Self-assembly of Human MxA GTPase into Highly Ordered Dynamin-like Oligomers*
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Summary
It is shown that recombinant MxA protein assembles into long filamentous structures with a diameter of about 20 nm at physiological salt concentration as demonstrated by sedimentation assays and electron microscopy.
- Type
- article
- Published
- 2002-04-19
- Cited by
- 105
- References
- 53
- Access
- Open access
- OpenAlex
- https://openalex.org/W2019532014
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:23324978
Keywords
GTPase, Dynamin, Chemistry, Cell biology, Computational biology
References
- The dynamins: redundant or distinct functions for an expanding family of related GTPases?
- Phragmoplastin, a dynamin‐like protein associated with cell plate formation in plants.
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- Structure of mouse Mx1 protein. Molecular assembly and GTP-dependent conformational change.
- Resistance to influenza virus and vesicular stomatitis virus conferred by expression of human MxA protein
- Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis
- Human MxA Protein Protects Mice Lacking a Functional Alpha/Beta Interferon System against La Crosse Virus and Other Lethal Viral Infections
- A functional GTP-binding motif is necessary for antiviral activity of Mx proteins
- Interferon-regulated Mx genes are not responsive to interleukin-1, tumor necrosis factor, and other cytokines
- Interferon-induced human protein with homology to protein Mx of influenza virus-resistant mice.
- Dynamin undergoes a GTP-dependent conformational change causing vesiculation.
- Signaling mechanistics: aluminum fluoride for molecule of the year.
- Aluminium fluoride associates with the small guanine nucleotide binding proteins
- GTPase mechanism of Gproteins from the 1.7-Å crystal structure of transducin α - GDP AIF−4
- Unexpected Structural Requirements for GTPase Activity of the Interferon-induced MxA Protein(*)
- A putative GTP binding protein homologous to interferon-inducible Mx proteins performs an essential function in yeast protein sorting.
- MxA GTPase: oligomerization and GTP-dependent interaction with viral RNP target structures.
- Dynamin Self-assembly Stimulates Its GTPase Activity*
- A Model for Dynamin Self-assembly Based on Binding Between Three Different Protein Domains*
Cited by
- Analysis of the role of the p47 GTPase IIGP1 in Resistance against Intracellular Pathogens
- Visualization of dynamins.
- Characterization, regulation and expression of the myxovirus resistance (Mx) genes in ovine endometrium and immune cells during early pregnancy
- Relationship between function and 3D-structure of interferon inducible GTPases
- Assay and functional analysis of dynamin-like Mx proteins.
- Missorting of LaCrosse Virus Nucleocapsid Protein by the Interferon‐Induced MxA GTPase Involves Smooth ER Membranes
- Cellular mechanisms of hantavirus-induced apoptosis
- Biochemische Charakterisierung der Oligomerisierung des Interferon-gamma-induzierten humanen Guanylat-bindenden Proteins I
- Cell-Biology of Interferon Inducible GTPases
- Oligomerization Requirements for MX2-Mediated Suppression of HIV-1 Infection
- IIGP1, an Interferon-γ-inducible 47-kDa GTPase of the Mouse, Showing Cooperative Enzymatic Activity and GTP-dependent Multimerization*
- Dynamin-like MxA GTPase: Structural Insights into Oligomerization and Implications for Antiviral Activity*
- Ca2+/Calmodulin-Dependent Protein Kinase IIα Is Required for the Initiation and Maintenance of Opioid-Induced Hyperalgesia
- Structural basis of oligomerization in the stalk region of dynamin-like MxA
- Inhibition of the Type I Interferon Antiviral Response During Arenavirus Infection
- Grouper Mx confers resistance to nodavirus and interacts with coat protein.
- Identification of residues in the human guanylate-binding protein 1 critical for nucleotide binding and cooperative GTP hydrolysis.
- Stalk Domain of the Dynamin-like MxA GTPase Protein Mediates Membrane Binding and Liposome Tubulation via the Unstructured L4 Loop*
- The Mx GTPase family of interferon-induced antiviral proteins.
- Dynamin and endocytosis.
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