Dr. Silke Hoffmann

Kompetenzbereiche

Molekularbiologie, Zellbiologie, rekombinante Proteinexpression, Proteinreinigung, Interaktionsstudien, Mikroskopie

Kontakt

+49 2461/61-9389

+49 2461/61-2023

E-Mail

ORCID: 0000-0003-1414-8957

ResearcherID: H-5059-2013

Adresse

Forschungszentrum Jülich GmbH
Wilhelm-Johnen-Straße
52428 Jülich

Institut für Biologische Informationsprozesse (IBI)

Strukturbiochemie (IBI-7)

Gebäude 05.8v / Raum 3018

Vita

1989 – 1994: Study of Biology at University Bayreuth, Germany (Dipl.-Biol.)

1995 – 1998: PhD in Biology (Insitute of Structure and Chemistry of Biopolymers/ Prof. P. Rösch) at University Bayreuth (Dr. rer. Nat.)

1997: Research project at the Sackler School of Medicine (Prof. A. Yaniv and Prof. A. Gazit) at Tel Aviv University, Israel

1998 – 2001: Research Assistant (C1), Institute of Biopolymers, University of Bayreuth, Germany

2002 – 2008: Postdoctoral fellow, Institute of Physical Biology, Heinrich Heine University Düsseldorf and Institut für Molekulare Biophysik II (INB-2), Forschungszentrum Jülich, Germany

since 2008: Research group leader (Topics: “Host-Virus-Interaction” and "Atg8-protein biology”) at Structural Biochemistry (IBI-7), Forschungszentrum Jülich, Germany

Miscellaneous: Activities in the Collaborative Research Centers 575, 974, 1208. Trained according to §15 GenTSV. Worked as a representative for biological safety. Peer reviewer activities. Teaching (internships, exercises, seminars). Supervision of students (Bc./M.Sc., PhD thesis). Active in the IBI-7 subinstitute advisory committee. Mental health first aider (MHFA).

Publikationen

GABARAP interacts with EGFR - supporting the unique role of this hAtg8 protein during receptor trafficking. Üffing A, Weiergräber OH, Schwarten M, Hoffmann S, Willbold D. FEBS Lett. 2024 doi: 10.1002/1873-3468.14997.

Highlighting the hidden: monitoring the avidity-driven association of a fluorescent GABARAP tandem with microtubules in living cells. Üffing A, Gold L, Gensch T, Weiergräber OH, Hoffmann S, Willbold D. Autophagy Reports 3:1 2024. doi: 10.1080/27694127.2024.2348899

Lack of GABARAP-Type Proteins Is Accompanied by Altered Golgi Morphology and Surfaceome Composition. Sanwald JL, Dobner J, Simons IM, Poschmann G, Stühler K, Üffing A, Hoffmann S, Willbold D. Int J Mol Sci. 2020 22(1):85. doi: 10.3390/ijms22010085.

The GABARAP Co-Secretome Identified by APEX2-GABARAP Proximity Labelling of Extracellular Vesicles. Sanwald JL, Poschmann G, Stühler K, Behrends C, Hoffmann S, Willbold D. Cells. 2020 Jun 16;9(6):1468. doi: 10.3390/cells9061468.

Deficiency of GABARAP but not its Paralogs Causes Enhanced EGF-induced EGFR Degradation. Dobner J, Simons IM, Rufinatscha K, Hänsch S, Schwarten M, Weiergräber OH, Abdollahzadeh I, Gensch T, Bode JG, Hoffmann S, Willbold D. Cells. 2020 May 22;9(5):1296. doi: 10.3390/cells9051296.

Autophagy-Related Proteins GABARAP and LC3B Label Structures of Similar Size but Different Shape in Super-Resolution Imaging. Abdollahzadeh I, Hendriks J, Sanwald JL, Simons IM, Hoffmann S, Weiergräber OH, Willbold D, Gensch T. Molecules. 2019 May 13;24(9):1833. doi: 10.3390/molecules24091833.

Phosphorylated tyrosine 93 of hepatitis C virus nonstructural protein 5A is essential for interaction with host c-Src and efficient viral replication. Klinker S, Stindt S, Gremer L, Bode JG, Gertzen CGW, Gohlke H, Weiergräber OH, Hoffmann S, Willbold D. J Biol Chem. 2019 May 3;294(18):7388-7402. doi: 10.1074/jbc.RA119.007656.

The highly GABARAP specific rat monoclonal antibody 8H5 visualizes GABARAP in immunofluorescence imaging at endogenous levels. Simons IM, Mohrlüder J, Feederle R, Kremmer E, Zobel T, Dobner J, Bleffert N, Hoffmann S, Willbold D. Sci Rep. 2019 Jan 24;9(1):526. doi: 10.1038/s41598-018-36717-1.

Direct binding to GABARAP family members is essential for HIV-1 Nef plasma membrane localization. Boeske A, Schwarten M, Ma P, Tusche M, Mötter J, Möller C, Neudecker P, Hoffmann S, Willbold D. Sci Rep. 2017 Jul 20;7(1):5979. doi: 10.1038/s41598-017-06319-4.

Amino Terminal Region of Dengue Virus NS4A Cytosolic Domain Binds to Highly Curved Liposomes. Hung YF, Schwarten M, Hoffmann S, Willbold D, Sklan EH, Koenig B. Viruses. 2015 Jul 21;7(7):4119-30. doi: 10.3390/v7072812.

Dengue virus NS4A cytoplasmic domain binding to liposomes is sensitive to membrane curvature. Hung YF, Schwarten M, Schünke S, Thiagarajan-Rosenkranz P, Hoffmann S, Sklan EH, Willbold D, Koenig BW. Biochim Biophys Acta. 2015 May;1848(5):1119-26. doi: 10.1016/j.bbamem.2015.01.015.

Hepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro. Aladag A, Hoffmann S, Stoldt M, Bösing C, Willbold D, Schwarten M. J Pept Sci. 2014 May;20(5):334-40. doi: 10.1002/psc.2618.

Recombinant production of the amino terminal cytoplasmic region of dengue virus non-structural protein 4A for structural studies. Hung YF, Valdau O, Schünke S, Stern O, Koenig BW, Willbold D, Hoffmann S. PLoS One. 2014 Jan 23;9(1):e86482. doi: 10.1371/journal.pone.0086482.

Interaction of Bcl-2 with the autophagy-related GABAA receptor-associated protein (GABARAP): biophysical characterization and functional implications. Ma P, Schwarten M, Schneider L, Boeske A, Henke N, Lisak D, Weber S, Mohrlüder J, Stoldt M, Strodel B, Methner A, Hoffmann S, Weiergräber OH, Willbold D. J Biol Chem. 2013 Dec 27;288(52):37204-15. doi: 10.1074/jbc.M113.528067.

Interaction of nonstructural protein 5A of the hepatitis C virus with Src homology 3 domains using noncanonical binding sites. Schwarten M, Sólyom Z, Feuerstein S, Aladağ A, Hoffmann S, Willbold D, Brutscher B. Biochemistry. 2013 Sep 10;52(36):6160-8. doi: 10.1021/bi400363v.

An N-terminal amphipathic helix in dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication. Stern O, Hung YF, Valdau O, Yaffe Y, Harris E, Hoffmann S, Willbold D, Sklan EH. J Virol. 2013 Apr;87(7):4080-5. doi: 10.1128/JVI.01900-12. Epub 2013 Jan 16.

Brain transcriptome-wide screen for HIV-1 Nef protein interaction partners reveals various membrane-associated proteins. Kammula EC, Mötter J, Gorgels A, Jonas E, Hoffmann S, Willbold D. PLoS One. 2012;7(12):e51578. doi: 10.1371/journal.pone.0051578.

Transient structure and SH3 interaction sites in an intrinsically disordered fragment of the hepatitis C virus protein NS5A. Feuerstein S, Solyom Z, Aladag A, Favier A, Schwarten M, Hoffmann S, Willbold D, Brutscher B. J Mol Biol. 2012 Jul 20;420(4-5):310-23. doi: 10.1016/j.jmb.2012.04.023.

1H, 13C, and 15N resonance assignment of a 179 residue fragment of hepatitis C virus non-structural protein 5A. Feuerstein S, Solyom Z, Aladağ A, Hoffmann S, Willbold D, Brutscher B. Biomol NMR Assign. 2011 Oct;5(2):241-3. doi: 10.1007/s12104-011-9309-2.

Single vector system for efficient N-myristoylation of recombinant proteins in E. coli. Glück JM, Hoffmann S, Koenig BW, Willbold D. PLoS One. 2010 Apr 9;5(4):e10081. doi: 10.1371/journal.pone.0010081.

Competitively selected protein ligands pay their increase in specificity by a decrease in affinity. Hoffmann S, Funke SA, Wiesehan K, Moedder S, Glück JM, Feuerstein S, Gerdts M, Mötter J, Willbold D. Mol Biosyst. 2010 Jan;6(1):126-33. doi: 10.1039/b910945e.

Structural studies of the phosphatidylinositol 3-kinase (PI3K) SH3 domain in complex with a peptide ligand: role of the anchor residue in ligand binding. Batra-Safferling R, Granzin J, Mödder S, Hoffmann S, Willbold D. Biol Chem. 2010 Jan;391(1):33-42. doi: 10.1515/BC.2010.003.

Integral membrane proteins in nanodiscs can be studied by solution NMR spectroscopy. Glück JM, Wittlich M, Feuerstein S, Hoffmann S, Willbold D, Koenig BW. J Am Chem Soc. 2009 Sep 2;131(34):12060-1. doi: 10.1021/ja904897p.

Structural characterization of the transmembrane and cytoplasmic domains of human CD4. Wittlich M, Koenig BW, Hoffmann S, Willbold D. Biochim Biophys Acta. 2007 Dec;1768(12):2949-60. doi: 10.1016/j.bbamem.2007.10.023.

Competitive displacement of full-length HIV-1 Nef from the Hck SH3 domain by a high-affinity artificial peptide. Stangler T, Tran T, Hoffmann S, Schmidt H, Jonas E, Willbold D. Biol Chem. 2007 Jun;388(6):611-5. doi: 10.1515/BC.2007.075.

Nef protein of human immunodeficiency virus type 1 binds its own myristoylated N-terminus. Hoffmann S, Jonas E, König S, Preusser-Kunze A, Willbold D. Biol Chem. 2007 Feb;388(2):181-3. doi: 10.1515/BC.2007.020.

Solution structure of a Hck SH3 domain ligand complex reveals novel interaction modes. Schmidt H, Hoffmann S, Tran T, Stoldt M, Stangler T, Wiesehan K, Willbold D. J Mol Biol. 2007 Feb 2;365(5):1517-32. doi: 10.1016/j.jmb.2006.11.013.

Insights into human Lck SH3 domain binding specificity: different binding modes of artificial and native ligands. Tran T, Hoffmann S, Wiesehan K, Jonas E, Luge C, Aladag A, Willbold D. Biochemistry. 2005 Nov 15;44(45):15042-52. doi: 10.1021/bi051403k.

Binding, domain orientation, and dynamics of the Lck SH3-SH2 domain pair and comparison with other Src-family kinases. Hofmann G, Schweimer K, Kiessling A, Hofinger E, Bauer F, Hoffmann S, Rösch P, Campbell ID, Werner JM, Sticht H. Biochemistry. 2005 Oct 4;44(39):13043-50. doi: 10.1021/bi050814y.

Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity. Bauer F, Schweimer K, Meiselbach H, Hoffmann S, Rösch P, Sticht H. Protein Sci. 2005 Oct;14(10):2487-98. doi: 10.1110/ps.051563605.

Characterization of Lck-binding elements in the herpesviral regulatory Tip protein. Bauer F, Hofinger E, Hoffmann S, Rösch P, Schweimer K, Sticht H. Biochemistry. 2004 Nov 30;43(47):14932-9. doi: 10.1021/bi0485068.

Sequence-specific 1H, 13C and 15N resonance assignments of the SH3-SH2 domain pair from the human tyrosine kinase Lck. Schweimer K, Kiessling A, Bauer F, Hör S, Hoffmann S, Rösch P, Sticht H. J Biomol NMR. 2003 Dec;27(4):405-6. doi: 10.1023/a:1025861326222.

Structural investigation of the binding of a herpesviral protein to the SH3 domain of tyrosine kinase Lck. Schweimer K, Hoffmann S, Bauer F, Friedrich U, Kardinal C, Feller SM, Biesinger B, Sticht H. Biochemistry. 2002 Apr 23;41(16):5120-30. doi: 10.1021/bi015986j. Binding of phage-displayed HIV-1 Tat to TAR RNA in the presence of cyclin T1. Jonas G, Hoffmann S, Willbold D. J Biomed Sci. 2001 Sep;8(5):430-6. doi: 10.1007/BF02255953.

Sequence-specific 1H, 13C and 15N resonance assignments of lymphocyte specific kinase unique and SH3 domains. Briese L, Hoffmann S, Friedrich U, Biesinger B, Willbold D. J Biomol NMR. 2001 Feb;19(2):193-4. doi: 10.1023/a:1008389229587.

Solution structure of a zinc substituted eukaryotic rubredoxin from the cryptomonad alga Guillardia theta. Schweimer K, Hoffmann S, Wastl J, Maier UG, Rösch P, Sticht H. Protein Sci. 2000 Aug;9(8):1474-86. doi: 10.1110/ps.9.8.1474.

Eukaryotically encoded and chloroplast-located rubredoxin is associated with photosystem II. Wastl J, Duin EC, Iuzzolino L, Dörner W, Link T, Hoffmann S, Sticht H, Dau H, Lingelbach K, Maier UG. J Biol Chem. 2000 Sep 29;275(39):30058-63. doi: 10.1074/jbc.M004629200.

Identification and characterization of a eukaryotically encoded rubredoxin in a cryptomonad alga. Wastl J, Sticht H, Maier UG, Rösch P, Hoffmann S. FEBS Lett. 2000 Apr 14;471(2-3):191-6. doi: 10.1016/s0014-5793(00)01399-5.

Antitermination in bacteriophage lambda. The structure of the N36 peptide-boxB RNA complex. Schärpf M, Sticht H, Schweimer K, Boehm M, Hoffmann S, Rösch P. Eur J Biochem. 2000 Apr;267(8):2397-408. doi: 10.1046/j.1432-1327.2000.01251.x.

The interaction of HIV-1 Tat(32-72) with its target RNA: a fluorescence and nuclear magnetic resonance study. Metzger AU, Bayer P, Willbold D, Hoffmann S, Frank RW, Goody RS, Rösch P. Biochem Biophys Res Commun. 1997 Dec 8;241(1):31-6. doi: 10.1006/bbrc.1997.7770.

A selection system to study protein-RNA interactions: functional display of HIV-1 Tat protein on filamentous bacteriophage M13. Hoffmann S, Willbold D. Biochem Biophys Res Commun. 1997 Jun 27;235(3):806-11. doi: 10.1006/bbrc.1997.6879.

Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution. Willbold D, Hoffmann S, Rösch P. Eur J Biochem. 1997 May 1;245(3):581-8. doi:10.1111/.1432-1033.1997.t01-1-00581.

Letzte Änderung: 29.10.2024