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Structural determinants of MIF functions in CXCR2-mediated inflammatory and atherogenic leukocyte recruitment.
Weber C, Kraemer S, Drechsler M, Lue H, Koenen RR, Kapurniotu A, Zernecke A, Bernhagen J. Weber C, et al. Proc Natl Acad Sci U S A. 2008 Oct 21;105(42):16278-83. doi: 10.1073/pnas.0804017105. Epub 2008 Oct 13. Proc Natl Acad Sci U S A. 2008. PMID: 18852457 Free PMC article.
Structure-function analysis demonstrated that mutation of residues R11, D44, or both preserve proper folding and the intrinsic catalytic property of MIF but severely compromises its binding to CXCR2 and abrogates MIF/CXCR2-media
Structure-function analysis demonstrated that mutation of residues R11, D44, or both preserve proper folding and the in
MIF-chemokine receptor interactions in atherogenesis are dependent on an N-loop-based 2-site binding mechanism.
Kraemer S, Lue H, Zernecke A, Kapurniotu A, Andreetto E, Frank R, Lennartz B, Weber C, Bernhagen J. Kraemer S, et al. FASEB J. 2011 Mar;25(3):894-906. doi: 10.1096/fj.10-168559. Epub 2010 Nov 24. FASEB J. 2011. PMID: 21106938
Macrophage migration inhibitory factor (MIF) is a cytokine that mediates inflammatory diseases. MIF promotes atherogenic leukocyte recruitment through a promiscuous, yet highly affine, interaction with CXCR2 and CXCR4. ...Th …
Macrophage migration inhibitory factor (MIF) is a cytokine that mediates inflammatory diseases. MIF promotes …
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