Grötzinger J - Search Results

1

CD9 Controls Integrin α5β1-Mediated Cell Adhesion by Modulating Its Association With the Metalloproteinase ADAM17.

Machado-Pineda Y, Cardeñes B, Reyes R, López-Martín S, Toribio V, Sánchez-Organero P, Suarez H, Grötzinger J, Lorenzen I, Yáñez-Mó M, Cabañas C. Machado-Pineda Y, et al. Among authors: grotzinger j. Front Immunol. 2018 Nov 5;9:2474. doi: 10.3389/fimmu.2018.02474. eCollection 2018. Front Immunol. 2018. PMID: 30455686 Free PMC article.

2

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

Lorenzen I, Trad A, Grötzinger J. Lorenzen I, et al. Among authors: grotzinger j. Biochem Biophys Res Commun. 2011 Nov 18;415(2):330-6. doi: 10.1016/j.bbrc.2011.10.056. Epub 2011 Oct 18. Biochem Biophys Res Commun. 2011. PMID: 22033402

3

Molecular insights into the multilayered regulation of ADAM17: The role of the extracellular region.

Grötzinger J, Lorenzen I, Düsterhöft S. Grötzinger J, et al. Biochim Biophys Acta Mol Cell Res. 2017 Nov;1864(11 Pt B):2088-2095. doi: 10.1016/j.bbamcr.2017.05.024. Epub 2017 May 29. Biochim Biophys Acta Mol Cell Res. 2017. PMID: 28571693 Free article. Review.

4

A novel bispecific single-chain antibody for ADAM17 and CD3 induces T-cell-mediated lysis of prostate cancer cells.

Yamamoto K, Trad A, Baumgart A, Hüske L, Lorenzen I, Chalaris A, Grötzinger J, Dechow T, Scheller J, Rose-John S. Yamamoto K, et al. Among authors: grotzinger j. Biochem J. 2012 Jul 1;445(1):135-44. doi: 10.1042/BJ20120433. Biochem J. 2012. PMID: 22509934

5

ADAM17-overexpressing breast cancer cells selectively targeted by antibody-toxin conjugates.

Trad A, Hansen HP, Shomali M, Peipp M, Klausz K, Hedemann N, Yamamoto K, Mauermann A, Desel C, Lorenzen I, Lemke H, Rose-John S, Grötzinger J. Trad A, et al. Among authors: grotzinger j. Cancer Immunol Immunother. 2013 Mar;62(3):411-21. doi: 10.1007/s00262-012-1346-x. Epub 2012 Sep 1. Cancer Immunol Immunother. 2013. PMID: 22940887 Free PMC article.

6

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

Trad A, Riese M, Shomali M, Hedeman N, Effenberger T, Grötzinger J, Lorenzen I. Trad A, et al. Among authors: grotzinger j. Int J Oncol. 2013 May;42(5):1793-800. doi: 10.3892/ijo.2013.1864. Epub 2013 Mar 26. Int J Oncol. 2013. PMID: 23545805

7

The membrane-proximal domain of A Disintegrin and Metalloprotease 17 (ADAM17) is responsible for recognition of the interleukin-6 receptor and interleukin-1 receptor II.

Lorenzen I, Lokau J, Düsterhöft S, Trad A, Garbers C, Scheller J, Rose-John S, Grötzinger J. Lorenzen I, et al. Among authors: grotzinger j. FEBS Lett. 2012 Apr 24;586(8):1093-100. doi: 10.1016/j.febslet.2012.03.012. Epub 2012 Mar 21. FEBS Lett. 2012. PMID: 22575642 Free article.

8

Development of sandwich ELISA for detection and quantification of human and murine a disintegrin and metalloproteinase17.

Trad A, Hedemann N, Shomali M, Pawlak V, Grötzinger J, Lorenzen I. Trad A, et al. Among authors: grotzinger j. J Immunol Methods. 2011 Aug 31;371(1-2):91-6. doi: 10.1016/j.jim.2011.06.015. Epub 2011 Jun 24. J Immunol Methods. 2011. PMID: 21726562

9

Redundancy of protein disulfide isomerases in the catalysis of the inactivating disulfide switch in A Disintegrin and Metalloprotease 17.

Krossa S, Scheidig AJ, Grötzinger J, Lorenzen I. Krossa S, et al. Among authors: grotzinger j. Sci Rep. 2018 Jan 18;8(1):1103. doi: 10.1038/s41598-018-19429-4. Sci Rep. 2018. PMID: 29348576 Free PMC article.

10

KDEL Receptor 1 Contributes to Cell Surface Association of Protein Disulfide Isomerases.

Bartels AK, Göttert S, Desel C, Schäfer M, Krossa S, Scheidig AJ, Grötzinger J, Lorenzen I. Bartels AK, et al. Among authors: grotzinger j. Cell Physiol Biochem. 2019;52(4):850-868. doi: 10.33594/000000059. Cell Physiol Biochem. 2019. PMID: 30958660 Free article.

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