Varaico: Literature-Extracted Genetic Variants

Gene:SDS
Variant:p.C49Y
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SDS

NM_006843.3:p.C49Y

Associated Papers

A redox-active HybG-HypD scaffold complex is required for optimal ATPase activity during [NiFe]-hydrogenase maturation in Escherichia coli.

Haase A et al.

Febs Open Bio, 2023

Succinate dehydrogenase variants in paraganglioma: why are B subunit variants 'bad'?

Gruber LM et al.

Endocrine Oncology (bristol, England), 2023

37434649 (PubMed )
Supplement: supplementary_table_1.xlsx › Missense_Variants

Intramolecular Interactions and Regulation of Cofactor Binding by the Four Repressive Elements in the Caspase Recruitment Domain-containing Protein 11 (CARD11) Inhibitory Domain.

Jattani RP et al.

The Journal of Biological Chemistry, 2016

Molecular Characterization of Gβ-Like Protein CpcB Involved in Antifungal Drug Susceptibility and Virulence in A. fumigatus.

Cai Z et al.

Frontiers in Microbiology, 2016

Identification of an L-phenylalanine binding site enhancing the cooperative responses of the calcium-sensing receptor to calcium.

Zhang C et al.

The Journal of Biological Chemistry, 2014

G146V mutation at the hinge region of actin reveals a myosin class-specific requirement of actin conformations for motility.

Noguchi TQ et al.

The Journal of Biological Chemistry, 2012

Mutational analysis of conserved glycine residues 142, 143 and 146 reveals Gly(142) is critical for tetramerization of CTP synthase from Escherichia coli.

Lunn FA et al.

The Biochemical Journal, 2008

Contribution of glycine 146 to a conserved folding module affecting stability and refolding of human glutathione transferase p1-1.

Kong GK et al.

The Journal of Biological Chemistry, 2003

Identification of essential amino acid residues for catalytic activity and thermostability of novel chitosanase by site-directed mutagenesis.

Yoon HG et al.

Applied Microbiology and Biotechnology, 2001

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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."