Richard Borner
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Explore the profile of Richard Borner including associated specialties, affiliations and a list of published articles.
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27
Citations
317
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Recent Articles
1.
Borner R, Steinert P, Bandaru N, Schubert A
Micromachines (Basel)
. 2024 Jun;
15(6).
PMID: 38930699
Ultrasonic vibration superimposed face milling enables the generation of predefined surface microstructures by an appropriate setting of the process parameters. The geometrical reproducibility of the surface characteristics depends strongly on...
2.
Steffen F, Cunha R, Sigel R, Borner R
Nucleic Acids Res
. 2024 Jun;
52(13):e59.
PMID: 38869063
The functional diversity of RNAs is encoded in their innate conformational heterogeneity. The combination of single-molecule spectroscopy and computational modeling offers new attractive opportunities to map structural transitions within nucleic...
3.
Gotz M, Barth A, Bohr S, Borner R, Chen J, Cordes T, et al.
Nat Commun
. 2024 Apr;
15(1):3626.
PMID: 38688911
No abstract available.
4.
Ploetz E, Ambrose B, Barth A, Borner R, Erichson F, Kapanidis A, et al.
Methods Appl Fluoresc
. 2023 Sep;
12(1).
PMID: 37726007
PIFE was first used as an acronym for protein-induced fluorescence enhancement, which refers to the increase in fluorescence observed upon the interaction of a fluorophore, such as a cyanine, with...
5.
Yang A, Lein F, Weiler J, Drechsel J, Schumann V, Erichson F, et al.
HardwareX
. 2023 Jul;
14:e00425.
PMID: 37424928
Sample preparation is a crucial step in single-molecule experiments and involves passivating the microfluidic sample chamber, immobilizing the molecules, and setting experimental buffer conditions. The efficiency of the experiment depends...
6.
Ploetz E, Ambrose B, Barth A, Borner R, Erichson F, Kapanidis A, et al.
ArXiv
. 2023 Mar;
PMID: 36866225
PIFE was first used as an acronym for protein-induced fluorescence enhancement, which refers to the increase in fluorescence observed upon the interaction of a fluorophore, such as a cyanine, with...
7.
Gotz M, Barth A, Bohr S, Borner R, Chen J, Cordes T, et al.
Nat Commun
. 2022 Sep;
13(1):5402.
PMID: 36104339
Single-molecule FRET (smFRET) is a versatile technique to study the dynamics and function of biomolecules since it makes nanoscale movements detectable as fluorescence signals. The powerful ability to infer quantitative...
8.
Hadzic M, Sigel R, Borner R
Methods Mol Biol
. 2022 Feb;
2439:173-190.
PMID: 35226322
Single-molecule microscopy is often used to observe and characterize the conformational dynamics of nucleic acids (NA). Due to the large variety of NA structures and the challenges specific to single-molecule...
9.
Steffen F, Sigel R, Borner R
Bioinformatics
. 2021 Sep;
37(21):3953-3955.
PMID: 34478493
Summary: Quantitative interpretation of single-molecule FRET experiments requires a model of the dye dynamics to link experimental energy transfer efficiencies to distances between atom positions. We have developed FRETraj, a...
10.
Gerhardy S, Oborska-Oplova M, Gillet L, Borner R, van Nues R, Leitner A, et al.
Nat Commun
. 2021 Aug;
12(1):4696.
PMID: 34349113
Productive ribosomal RNA (rRNA) compaction during ribosome assembly necessitates establishing correct tertiary contacts between distant secondary structure elements. Here, we quantify the response of the yeast proteome to low temperature...