Fu X - Search Results

1

The biological activity of FasL in human and mouse lungs is determined by the structure of its stalk region.

Herrero R, Kajikawa O, Matute-Bello G, Wang Y, Hagimoto N, Mongovin S, Wong V, Park DR, Brot N, Heinecke JW, Rosen H, Goodman RB, Fu X, Martin TR. Herrero R, et al. Among authors: fu x. J Clin Invest. 2011 Mar;121(3):1174-90. doi: 10.1172/JCI43004. J Clin Invest. 2011. PMID: 21285513 Free PMC article.

2

Hypochlorous acid oxygenates the cysteine switch domain of pro-matrilysin (MMP-7). A mechanism for matrix metalloproteinase activation and atherosclerotic plaque rupture by myeloperoxidase.

Fu X, Kassim SY, Parks WC, Heinecke JW. Fu X, et al. J Biol Chem. 2001 Nov 2;276(44):41279-87. doi: 10.1074/jbc.M106958200. Epub 2001 Aug 30. J Biol Chem. 2001. PMID: 11533038 Free article.

3

Generation of intramolecular and intermolecular sulfenamides, sulfinamides, and sulfonamides by hypochlorous acid: a potential pathway for oxidative cross-linking of low-density lipoprotein by myeloperoxidase.

Fu X, Mueller DM, Heinecke JW. Fu X, et al. Biochemistry. 2002 Jan 29;41(4):1293-301. doi: 10.1021/bi015777z. Biochemistry. 2002. PMID: 11802729

4

Bcl-xL deamidation is a critical switch in the regulation of the response to DNA damage.

Deverman BE, Cook BL, Manson SR, Niederhoff RA, Langer EM, Rosová I, Kulans LA, Fu X, Weinberg JS, Heinecke JW, Roth KA, Weintraub SJ. Deverman BE, et al. Among authors: fu x. Cell. 2002 Oct 4;111(1):51-62. doi: 10.1016/s0092-8674(02)00972-8. Cell. 2002. PMID: 12372300 Free article.

5

Hypochlorous acid generated by myeloperoxidase modifies adjacent tryptophan and glycine residues in the catalytic domain of matrix metalloproteinase-7 (matrilysin): an oxidative mechanism for restraining proteolytic activity during inflammation.

Fu X, Kassim SY, Parks WC, Heinecke JW. Fu X, et al. J Biol Chem. 2003 Aug 1;278(31):28403-9. doi: 10.1074/jbc.M304739200. Epub 2003 May 20. J Biol Chem. 2003. PMID: 12759346 Free article.

6

Lysine residues direct the chlorination of tyrosines in YXXK motifs of apolipoprotein A-I when hypochlorous acid oxidizes high density lipoprotein.

Bergt C, Fu X, Huq NP, Kao J, Heinecke JW. Bergt C, et al. Among authors: fu x. J Biol Chem. 2004 Feb 27;279(9):7856-66. doi: 10.1074/jbc.M309046200. Epub 2003 Dec 3. J Biol Chem. 2004. PMID: 14660678 Free article.

7

Oxidative cross-linking of tryptophan to glycine restrains matrix metalloproteinase activity: specific structural motifs control protein oxidation.

Fu X, Kao JL, Bergt C, Kassim SY, Huq NP, d'Avignon A, Parks WC, Mecham RP, Heinecke JW. Fu X, et al. J Biol Chem. 2004 Feb 20;279(8):6209-12. doi: 10.1074/jbc.C300506200. Epub 2003 Dec 11. J Biol Chem. 2004. PMID: 14670964 Free article.

8

The myeloperoxidase product hypochlorous acid oxidizes HDL in the human artery wall and impairs ABCA1-dependent cholesterol transport.

Bergt C, Pennathur S, Fu X, Byun J, O'Brien K, McDonald TO, Singh P, Anantharamaiah GM, Chait A, Brunzell J, Geary RL, Oram JF, Heinecke JW. Bergt C, et al. Among authors: fu x. Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):13032-7. doi: 10.1073/pnas.0405292101. Epub 2004 Aug 23. Proc Natl Acad Sci U S A. 2004. PMID: 15326314 Free PMC article.

9

Tyrosine 192 in apolipoprotein A-I is the major site of nitration and chlorination by myeloperoxidase, but only chlorination markedly impairs ABCA1-dependent cholesterol transport.

Shao B, Bergt C, Fu X, Green P, Voss JC, Oda MN, Oram JF, Heinecke JW. Shao B, et al. Among authors: fu x. J Biol Chem. 2005 Feb 18;280(7):5983-93. doi: 10.1074/jbc.M411484200. Epub 2004 Nov 30. J Biol Chem. 2005. PMID: 15574409 Free article.

10

Methionine sulfoxide and proteolytic cleavage contribute to the inactivation of cathepsin G by hypochlorous acid: an oxidative mechanism for regulation of serine proteinases by myeloperoxidase.

Shao B, Belaaouaj A, Verlinde CL, Fu X, Heinecke JW. Shao B, et al. Among authors: fu x. J Biol Chem. 2005 Aug 12;280(32):29311-21. doi: 10.1074/jbc.M504040200. Epub 2005 Jun 20. J Biol Chem. 2005. PMID: 15967795 Free article.

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