM

Article GUID: 29454993

Analysis of the pathogenic I326T variant of human tRNA nucleotidyltransferase reveals reduced catalytic activity and thermal stability in vitro linked to a conformational change.

Author(s): Leibovitch M, Reid NE, Victoria J, Hanic-Joyce PJ, Joyce PBM

Biochim Biophys Acta Proteins Proteom. 2019 Jun;1867(6):616-626 Authors: Leibovitch M, Reid NE, Victoria J, Hanic-Joyce PJ, Joyce PBM

Article GUID: 30959222

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The folding capacity of the mature domain of the dual-targeted plant tRNA nucleotidyltransferase influences organelle selection.

In vitro studies of disease-linked variants of human tRNA nucleotidyltransferase reveal decreased thermal stability and altered catalytic activity.

Analysis of the pathogenic I326T variant of human tRNA nucleotidyltransferase reveals reduced catalytic activity and thermal stability in vitro linked to a conformational change.