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pubmed-article:9645476pubmed:abstractTextNatural resistance-associated macrophage protein 1 (NRAMP1) is a putative membrane protein that dominates natural resistance to infection. An NRAMP1-glutathione S-transferase fusion protein was used to test the ability of the NRAMP1 NH2-terminal domain to bind to taxol-stabilized microtubules. Co-sedimentation analysis showed that the fusion protein binds to microtubules. Although the NH2-terminal domain of the NRAMP1 molecule has structural homology with the Pro-rich region of microtubule-associated protein 4 (MAP4), the presence of the MAP4 microtubule-binding domain fragment had little effect on the binding of the fusion protein to microtubules.lld:pubmed
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pubmed-article:9645476pubmed:articleTitleHuman natural resistance-associated macrophage protein is a new type of microtubule-associated protein.lld:pubmed
pubmed-article:9645476pubmed:affiliationDepartment of Biochemical Engineering and Science, Faculty of Computer Science and Systems Engineering, Kyushu Institute of Technology, Fukuoka, Japan. dc9603@bse.kyutech.ac.jplld:pubmed
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