SFB 1243 Cancer Evolution
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Helma-Smets, Jonas

Dr. Jonas Helma-Smets

BioSysM, LMU Human Biology and BioImaging and Tubulis Technologies

Contact

Mailing address:
LMU Biozentrum
Großhaderner Str. 2
82152 Planegg-Martinsried

Visitor address:
Center for Molecular Biosystems (BioSysM)
Butenandtstr. 1
81377 München-Großhadern

Phone: +49 (0)89 2180 74233

Website: Tubulis Technologies: next-gen antibody conjugates

Work group

Jonas Helma-Smets is an associated SFB 1243 member since March 2017.

Our spin-off team focuses on novel technologies for the generation of antibody conjugates in therapy (Antibody-Drug-Conjugates; ADCs) and diagnostics. In relation to the SFB, we aim to implement and translate chemical, biochemical, chemotherapeutic and antibody technologies towards biomedical application in hematological cancers. The project has emerged from an academic collaboration on site-selective protein functionalization between the groups of Professor Heinrich Leonhardt (LMU) and Professor Christian Hackenberger (FMP Berlin).

Schumacher and Helma 435x

Tubulis Technologies Team co-led by Dominik Schumacher (left) and Jonas Helma-Smets

 

Publications related to project
Schumacher D, Lemke O, Helma J, Gerszonowicz L, Waller V, Stoschek T, Durkin P, Budisa N, Leonhardt H, Keller K and Hackenberger CP (2017) Broad substrate tolerance of tubulin tyrosine ligase enables one-step site-specific enzymatic protein labeling. Chem. Sci., 2017, doi: 10.1039/C7SC00574A

Stengl A, Hörl D, Leonhardt H, Helma J. (2017) A Simple and Sensitive High-Content Assay for the Characterization of Antiproliferative Therapeutic Antibodies. SLAS Discov. 22(3):309-315. doi: 10.1177/1087057116677821

Schumacher D, Hackenberger CP, Leonhardt H, Helma J.(2016) Current Status: Site-Specific Antibody Drug Conjugates. J Clin Immunol. 36 Suppl 1:100-7. doi: 10.1007/s10875-016-0265-6

Schumacher D, Helma J, Mann FA, Pichler G, Natale F, Krause E, Cardoso MC, Hackenberger CP, Leonhardt H. (2015) Versatile and Efficient Site-Specific Protein Functionalization by Tubulin Tyrosine Ligase. Angew Chem Int Ed Engl. 54(46):13787-91. doi: 10.1002/anie.201505456