Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A Triple-Arginine Motif in the Amino-Terminal Domain and Oligomerization Are Required for HIV-1 Inhibition by Human MX2

12 Feb 2015

Abstract excerpt

We have employed molecular genetic approaches to understand the domain organization of the HIV-1 resistance factor myxovirus resistance 2 (MX2). First, we describe an essential triple-arginine motif in the amino-terminal domain. Second, we demonstrate that this 91-residue domain mediates antiviral activity when appended to heterologous proteins, and we provide genetic evidence that protein oligomerization is...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Viral Infections and Immunology Research
Share to Virology and Viral Diseases
Share to Virus-based gene therapy research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 25673704
DOI: 10.1128/jvi.00169-15

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A Triple-Arginine Motif in the Amino-Terminal Domain and Oligomerization Are Required for HIV-1 Inhibition by Human MX2PMID 25673704Read ↗

Host and Viral Determinants of Mx2 Antiretroviral ActivitySemantic proximity Read ↗

The N-terminal domain of MX1 proteins is essential for their antiviral activity against different families of RNA virusesSemantic proximity Read ↗

MX2 viral substrate breadth and inhibitory activity are regulated by protein phosphorylationSemantic proximity Read ↗

Functional diversity of Mx proteins: variations on a theme of host resistance to infection.Semantic proximity Read ↗

MxB restricts HIV-1 by targeting the tri-hexamer interface of the viral capsidSemantic proximity Read ↗

Structural requirements for the antiviral activity of the human MxA protein against Thogoto and influenza A virus.Semantic proximity Read ↗

An Evolutionary Insertion in the Mxra8 Receptor-Binding Site Confers Resistance to Alphavirus Infection and PathogenesisSemantic proximity Read ↗

Intramolecular backfolding of the carboxyl-terminal end of MxA protein is a prerequisite for its oligomerization.Semantic proximity Read ↗

A single polymorphic residue in humans underlies species-specific restriction of HSV-1 by the antiviral protein MxBSemantic proximity Read ↗

A Single Amino Acid Change in the SPRY Domain of Human Trim5α Leads to HIV-1 RestrictionSemantic proximity Read ↗

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

An evolutionary perspective on the broad antiviral specificity of MxASemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.