His scientific interests lie mostly in Protein structure, Cell biology, Stereochemistry, Biochemistry and Genetics. His work carried out in the field of Protein structure brings together such families of science as Plasma protein binding, Biophysics, DNA, Peptide sequence and Binding site. Christoph W. Müller focuses mostly in the field of DNA, narrowing it down to matters related to HMG-box and, in some cases, B3 domain, Rel homology domain, Methyl-CpG-binding domain and DNA-binding domain.
The concepts of his Cell biology study are interwoven with issues in Gene and Zinc finger. His biological study spans a wide range of topics, including Nucleus, Beta Karyopherins and Adenylate kinase, Enzyme. In general Genetics study, his work on Histone H2A monoubiquitination, Histone H3 and Sequence analysis often relates to the realm of Histone methylation and Armadillo repeats, thereby connecting several areas of interest.
Cell biology, Genetics, RNA polymerase III, Molecular biology and Biochemistry are his primary areas of study. His Cell biology research includes themes of Transcription factor, Chromatin, Histone, Transcription and Binding site. His Binding site research integrates issues from Psychological repression, DNA, Active site, Winged Helix and Protein structure.
His DNA study incorporates themes from HMG-box, Stereochemistry and Eukaryotic transcription. His studies in Protein structure integrate themes in fields like Biophysics, Peptide sequence and Computational biology. DNA-binding domain and Protein biosynthesis are the primary areas of interest in his Genetics study.
His primary areas of investigation include Cell biology, RNA polymerase III, Transcription, Protein subunit and Binding site. Christoph W. Müller combines subjects such as BAP1, Ubiquitin, Psychological repression, Transcription factor and Protein structure with his study of Cell biology. His Protein structure research incorporates elements of Signal transduction and Leucine zipper.
As part of the same scientific family, he usually focuses on RNA polymerase III, concentrating on RNA polymerase II and intersecting with Chromatin and Fungal genetics. His Transcription study integrates concerns from other disciplines, such as RNA, Gene expression and DNA. Christoph W. Müller has included themes like Plasma protein binding, Saccharomyces cerevisiae and Active site in his Binding site study.
Christoph W. Müller focuses on Cell biology, Transfer RNA, RNA polymerase II, Structural biology and Genetics. His work in the fields of Nuclear pore overlaps with other areas such as Insulin analog. Christoph W. Müller combines subjects such as Translation elongation, Protein subunit and Protein biosynthesis with his study of Transfer RNA.
His RNA polymerase II research integrates issues from Cell, Proteome, Biophysics, Proteomics and Mitosis. His Structural biology research is multidisciplinary, relying on both Protein structure, Biogenesis, Nucleoporin and Saccharomyces cerevisiae. In his research, he performs multidisciplinary study on Genetics and Exon skipping.
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Three-dimensional structure of the Stat3β homodimer bound to DNA
Stefan Becker;Bernd Groner;Christoph W. Müller.
Structure of importin-beta bound to the IBB domain of importin-alpha.
Gino Cingolani;Carlo Petosa;Karsten Weis;Christoph W. Müller.
Structure of the NF-kappa B p50 homodimer bound to DNA.
Christoph W. Müller;Félix A. Rey;Mikiko Sodeoka;Mikiko Sodeoka;Gregory L. Verdine.
Comparison of ARM and HEAT protein repeats.
Miguel A Andrade;Carlo Petosa;Sean I O’Donoghue;Christoph W Müller.
Journal of Molecular Biology (2001)
WD40 proteins propel cellular networks
Christian U. Stirnimann;Evangelia Petsalaki;Robert B. Russell;Christoph W. Müller.
Trends in Biochemical Sciences (2010)
Structure of the complex between adenylate kinase from Escherichia coli and the inhibitor Ap5A refined at 1.9 A resolution. A model for a catalytic transition state.
Christoph W. Müller;Georg E. Schulz.
Journal of Molecular Biology (1992)
Cooperative binding of two acetylation marks on a histone tail by a single bromodomain
Jeanne Morinière;Sophie Rousseaux;Ulrich Steuerwald;Montserrat Soler-López.
Adenylate kinase motions during catalysis: an energetic counterweight balancing substrate binding
C. W. Müller;G. J. Schlauderer;Jochen Reinstein;Georg E. Schulz.
Histone H2A monoubiquitination promotes histone H3 methylation in Polycomb repression.
Reinhard Kalb;Sebastian Latwiel;H Irem Baymaz;Pascal W T C Jansen.
Nature Structural & Molecular Biology (2014)
Crystallographic structure of the T domain-DNA complex of the Brachyury transcription factor.
Christoph W. Müller;Bernhard G. Herrmann.
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