Varaico: Literature-Extracted Genetic Variants

Gene:MX1
Variant:p.S35T
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MX1

NM_002462.5:p.S35T

Associated Papers

An evolutionarily conserved N-terminal leucine is essential for MX1 GTPase antiviral activity against different families of RNA viruses.

McKellar J et al.

The Journal of Biological Chemistry, 2023

Increased Polymerase Activity of Zoonotic H7N9 Allows Partial Escape from MxA.

Petric PP et al.

Viruses, 2022

Rare variant MX1 alleles increase human susceptibility to zoonotic H7N9 influenza virus.

Chen Y et al.

Science (new York, N.y.), 2021

The 125th Lys and 145th Thr Amino Acids in the GTPase Domain of Goose Mx Confer Its Antiviral Activity against the Tembusu Virus.

Chen S et al.

Viruses, 2018

Effects of allelic variations in the human myxovirus resistance protein A on its antiviral activity.

Graf L et al.

The Journal of Biological Chemistry, 2018

Conformational dynamics of dynamin-like MxA revealed by single-molecule FRET.

Chen Y et al.

Nature Communications, 2017

Role of nucleotide binding and GTPase domain dimerization in dynamin-like myxovirus resistance protein A for GTPase activation and antiviral activity.

Dick A et al.

The Journal of Biological Chemistry, 2015

Stalk domain of the dynamin-like MxA GTPase protein mediates membrane binding and liposome tubulation via the unstructured L4 loop.

von der Malsburg A et al.

The Journal of Biological Chemistry, 2011

Inhibition of tumor cell motility by the interferon-inducible GTPase MxA.

Mushinski JF et al.

The Journal of Biological Chemistry, 2009

MxA, a member of the dynamin superfamily, interacts with the ankyrin-like repeat domain of TRPC.

Lussier MP et al.

The Journal of Biological Chemistry, 2005

Self-assembly of human MxA GTPase into highly ordered dynamin-like oligomers.

Kochs G et al.

The Journal of Biological Chemistry, 2002

Dominant-negative mutants of human MxA protein: domains in the carboxy-terminal moiety are important for oligomerization and antiviral activity.

Ponten A et al.

Journal of Virology, 1997

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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."