What is he best known for?
The fields of study he is best known for:
Cell biology, Biochemistry, Stereochemistry, snRNP and Protein structure are his primary areas of study.
His Stereochemistry research is multidisciplinary, relying on both Short-chain dehydrogenase, Carbonyl Reductase, Reductase, Hydroxysteroid dehydrogenase and Multiple isomorphous replacement.
His snRNP research incorporates elements of Molecular biology, Spliceosome and Small nuclear RNA.
Ralf Ficner focuses mostly in the field of Small nuclear RNA, narrowing it down to matters related to Prp24 and, in some cases, Non-coding RNA, Signal recognition particle RNA, Heterogeneous ribonucleoprotein particle and RNA-Protein Interaction.
His research integrates issues of Nuclear export signal, Exportin-1 and Crystallography, Crystal structure, Random hexamer in his study of Protein structure.
The study incorporates disciplines such as Cryo-electron microscopy, Ribosome, EF-Tu, Ribosomal protein and Binding site in addition to Crystallography.
His most cited work include:
- Structure of the E. coli ribosome–EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM. (268 citations)
- Crystal Structure of the Spliceosomal 15.5Kd Protein Bound to a U4 Snrna Fragment (245 citations)
- Crystal Structure of the Spliceosomal 15.5Kd Protein Bound to a U4 Snrna Fragment (245 citations)
What are the main themes of his work throughout his whole career to date?
Ralf Ficner spends much of his time researching Biochemistry, Stereochemistry, Cell biology, Crystallography and RNA.
His study in Active site, Protein structure, Transfer RNA, Binding site and Enzyme falls under the purview of Biochemistry.
His work carried out in the field of Stereochemistry brings together such families of science as Transferase and Cofactor.
His Cell biology research integrates issues from Saccharomyces cerevisiae, Ribonucleoprotein, snRNP, Spliceosome and Molecular biology.
His Crystallography research focuses on subjects like Biophysics, which are linked to Ran, Nuclear pore and Nuclear export signal.
His RNA study frequently draws parallels with other fields, such as Protein subunit.
He most often published in these fields:
- Biochemistry (41.85%)
- Stereochemistry (25.55%)
- Cell biology (18.94%)
What were the highlights of his more recent work (between 2015-2021)?
- Cell biology (18.94%)
- Biochemistry (41.85%)
- RNA (16.74%)
In recent papers he was focusing on the following fields of study:
His primary areas of investigation include Cell biology, Biochemistry, RNA, Biophysics and Helicase.
He interconnects Saccharomyces cerevisiae, Ribonucleoprotein, Mutant, RNA splicing and Binding site in the investigation of issues within Cell biology.
Biochemistry and Bacillus subtilis are frequently intertwined in his study.
His RNA study incorporates themes from Protein domain, Guanine and Chromosomal translocation.
His biological study deals with issues like Spliceosome, which deal with fields such as snRNP, Intron, Peptide sequence, Plasma protein binding and Sequence alignment.
His Active site study combines topics from a wide range of disciplines, such as Protein structure, Lipoxygenase, Stereochemistry and Substrate.
Between 2015 and 2021, his most popular works were:
- The pathway to GTPase activation of elongation factor SelB on the ribosome (56 citations)
- Structural insights into the mechanism of the DEAH-box RNA helicase Prp43 (49 citations)
- Making and Breaking of an Essential Poison: the Cyclases and Phosphodiesterases That Produce and Degrade the Essential Second Messenger Cyclic di-AMP in Bacteria. (42 citations)
In his most recent research, the most cited papers focused on:
Ralf Ficner mostly deals with Biochemistry, RNA, Cell biology, Protein domain and Helicase.
Active site, RNA splicing, Membrane, Lipoxygenase and Enzyme are the subjects of his Biochemistry studies.
The various areas that he examines in his Active site study include Molecular replacement, Stereochemistry, Substrate and Biosynthesis.
Ralf Ficner has researched Cell biology in several fields, including Phenotype, Stop codon, Mutant and Spliceosome.
Ralf Ficner has included themes like Saccharomyces cerevisiae, Binding site and snRNP in his Spliceosome study.
His Helicase research is multidisciplinary, incorporating elements of Non-coding RNA, Biophysics and RNA editing, Intron.
This overview was generated by a machine learning system which analysed the scientist’s
body of work. If you have any feedback, you can
contact us
here.
