R
Ralph Feltens
Researcher at University of Lübeck
Publications - 12
Citations - 460
Ralph Feltens is an academic researcher from University of Lübeck. The author has contributed to research in topics: RNase P & RNase MRP. The author has an hindex of 11, co-authored 12 publications receiving 437 citations. Previous affiliations of Ralph Feltens include Free University of Berlin.
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Journal ArticleDOI
Genetic association of vitamin D receptor polymorphisms with autoimmune hepatitis and primary biliary cirrhosis in the Chinese.
Lie-ying Fan,Xiao-qing Tu,Ye Zhu,Lin Zhou,Thomas Pfeiffer,Ralph Feltens,Winfried Stoecker,Ren-qian Zhong +7 more
TL;DR: The association between Chinese patients with AIH, PBC and the polymorphisms in exon 2, intron 8 and exon 9 of vitamin D receptor genes was studied and it was found that these polymorphisms are associated with autoimmune diseases.
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Cytotoxic T lymphocyte associated antigen-4 gene polymorphisms confer susceptibility to primary biliary cirrhosis and autoimmune hepatitis in Chinese population.
TL;DR: Polymorphisms of CTLA-4 gene probably confer susceptibility to AIH and PBC in Chinese population, and the frequency of C alleles in promoter -318 was significantly increased in AIH patients compared with controls.
Journal ArticleDOI
Genetic association of cytokines polymorphisms with autoimmune hepatitis and primary biliary cirrhosis in the Chinese.
Lie-ying Fan,Xiao-qing Tu,Ye Zhu,Thomas Pfeiffer,Ralph Feltens,Winfried Stoecker,Renqian Zhong +6 more
TL;DR: The polymorphisms of IL-1RN and IL-6 -174G/C appear to be associated with PBC in Chinese patients according to the study population and the difference of the polymorphism distribution between Chinese patients and healthy controls.
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Exploring the minimal substrate requirements for trans-cleavage by RNase P holoenzymes from Escherichia coli and Bacillus subtilis.
Annika Hansen,Thomas Pfeiffer,Tilman Zuleeg,Stefan Limmer,Jerzy Ciesiołka,Ralph Feltens,Roland K. Hartmann +6 more
TL;DR: The results indicate that the crucial contribution of nt −2 in the single‐stranded 5′ flank to productive interaction is a general feature of A‐ and B‐type bacterial RNase P enzymes.
Journal ArticleDOI
Potential contact sites between the protein and RNA subunit in the Bacillus subtilis RNase P holoenzyme
TL;DR: The results suggest that P3, P2-J18/2 and J19/4 are key elements for anchoring of the protein to the catalytic domain close to the scissile phosphodiester in enzyme-substrate complexes, and the current 3D model has to be rearranged in order to reduce the distance between clusters 1 and 2a.