Skip to content. Skip to navigation
Max Planck Institute for Developmental Biology
You are here: Home → Research Groups → Birte Höcker → staff → Birte Höcker
home
MPS Links
 
Document Actions

Birte Höcker

Group Leader


Birte.jpgHöcker Group (Protein Design)



MPI for Developmental Biology, Spemannstr. 35, 72076 Tübingen, Germany

Tel: +49 7071 601 322
Fax: +49 7071 601 305
E-Mail: Birte.Hoecker [AT] Tuebingen [DOT] MPG [DOT] de



Biography


  • PhD 2003 Biochemistry, Universität zu Köln, Germany
  • 2003-2005 Postdoctoral Fellow at Duke University Medical Center, USA
  • since 2006 Group leader at MPI for Developmental Biology, Germany


Publications


Malisi, C., Stiel, A.C. & Höcker, B. (2011) Enzyme am Reißbrett. BIOspektrum 7, 736-8. [BIOspektrum]

Schreier, B. & Höcker, B. (2010) Engineering the enolase magnesium II binding site: implications for its evolution. Biochem 49, 7582-9. [PubMed]

Eisenbeis, S. & Höcker, B. (2010) Evolutionary mechanism as a template for protein engineering. J Pep Sci 16, 538-44. [PubMed]

Höcker, B. (2010) Metals make proteins stick. Chem Biol 17, 103-4. [PubMed] - Preview on Salgado et al. (2010): Metal templated design of protein interfaces.

Höcker, B. Mechanismen der Evolution als Matrize für Protein Engineering (Forschungsbericht 2010 - MPI für Entwicklungsbiologie) [MPG website]

Schreier, B., Stumpp, C., Wiesner, S. & Höcker, B. (2009) Computational design of ligand binding is not a solved problem. Proc Natl Acad Sci U S A 106, 18491-6. [PubMed]     -Media coverage on this paper: "Protein design papers challenged" in Nature News & "Designed proteins debunked?" in The Scientist   f1000

Malisi, C., Kohlbacher, O. & Höcker, B. (2009) Automated scaffold selection for enzyme design. Proteins 77, 74-83. [PubMed]

Claren, J., Malisi, C., Höcker, B. & Sterner, R. (2009) Establishing wild-type levels of catalytic activity on natural and artificial (βα)8-barrel protein scaffolds. Proc Natl Acad Sci U S A 106, 3704-9. [PubMed]   f1000

Höcker, B., Lochner, A., Seitz, T., Claren, J. & Sterner, R. (2009) High-resolution crystal structure of an artificial (βα)8-barrel protein designed from identical half-barrels. Biochemistry 48, 1145-1147. [PubMed]

Höcker, B. Chapter 8: Structural frameworks suitable for engineering. In Protein Engineering Handbook. Eds. S.Lutz & U.T.Bornscheuer. Wiley-VCH 2008.

Bharat, T.A.M., Eisenbeis, S., Zeth, K. & Höcker, B. (2008) A βα-barrel built by the combination of fragments from different folds. Proc Natl Acad Sci U S A 105, 9942-7. [PubMed]   f1000

Höcker, B. (2008). Proteindesign und -engineering. Trendbericht in Biochemie und Molekularbiologie. Nachrichten aus der Chemie 56/3, 298-301. [GDCh]

Reetz, M.T., Rentzsch, M., Pletsch, A., Taglieber, A., Hollmann, F., Mondiere, R.J.G., Dickmann, N., Höcker, B., Cerrone, S., Haeger, M.C. & Sterner, R. (2008) A robust protein host for anchoring chelating ligands and organocatalysts. ChemBioChem 9, 552-64. [PubMed]

Tian, Y., Cuneo, M.J., Changela, A., Höcker, B., Beese, L.S. & Hellinga, H.W. (2007). Structure-based design of robust glucose biosensors using a Thermotoga maritima periplasmic glucose-binding protein. Protein Sci 16, 2240-50. [PubMed]

Sterner, R. & Höcker, B. (2005). Catalytic versatility, stability, and evolution of the (βα)8-barrel enzyme fold. Chem Rev 105, 4038-55. [PubMed]

Höcker, B. (2005). Directed evolution of (βα)8-barrel enzymes. Biomol Eng 22, 31-8. [PubMed]

Höcker, B., Claren, J. & Sterner, R. (2004). Mimicking enzyme evolution by generating new (βα)8-barrels from (βα)4-half-barrels. Proc Natl Acad Sci U S A 101, 16448-53. [PubMed]     f1000

Raasch, C., Armbrecht, M., Streit, W., Höcker, B., Strater, N. & Liebl, W. (2002). Identification of residues important for NAD+ binding by the Thermotoga maritima α-glucosidase AglA, a member of glycoside hydrolase family 4. FEBS Lett 517, 267-71. [PubMed]

Höcker, B., Schmidt, S. & Sterner, R. (2002). A common evolutionary origin of two elementary enzyme folds. FEBS Lett 510, 133-5. [PubMed]

Höcker, B., Jürgens, C., Wilmanns, M. & Sterner, R. (2001). Stability, catalytic versatility and evolution of the (βα)8-barrel fold. Curr Opin Biotechnol 12, 376-81. [PubMed]

Höcker, B., Beismann-Driemeyer, S., Hettwer, S., Lustig, A. & Sterner, R. (2001). Dissection of a (βα)8-barrel enzyme into two folded halves. Nat Struct Biol 8, 32-6. [PubMed]

Henn-Sax, M., Höcker, B., Wilmanns, M. & Sterner, R. (2001). Divergent evolution of (βα)8-barrel enzymes. Biol Chem 382, 1315-20. [PubMed]

Whiteway, J., Koziarz, P., Veall, J., Sanhu, N., Kumar, P., Höcker, B. & Lambert, I.B. (1998). Oxygen-insensitive nitroreductases: analysis of the roles of nfsA and nfsB in development of resistance to 5-nitrofuran derivatives in Escherichia coli. J Bacteriol, 180, 5529-39. [PubMed]

 

Awards and Funding


2007-2010 DFG research grant: Evolutionary relationship of two elementary protein folds

2010-2013 DFG research grant: Computational tools for the design of ligand binding in proteins

2010          Biologie Preis der Akademie der Wissenschaften zu Göttingen [link]

2011-2014 DFG research grant: Evolutionary relationship of two elementary protein folds (follow-up)

top
last modified 2011-11-23