ArticleMolecular immunology2007
Mutagenesis, biochemical, and biophysical characterization of Mycoplasma arthritidis-derived mitogen.
Article in Molecular immunology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Structure, Function, and Inhibition of Adenylosuccinate Lyase (ADSL) fromACS infectious diseases · 2026Article
- Refolding of a fully functional flavivirus methyltransferase revealed that S-adenosyl methionine but not S-adenosyl homocysteine is copurified with flavivirus methyltransferase.Protein science : a publication of the Protein Society · 2015Article
- Crystal structure of the Mycoplasma arthritidis-derived mitogen in apo form reveals a 3D domain-swapped dimer.Journal of molecular biology · 2010Article
- Association of Mycoplasma arthritidis mitogen with lethal toxicity but not with arthritis in mice.Infection and immunity · 2008Article
- Zinc induces dimerization of the class II major histocompatibility complex molecule that leads to cooperative binding to a superantigen.The Journal of biological chemistry · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Mycoplasma arthritidis-derived mitogen (MAM) is a superantigen (SAg) that can activate large fractions of T cells bearing particular TCR Vbeta elements. Here we report the mutagenesis, biochemical and biophysical studies on the dimerization of MAM in solution. Our studies showed that although MAM mainly exists as a monomer in solution, a small percentage of MAM molecules form homodimer at high protein concentration, regardless of the presence of Zn2+. A distinct peak corresponding to a MAM homodimer was detected in the presence of EDTA, using both chemical cross-linking and analytical ultracentrifugation methods. Further mutagenesis studies revealed that single mutation of residues at the interface of the crystallographic dimer of MAM does not significantly affect the dimerization of MAM in solution. Circular dichroism (CD) analysis indicated that addition of Zn2+ does not induce conformational changes of MAM from its apo-state. Thermal denaturation experiments indicated that addition of Zn2+ to MAM solution resulted in a decrease of melting point (Tm), whereas addition of EDTA did not affect the Tm of MAM. These results imply that there is no defined Zn2+-binding site on MAM.
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Registered trials
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