S. Werten

发表

Identification of the Single-stranded DNA Binding Surface of the Transcriptional Coactivator PC4 by NMR*

R. Kaptein, R. Boelens, S. Werten, 1999, The Journal of Biological Chemistry.

Identification of the ssDNA-binding protein of bacteriophage T5

S. Werten, 2013, Bacteriophage.

Interaction of PC4 with melted DNA inhibits transcription

P. Gros, M. Meisterernst, H. Timmers, 1998, The EMBO journal.

Production and isotope labeling of antimicrobial peptides in Escherichia coli by means of a novel fusion partner that enables high‐yield insoluble expression and fast purification

B. Bechinger, V. Vidovic, S. Werten, 2009, Journal of peptide science : an official publication of the European Peptide Society.

Functional Analysis of the TFIID-specific Yeast TAF4 (yTAFII48) Reveals an Unexpected Organization of Its Histone-fold Domain*

C. Romier, S. Sanders, P. A. Weil, 2002, The Journal of Biological Chemistry.

Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E. coli.

D. Moras, C. Romier, S. Fribourg, 2001, Journal of molecular biology.

Membrane interactions of the amphipathic amino terminus of huntingtin.

B. Bechinger, S. Werten, M. Michalek, 2013, Biochemistry.

Structural basis of activation of the tumor suppressor protein neuroﬁbromin

T. Maier, K. Scheffzek, M. Chaker-Margot, 2022 .

Bacteriophage T5 encodes a homolog of the eukaryotic transcription coactivator PC4 implicated in recombination-dependent DNA replication.

A. Schulz, S. Werten, Birthe Steigemann, 2013, Journal of molecular biology.

A global transcription cofactor bound to juxtaposed strands of unwound DNA

D. Moras, S. Werten, 2006, Nature Structural &Molecular Biology.

High-affinity DNA binding by the C-terminal domain of the transcriptional coactivator PC4 requires simultaneous interaction with two opposing unpaired strands and results in helix destabilization.

M. Meisterernst, H. Timmers, R. van Schaik, 1998, Journal of molecular biology.

C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA binding site

P. Gros, M. Meisterernst, J. Brandsen, 1997, Nature Structural Biology.

Tetracycline repressor allostery does not depend on divalent metal recognition.

W. Hinrichs, G. Palm, S. Werten, 2014, Biochemistry.

The histone fold is a key structural motif of transcription factor TFIID.

C. Romier, I. Davidson, S. Werten, 2001, Trends in biochemical sciences.

Structure and regulatory targets of SCO3201, a highly promiscuous TetR-like regulator of Streptomyces coelicolor M145.

W. Hinrichs, S. Werten, M. Virolle, 2014, Biochemical and biophysical research communications.

Mapping the initiator binding Taf2 subunit in the structure of hydrated yeast TFIID.

P. Schultz, S. Werten, G. Papai, 2009, Structure.

Structural basis of activation of the tumor suppressor protein neurofibromin.

T. Maier, K. Scheffzek, M. Chaker-Margot, 2022, Molecular cell.

Impact of Phosphate Availability on Membrane Lipid Content of the Model Strains, Streptomyces lividans and Streptomyces coelicolor

Thierry Dulermo, S. Werten, P. Chaminade, 2021, Frontiers in Microbiology.

The Phosin PptA Plays a Negative Role in the Regulation of Antibiotic Production in Streptomyces lividans

E. Jacquet, A. Deniset-Besseau, S. Werten, 2021, Antibiotics.

Structural and biochemical analysis of a phosin from Streptomyces chartreusis reveals a combined polyphosphate‐ and metal‐binding fold

W. Hinrichs, S. Werten, M. Virolle, 2019, FEBS letters.

The induction mechanism of the flavonoid‐responsive regulator FrrA

W. Hinrichs, G. Palm, M. Göttfert, 2021, The FEBS journal.

The Human TFIID Components TAFII135 and TAFII20 and the Yeast SAGA Components ADA1 and TAFII68 Heterodimerize to Form Histone-Like Pairs

D. Moras, C. Romier, O. Poch, 2000, Molecular and Cellular Biology.

Conformational Analysis of DNA Using Genetic Algorithms

Gerrit Kateman, C. B. Lucasius, Carlos B. Lucasius, 1990, PPSN.

Modular organisation of inducer recognition and allostery in the tetracycline repressor

W. Hinrichs, J. Schneider, G. Palm, 2016, The FEBS journal.

Thermodynamics, cooperativity and stability of the tetracycline repressor (TetR) upon tetracycline binding.

W. Hinrichs, G. Palm, M. Delcea, 2020, Biochimica et biophysica acta. Proteins and proteomics.

Dimerization-Induced Allosteric Changes of the Oxyanion-Hole Loop Activate the Pseudorabies Virus Assemblin pUL26N, a Herpesvirus Serine Protease

W. Hinrichs, M. Zühlsdorf, B. Klupp, 2015, PLoS pathogens.

Crystal structures of free and ligand‐bound forms of the TetR/AcrR‐like regulator SCO3201 from Streptomyces coelicolor suggest a novel allosteric mechanism

W. Hinrichs, G. Palm, S. Werten, 2022, The FEBS journal.

Heterodimerize to Form Histone-Like Pairs 68 II Components ADA1 and TAF 20 and the Yeast SAGA II and TAF 135 II The Human TFIID Components TAF

D. Moras, O. Poch, S. Werten, 2014 .

Crystal Structure of a Subcomplex of Human Transcription Factor TFIID Formed by TATA Binding Protein-associated Factors hTAF4 (hTAFII135) and hTAF12 (hTAFII20)*

D. Moras, C. Romier, A. Mitschler, 2002, The Journal of Biological Chemistry.

Correction: Dimerization-Induced Allosteric Changes of the Oxyanion-Hole Loop Activate the Pseudorabies Virus Assemblin pUL26N, a Herpesvirus Serine Protease

W. Hinrichs, M. Zühlsdorf, B. Klupp, 2016, PLoS pathogens.

Modular organisation of inducer recognition and allostery in the tetracycline repressor.

W. Hinrichs, J. Schneider, G. Palm, 2016 .