Opposite effect of polymorphic mutations on the electrostatic aggregation of human alanine:glyoxylate aminotransferase: implications for the pathogenesis of Primary Hyperoxaluria Type I-Reference-Cited by-同舟云学术

Opposite effect of polymorphic mutations on the electrostatic aggregation of human alanine:glyoxylate aminotransferase: implications for the pathogenesis of Primary Hyperoxaluria Type I

Published:2017-09-14 Issue: Volume: Page:
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:FEBS J

Author:

Dindo Mirco¹,Conter Carolina¹,Cellini Barbara²

Affiliation:

1. Department of Neurosciences, Biomedicine and Movement Sciences; Section of Biological Chemistry; University of Verona; Strada Le Grazie 8 37134 Verona Italy

2. Department of Experimental Medicine; University of Perugia; Piazzale Gambuli 1 06132 Perugia Italy

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/febs.14269/fullpdf

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1. Evaluation of the impact of antibody fragments on aggregation of intact molecules via size exclusion chromatography coupled with native mass spectrometry;mAbs;2024-03-27

2. Insights into the pathogenesis of primary hyperoxaluria type I from the structural dynamics of alanine:glyoxylate aminotransferase variants;FEBS Letters;2024-01-19

3. Biochemical and cellular effects of a novel missense mutation of the AGXT gene associated with Primary Hyperoxaluria Type 1;Biochemical and Biophysical Research Communications;2023-02

4. Structural dynamics shape the fitness window of alanine:glyoxylate aminotransferase;Protein Science;2022-04-11

5. Cryptic genetic variations of alanine:glyoxylate aminotransferase shape its fitness and dynamics;2021-05-25