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Glycosylation of a disintegrin and metalloprotease 17 affects its activity and inhibition.

Chavaroche A, Cudic M, Giulianotti M, Houghten RA, Fields GB, Minond D.

Anal Biochem. 2014 Mar 15;449:68-75. doi: 10.1016/j.ab.2013.12.018. Epub 2013 Dec 19.


Discovery of novel inhibitors of a disintegrin and metalloprotease 17 (ADAM17) using glycosylated and non-glycosylated substrates.

Minond D, Cudic M, Bionda N, Giulianotti M, Maida L, Houghten RA, Fields GB.

J Biol Chem. 2012 Oct 19;287(43):36473-87. doi: 10.1074/jbc.M112.389114. Epub 2012 Aug 27.


Activity of ADAM17 (a disintegrin and metalloprotease 17) is regulated by its noncatalytic domains and secondary structure of its substrates.

Stawikowska R, Cudic M, Giulianotti M, Houghten RA, Fields GB, Minond D.

J Biol Chem. 2013 Aug 2;288(31):22871-9. doi: 10.1074/jbc.M113.462267. Epub 2013 Jun 18.


Secreted Frizzled-related protein 3 (sFRP3)-mediated suppression of interleukin-6 receptor release by A disintegrin and metalloprotease 17 (ADAM17) is abrogated in the osteoarthritis-associated rare double variant of sFRP3.

Oldefest M, Düsterhöft S, Desel C, Thysen S, Fink C, Rabe B, Lories R, Grötzinger J, Lorenzen I.

Biochem J. 2015 Jun 15;468(3):507-18. doi: 10.1042/BJ20141231. Epub 2015 Apr 7.


SAR Studies of Exosite-Binding Substrate-Selective Inhibitors of A Disintegrin And Metalloprotease 17 (ADAM17) and Application as Selective in Vitro Probes.

Knapinska AM, Dreymuller D, Ludwig A, Smith L, Golubkov V, Sohail A, Fridman R, Giulianotti M, LaVoi TM, Houghten RA, Fields GB, Minond D.

J Med Chem. 2015 Aug 13;58(15):5808-24. doi: 10.1021/acs.jmedchem.5b00354. Epub 2015 Aug 4.


Identification of novel interaction between ADAM17 (a disintegrin and metalloprotease 17) and thioredoxin-1.

Aragão AZ, Nogueira ML, Granato DC, Simabuco FM, Honorato RV, Hoffman Z, Yokoo S, Laurindo FR, Squina FM, Zeri AC, Oliveira PS, Sherman NE, Paes Leme AF.

J Biol Chem. 2012 Dec 14;287(51):43071-82. doi: 10.1074/jbc.M112.364513. Epub 2012 Oct 26.


Multimerisation of A disintegrin and metalloprotease protein-17 (ADAM17) is mediated by its EGF-like domain.

Lorenzen I, Trad A, Grötzinger J.

Biochem Biophys Res Commun. 2011 Nov 18;415(2):330-6. doi: 10.1016/j.bbrc.2011.10.056. Epub 2011 Oct 18.


A transforming Src mutant increases the bioavailability of EGFR ligands via stimulation of the cell-surface metalloproteinase ADAM17.

Maretzky T, Zhou W, Huang XY, Blobel CP.

Oncogene. 2011 Feb 3;30(5):611-8. doi: 10.1038/onc.2010.443. Epub 2010 Sep 27.


The disintegrin domain of ADAM17 antagonises fibroblast‑carcinoma cell interactions.

Trad A, Riese M, Shomali M, Hedeman N, Effenberger T, Grötzinger J, Lorenzen I.

Int J Oncol. 2013 May;42(5):1793-800. doi: 10.3892/ijo.2013.1864. Epub 2013 Mar 26.


A disintegrin and metalloprotease 17 dynamic interaction sequence, the sweet tooth for the human interleukin 6 receptor.

Düsterhöft S, Höbel K, Oldefest M, Lokau J, Waetzig GH, Chalaris A, Garbers C, Scheller J, Rose-John S, Lorenzen I, Grötzinger J.

J Biol Chem. 2014 Jun 6;289(23):16336-48. doi: 10.1074/jbc.M114.557322. Epub 2014 Apr 30.


Polo-like kinase 2, a novel ADAM17 signaling component, regulates tumor necrosis factor α ectodomain shedding.

Schwarz J, Schmidt S, Will O, Koudelka T, Köhler K, Boss M, Rabe B, Tholey A, Scheller J, Schmidt-Arras D, Schwake M, Rose-John S, Chalaris A.

J Biol Chem. 2014 Jan 31;289(5):3080-93. doi: 10.1074/jbc.M113.536847. Epub 2013 Dec 13.


The ALCAM shedding by the metalloprotease ADAM17/TACE is involved in motility of ovarian carcinoma cells.

Rosso O, Piazza T, Bongarzone I, Rossello A, Mezzanzanica D, Canevari S, Orengo AM, Puppo A, Ferrini S, Fabbi M.

Mol Cancer Res. 2007 Dec;5(12):1246-53. doi: 10.1158/1541-7786.MCR-07-0060.


Expression and protein chemistry yielding crystallization of the catalytic domain of ADAM17 complexed with a hydroxamate inhibitor.

Hoth LR, Tan DH, Wang IK, Wengender PA, Thompson MA, Kamath AV, Geoghegan KF.

Protein Expr Purif. 2007 Apr;52(2):313-9. Epub 2006 Nov 7.


ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity.

Lund J, Olsen OH, Sørensen ES, Stennicke HR, Petersen HH, Overgaard MT.

J Biol Chem. 2013 Jul 19;288(29):21367-75. doi: 10.1074/jbc.M113.474536. Epub 2013 Jun 10.


Modulation of CD163 expression by metalloprotease ADAM17 regulates porcine reproductive and respiratory syndrome virus entry.

Guo L, Niu J, Yu H, Gu W, Li R, Luo X, Huang M, Tian Z, Feng L, Wang Y.

J Virol. 2014 Sep;88(18):10448-58. doi: 10.1128/JVI.01117-14. Epub 2014 Jun 25. Erratum in: J Virol. 2016 Jun 1;90(11):5532.


Regulation of mature ADAM17 by redox agents for L-selectin shedding.

Wang Y, Herrera AH, Li Y, Belani KK, Walcheck B.

J Immunol. 2009 Feb 15;182(4):2449-57. doi: 10.4049/jimmunol.0802770.


Regulated ADAM17-dependent EGF family ligand release by substrate-selecting signaling pathways.

Dang M, Armbruster N, Miller MA, Cermeno E, Hartmann M, Bell GW, Root DE, Lauffenburger DA, Lodish HF, Herrlich A.

Proc Natl Acad Sci U S A. 2013 Jun 11;110(24):9776-81. doi: 10.1073/pnas.1307478110. Epub 2013 May 29.


M1 and M3 muscarinic receptors control physiological processing of cellular prion by modulating ADAM17 phosphorylation and activity.

Alfa Cissé M, Sunyach C, Slack BE, Fisher A, Vincent B, Checler F.

J Neurosci. 2007 Apr 11;27(15):4083-92.


Catalytic properties of ADAM12 and its domain deletion mutants.

Jacobsen J, Visse R, Sørensen HP, Enghild JJ, Brew K, Wewer UM, Nagase H.

Biochemistry. 2008 Jan 15;47(2):537-47. Epub 2007 Dec 15.


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