2014 - German National Academy of Sciences Leopoldina - Deutsche Akademie der Naturforscher Leopoldina – Nationale Akademie der Wissenschaften Biochemistry and Biophysics
Member of the European Molecular Biology Organization (EMBO)
Karl-Peter Hopfner mainly focuses on Biochemistry, DNA, Protein structure, Cell biology and Molecular biology. His studies in DNA integrate themes in fields like ATPase, Biophysics and Cyclic GMP-AMP synthase, Stimulator of interferon genes. His Protein structure research includes themes of Plasma protein binding, Cyclase activity, Histone octamer, DNA repair and Antibody.
His study in Cell biology is interdisciplinary in nature, drawing from both Interferon and Base pair. He has researched Molecular biology in several fields, including Epitope, Primary and secondary antibodies, Antigen, Signal transduction and Monoclonal antibody. His biological study spans a wide range of topics, including Nucleic acid and Pattern recognition receptor.
Karl-Peter Hopfner focuses on Cell biology, DNA, Biochemistry, RNA and Genetics. The study incorporates disciplines such as ATP hydrolysis, Molecular biology, Protein structure, Innate immune system and Binding site in addition to Cell biology. His studies deal with areas such as Mutation, Signal transduction, Antibody and Transcription factor as well as Molecular biology.
His DNA research is multidisciplinary, incorporating perspectives in Biophysics and Rad50. His research investigates the link between Biophysics and topics such as ATPase that cross with problems in Adenosine triphosphate, Hydrolase and Structural biology. His work on Active site, Enzyme and Plasma protein binding as part of his general Biochemistry study is frequently connected to DNA clamp, thereby bridging the divide between different branches of science.
Karl-Peter Hopfner mostly deals with DNA, Cell biology, Cancer research, Chromatin and Nucleosome. His DNA research is included under the broader classification of Biochemistry. His Cell biology research integrates issues from Protein structure, Innate immune system, DNA repair and DNA-binding protein.
His Innate immune system research is multidisciplinary, incorporating elements of RNA, Endogeny and Function. As part of one scientific family, he deals mainly with the area of Chromatin, narrowing it down to issues related to the Microbial DNA, and often MAPK/ERK pathway, Signal transduction, Stimulator of interferon genes and ATP synthase. His work carried out in the field of Nucleosome brings together such families of science as Genome, Computational biology and Chromatin remodeling.
His scientific interests lie mostly in Cell biology, DNA, Chromatin, RNA and RIG-I. Karl-Peter Hopfner combines subjects such as Protein structure, Innate immune system, DNA repair and DNA-binding protein with his study of Cell biology. His research in DNA intersects with topics in Biophysics and Rad50.
His work deals with themes such as Gene expression, Virus, Herpes simplex virus, Virology and Ribosomal RNA, which intersect with RNA. He has included themes like Influenza A virus and Gene silencing in his RIG-I study. Base pair is a subfield of Biochemistry that Karl-Peter Hopfner tackles.
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Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily.
Karl Peter Hopfner;Annette Karcher;David S. Shin;Lisa Craig.
Cell (2000)
cGAS produces a 2′-5′-linked cyclic dinucleotide second messenger that activates STING
Andrea Ablasser;Marion Goldeck;Taner Cavlar;Tobias Deimling.
Nature (2013)
The Rad50 zinc-hook is a structure joining Mre11 complexes in DNA recombination and repair
Karl Peter Hopfner;Lisa Craig;Gabriel Moncalian;Robert A. Zinkel.
Nature (2002)
The C-Terminal Regulatory Domain Is the RNA 5'-Triphosphate Sensor of RIG-I.
Sheng Cui;Katharina Eisenächer;Axel Kirchhofer;Krzysztof Brzózka.
Molecular Cell (2008)
Structural Biochemistry and Interaction Architecture of the DNA Double-Strand Break Repair Mre11 Nuclease and Rad50-ATPase
Karl Peter Hopfner;Annette Karcher;Lisa Craig;Tammy T. Woo.
Cell (2001)
Structural mechanism of cytosolic DNA sensing by cGAS
Filiz Civril;Tobias Deimling;Carina C. de Oliveira Mann;Andrea Ablasser.
Nature (2013)
Modulation of protein properties in living cells using nanobodies
Axel Kirchhofer;Jonas Helma;Jonas Helma;Katrin Schmidthals;Katrin Schmidthals;Carina Frauer;Carina Frauer.
Nature Structural & Molecular Biology (2010)
5′-triphosphate RNA requires base-paired structures to activate antiviral signaling via RIG-I
Andreas Schmidt;Tobias Schwerd;Wolfgang Hamm;Johannes C. Hellmuth.
Proceedings of the National Academy of Sciences of the United States of America (2009)
Structural Biochemistry of a Bacterial Checkpoint Protein Reveals Diadenylate Cyclase Activity Regulated by DNA Recombination Intermediates
Gregor Witte;Sophia Hartung;Katharina Büttner;Karl-Peter Hopfner.
Molecular Cell (2008)
Cytosolic Viral Sensor RIG-I Is a 5′-Triphosphate-Dependent Translocase on Double-Stranded RNA
Su-A Myong;Sheng Cui;Peter V. Cornish;Peter V. Cornish;Axel Kirchhofer.
Science (2009)
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