Varaico: Literature-Extracted Genetic Variants

Gene:SDS
Variant:p.H59Q
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SDS

NM_006843.3:p.H59Q

Associated Papers

Autoinflammatory mutation in NLRC4 reveals a leucine-rich repeat (LRR)-LRR oligomerization interface.

Moghaddas F et al.

The Journal of Allergy and Clinical Immunology, 2018

A PP2A active site mutant impedes growth and causes misregulation of native catalytic subunit expression.

Lizotte DL et al.

Journal of Cellular Biochemistry, 2008

Mutant R1 proteins from Escherichia coli class Ia ribonucleotide reductase with altered responses to dATP inhibition.

Birgander PL et al.

The Journal of Biological Chemistry, 2004

A novel and essential mechanism determining specificity and activity of protein phosphatase 2A (PP2A) in vivo.

Fellner T et al.

Genes & Development, 2003

Effects of substitution of conserved amino acid residues on the sugar-binding property of the tandem-repeat 32-kDa galectin of the nematode Caenorhabditis elegans.

Arata A et al.

Biological & Pharmaceutical Bulletin, 2001

Catalytically inactive protein phosphatase 2A can bind to polyomavirus middle tumor antigen and support complex formation with pp60(c-src).

Ogris E et al.

Journal of Virology, 1999

A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A.

Ogris E et al.

The Journal of Biological Chemistry, 1999

Thermoanaerobacter brockii alcohol dehydrogenase: characterization of the active site metal and its ligand amino acids.

Bogin O et al.

Protein Science : a Publication of the Protein Society, 1997

Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase.

Haribabu B et al.

The Embo Journal, 1995

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Regarding the variants extracted from papers and shown text snippets from research papers, the following holds: "Some rights reserved. This work permits non-commercial use, distribution and reproduction in any medium, provided the original author and source are credited."