---
_id: '51121'
abstract:
- lang: eng
text: DNA origami nanostructures are a powerful tool in biomedicine and
can be used to combat drug‐resistant bacterial infections. However, the effect
of unmodified DNA origami nanostructures on bacteria is yet to be elucidated.
With the aim to obtain a better understanding of this phenomenon, the effect of
three DNA origami shapes, i.e., DNA origami triangles, six‐helix bundles (6HBs),
and 24‐helix bundles (24HBs), on the growth of Gram‐negative Escherichia coli
and Gram‐positive Bacillus subtilis is investigated. These results reveal that
while triangles and 24HBs can be used as a source of nutrients by E. coli and
thereby promote population growth, their effect is much smaller than that of genomic
single‐ and double‐stranded DNA. However, no effect on E. coli population growth
is observed for the 6HBs. On the other hand, B. subtilis does not show any significant
changes in population growth when cultured with the different DNA origami shapes
or genomic DNA. The detailed effect of DNA origami nanostructures on bacterial
growth thus depends on the competence signals and uptake mechanism of each bacterial
species, as well as the DNA origami shape. This should be considered in the development
of antimicrobial DNA origami nanostructures.
author:
- first_name: Jaime Andres
full_name: Garcia-Diosa, Jaime Andres
last_name: Garcia-Diosa
- first_name: Guido
full_name: Grundmeier, Guido
id: '194'
last_name: Grundmeier
- first_name: Adrian
full_name: Keller, Adrian
id: '48864'
last_name: Keller
orcid: 0000-0001-7139-3110
citation:
ama: Garcia-Diosa JA, Grundmeier G, Keller A. Effect of DNA Origami Nanostructures
on Bacterial Growth. ChemBioChem. Published online 2024. doi:10.1002/cbic.202400091
apa: Garcia-Diosa, J. A., Grundmeier, G., & Keller, A. (2024). Effect of DNA
Origami Nanostructures on Bacterial Growth. ChemBioChem. https://doi.org/10.1002/cbic.202400091
bibtex: '@article{Garcia-Diosa_Grundmeier_Keller_2024, title={Effect of DNA Origami
Nanostructures on Bacterial Growth}, DOI={10.1002/cbic.202400091},
journal={ChemBioChem}, publisher={Wiley}, author={Garcia-Diosa, Jaime Andres and
Grundmeier, Guido and Keller, Adrian}, year={2024} }'
chicago: Garcia-Diosa, Jaime Andres, Guido Grundmeier, and Adrian Keller. “Effect
of DNA Origami Nanostructures on Bacterial Growth.” ChemBioChem, 2024.
https://doi.org/10.1002/cbic.202400091.
ieee: 'J. A. Garcia-Diosa, G. Grundmeier, and A. Keller, “Effect of DNA Origami
Nanostructures on Bacterial Growth,” ChemBioChem, 2024, doi: 10.1002/cbic.202400091.'
mla: Garcia-Diosa, Jaime Andres, et al. “Effect of DNA Origami Nanostructures on
Bacterial Growth.” ChemBioChem, Wiley, 2024, doi:10.1002/cbic.202400091.
short: J.A. Garcia-Diosa, G. Grundmeier, A. Keller, ChemBioChem (2024).
date_created: 2024-02-03T12:41:16Z
date_updated: 2024-02-03T12:42:48Z
department:
- _id: '302'
doi: 10.1002/cbic.202400091
keyword:
- Organic Chemistry
- Molecular Biology
- Molecular Medicine
- Biochemistry
language:
- iso: eng
publication: ChemBioChem
publication_identifier:
issn:
- 1439-4227
- 1439-7633
publication_status: published
publisher: Wiley
status: public
title: Effect of DNA Origami Nanostructures on Bacterial Growth
type: journal_article
user_id: '48864'
year: '2024'
...
---
_id: '46023'
abstract:
- lang: eng
text: This article presents the potential-dependent adsorption of two proteins,
bovine serum albumin (BSA) and lysozyme (LYZ), on Ti6Al4V alloy at pH 7.4 and
37 °C. The adsorption process was studied on an electropolished alloy under cathodic
and anodic overpotentials, compared to the open circuit potential (OCP). To analyze
the adsorption process, various complementary interface analytical techniques
were employed, including PM-IRRAS (polarization-modulation infrared reflection-absorption
spectroscopy), AFM (atomic force microscopy), XPS (X-ray photoelectron spectroscopy),
and E-QCM (electrochemical quartz crystal microbalance) measurements. The polarization
experiments were conducted within a potential range where charging of the electric
double layer dominates, and Faradaic currents can be disregarded. The findings
highlight the significant influence of the interfacial charge distribution on
the adsorption of BSA and LYZ onto the alloy surface. Furthermore, electrochemical
analysis of the protein layers formed under applied overpotentials demonstrated
improved corrosion protection properties. These studies provide valuable insights
into protein adsorption on titanium alloys under physiological conditions, characterized
by varying potentials of the passive alloy.
article_number: '5109'
author:
- first_name: Belma
full_name: Duderija, Belma
last_name: Duderija
- first_name: Alejandro
full_name: González-Orive, Alejandro
last_name: González-Orive
- first_name: Christoph
full_name: Ebbert, Christoph
last_name: Ebbert
- first_name: Vanessa
full_name: Neßlinger, Vanessa
last_name: Neßlinger
- first_name: Adrian
full_name: Keller, Adrian
last_name: Keller
- first_name: Guido
full_name: Grundmeier, Guido
last_name: Grundmeier
citation:
ama: Duderija B, González-Orive A, Ebbert C, Neßlinger V, Keller A, Grundmeier G.
Electrode Potential-Dependent Studies of Protein Adsorption on Ti6Al4V Alloy.
Molecules. 2023;28(13). doi:10.3390/molecules28135109
apa: Duderija, B., González-Orive, A., Ebbert, C., Neßlinger, V., Keller, A., &
Grundmeier, G. (2023). Electrode Potential-Dependent Studies of Protein Adsorption
on Ti6Al4V Alloy. Molecules, 28(13), Article 5109. https://doi.org/10.3390/molecules28135109
bibtex: '@article{Duderija_González-Orive_Ebbert_Neßlinger_Keller_Grundmeier_2023,
title={Electrode Potential-Dependent Studies of Protein Adsorption on Ti6Al4V
Alloy}, volume={28}, DOI={10.3390/molecules28135109},
number={135109}, journal={Molecules}, publisher={MDPI AG}, author={Duderija, Belma
and González-Orive, Alejandro and Ebbert, Christoph and Neßlinger, Vanessa and
Keller, Adrian and Grundmeier, Guido}, year={2023} }'
chicago: Duderija, Belma, Alejandro González-Orive, Christoph Ebbert, Vanessa Neßlinger,
Adrian Keller, and Guido Grundmeier. “Electrode Potential-Dependent Studies of
Protein Adsorption on Ti6Al4V Alloy.” Molecules 28, no. 13 (2023). https://doi.org/10.3390/molecules28135109.
ieee: 'B. Duderija, A. González-Orive, C. Ebbert, V. Neßlinger, A. Keller, and G.
Grundmeier, “Electrode Potential-Dependent Studies of Protein Adsorption on Ti6Al4V
Alloy,” Molecules, vol. 28, no. 13, Art. no. 5109, 2023, doi: 10.3390/molecules28135109.'
mla: Duderija, Belma, et al. “Electrode Potential-Dependent Studies of Protein Adsorption
on Ti6Al4V Alloy.” Molecules, vol. 28, no. 13, 5109, MDPI AG, 2023, doi:10.3390/molecules28135109.
short: B. Duderija, A. González-Orive, C. Ebbert, V. Neßlinger, A. Keller, G. Grundmeier,
Molecules 28 (2023).
date_created: 2023-07-12T07:55:40Z
date_updated: 2024-02-06T12:33:55Z
department:
- _id: '321'
- _id: '302'
doi: 10.3390/molecules28135109
intvolume: ' 28'
issue: '13'
keyword:
- Chemistry (miscellaneous)
- Analytical Chemistry
- Organic Chemistry
- Physical and Theoretical Chemistry
- Molecular Medicine
- Drug Discovery
- Pharmaceutical Science
language:
- iso: eng
publication: Molecules
publication_identifier:
issn:
- 1420-3049
publication_status: published
publisher: MDPI AG
status: public
title: Electrode Potential-Dependent Studies of Protein Adsorption on Ti6Al4V Alloy
type: journal_article
user_id: '54863'
volume: 28
year: '2023'
...
---
_id: '44503'
author:
- first_name: Marcel
full_name: Hanke, Marcel
last_name: Hanke
- first_name: Emilia
full_name: Tomm, Emilia
last_name: Tomm
- first_name: Guido
full_name: Grundmeier, Guido
id: '194'
last_name: Grundmeier
- first_name: Adrian
full_name: Keller, Adrian
id: '48864'
last_name: Keller
orcid: 0000-0001-7139-3110
citation:
ama: Hanke M, Tomm E, Grundmeier G, Keller A. Effect of Ionic Strength on the Thermal
Stability of DNA Origami Nanostructures. ChemBioChem. Published online
2023. doi:10.1002/cbic.202300338
apa: Hanke, M., Tomm, E., Grundmeier, G., & Keller, A. (2023). Effect of Ionic
Strength on the Thermal Stability of DNA Origami Nanostructures. ChemBioChem.
https://doi.org/10.1002/cbic.202300338
bibtex: '@article{Hanke_Tomm_Grundmeier_Keller_2023, title={Effect of Ionic Strength
on the Thermal Stability of DNA Origami Nanostructures}, DOI={10.1002/cbic.202300338},
journal={ChemBioChem}, publisher={Wiley}, author={Hanke, Marcel and Tomm, Emilia
and Grundmeier, Guido and Keller, Adrian}, year={2023} }'
chicago: Hanke, Marcel, Emilia Tomm, Guido Grundmeier, and Adrian Keller. “Effect
of Ionic Strength on the Thermal Stability of DNA Origami Nanostructures.” ChemBioChem,
2023. https://doi.org/10.1002/cbic.202300338.
ieee: 'M. Hanke, E. Tomm, G. Grundmeier, and A. Keller, “Effect of Ionic Strength
on the Thermal Stability of DNA Origami Nanostructures,” ChemBioChem, 2023,
doi: 10.1002/cbic.202300338.'
mla: Hanke, Marcel, et al. “Effect of Ionic Strength on the Thermal Stability of
DNA Origami Nanostructures.” ChemBioChem, Wiley, 2023, doi:10.1002/cbic.202300338.
short: M. Hanke, E. Tomm, G. Grundmeier, A. Keller, ChemBioChem (2023).
date_created: 2023-05-05T10:47:29Z
date_updated: 2023-05-05T10:48:00Z
department:
- _id: '302'
doi: 10.1002/cbic.202300338
keyword:
- Organic Chemistry
- Molecular Biology
- Molecular Medicine
- Biochemistry
language:
- iso: eng
publication: ChemBioChem
publication_identifier:
issn:
- 1439-4227
- 1439-7633
publication_status: published
publisher: Wiley
status: public
title: Effect of Ionic Strength on the Thermal Stability of DNA Origami Nanostructures
type: journal_article
user_id: '48864'
year: '2023'
...
---
_id: '45828'
abstract:
- lang: eng
text: This article presents the potential-dependent adsorption of two proteins,
bovine serum albumin (BSA) and lysozyme (LYZ), on Ti6Al4V alloy at pH 7.4 and
37 °C. The adsorption process was studied on an electropolished alloy under cathodic
and anodic overpotentials, compared to the open circuit potential (OCP). To analyze
the adsorption process, various complementary interface analytical techniques
were employed, including PM-IRRAS (polarization-modulation infrared reflection-absorption
spectroscopy), AFM (atomic force microscopy), XPS (X-ray photoelectron spectroscopy),
and E-QCM (electrochemical quartz crystal microbalance) measurements. The polarization
experiments were conducted within a potential range where charging of the electric
double layer dominates, and Faradaic currents can be disregarded. The findings
highlight the significant influence of the interfacial charge distribution on
the adsorption of BSA and LYZ onto the alloy surface. Furthermore, electrochemical
analysis of the protein layers formed under applied overpotentials demonstrated
improved corrosion protection properties. These studies provide valuable insights
into protein adsorption on titanium alloys under physiological conditions, characterized
by varying potentials of the passive alloy.
author:
- first_name: Belma
full_name: Duderija, Belma
id: '54863'
last_name: Duderija
- first_name: Alejandro
full_name: González-Orive, Alejandro
last_name: González-Orive
- first_name: Christoph
full_name: Ebbert, Christoph
id: '7266'
last_name: Ebbert
- first_name: Vanessa
full_name: Neßlinger, Vanessa
last_name: Neßlinger
- first_name: Adrian
full_name: Keller, Adrian
id: '48864'
last_name: Keller
orcid: 0000-0001-7139-3110
- first_name: Guido
full_name: Grundmeier, Guido
id: '194'
last_name: Grundmeier
citation:
ama: Duderija B, González-Orive A, Ebbert C, Neßlinger V, Keller A, Grundmeier G.
Electrode Potential-Dependent Studies of Protein Adsorption on Ti6Al4V Alloy.
Molecules. 2023;28(13):5109. doi:10.3390/molecules28135109
apa: Duderija, B., González-Orive, A., Ebbert, C., Neßlinger, V., Keller, A., &
Grundmeier, G. (2023). Electrode Potential-Dependent Studies of Protein Adsorption
on Ti6Al4V Alloy. Molecules, 28(13), 5109. https://doi.org/10.3390/molecules28135109
bibtex: '@article{Duderija_González-Orive_Ebbert_Neßlinger_Keller_Grundmeier_2023,
title={Electrode Potential-Dependent Studies of Protein Adsorption on Ti6Al4V
Alloy}, volume={28}, DOI={10.3390/molecules28135109},
number={13}, journal={Molecules}, publisher={MDPI AG}, author={Duderija, Belma
and González-Orive, Alejandro and Ebbert, Christoph and Neßlinger, Vanessa and
Keller, Adrian and Grundmeier, Guido}, year={2023}, pages={5109} }'
chicago: 'Duderija, Belma, Alejandro González-Orive, Christoph Ebbert, Vanessa Neßlinger,
Adrian Keller, and Guido Grundmeier. “Electrode Potential-Dependent Studies of
Protein Adsorption on Ti6Al4V Alloy.” Molecules 28, no. 13 (2023): 5109.
https://doi.org/10.3390/molecules28135109.'
ieee: 'B. Duderija, A. González-Orive, C. Ebbert, V. Neßlinger, A. Keller, and G.
Grundmeier, “Electrode Potential-Dependent Studies of Protein Adsorption on Ti6Al4V
Alloy,” Molecules, vol. 28, no. 13, p. 5109, 2023, doi: 10.3390/molecules28135109.'
mla: Duderija, Belma, et al. “Electrode Potential-Dependent Studies of Protein Adsorption
on Ti6Al4V Alloy.” Molecules, vol. 28, no. 13, MDPI AG, 2023, p. 5109,
doi:10.3390/molecules28135109.
short: B. Duderija, A. González-Orive, C. Ebbert, V. Neßlinger, A. Keller, G. Grundmeier,
Molecules 28 (2023) 5109.
date_created: 2023-07-03T08:06:28Z
date_updated: 2023-07-03T08:07:55Z
department:
- _id: '302'
doi: 10.3390/molecules28135109
intvolume: ' 28'
issue: '13'
keyword:
- Chemistry (miscellaneous)
- Analytical Chemistry
- Organic Chemistry
- Physical and Theoretical Chemistry
- Molecular Medicine
- Drug Discovery
- Pharmaceutical Science
language:
- iso: eng
page: '5109'
publication: Molecules
publication_identifier:
issn:
- 1420-3049
publication_status: published
publisher: MDPI AG
status: public
title: Electrode Potential-Dependent Studies of Protein Adsorption on Ti6Al4V Alloy
type: journal_article
user_id: '48864'
volume: 28
year: '2023'
...
---
_id: '46542'
abstract:
- lang: eng
text: Multiprotein adsorption from complex body fluids represents a highly
important and complicated phenomenon in medicine. In this work, multiprotein adsorption
from diluted human serum at gold and oxidized iron surfaces is investigated at
different serum concentrations and pH values. Adsorption-induced changes in surface
topography and the total amount of adsorbed proteins are quantified by atomic
force microscopy (AFM) and polarization-modulation infrared reflection absorption
spectroscopy (PM-IRRAS), respectively. For both surfaces, stronger protein adsorption
is observed at pH 6 compared to pH 7 and pH 8. PM-IRRAS furthermore provides some
qualitative insights into the pH-dependent alterations in the composition of the
adsorbed multiprotein films. Changes in the amide II/amide I band area ratio and
in particular side-chain IR absorption suggest that the increased adsorption at
pH 6 is accompanied by a change in protein film composition. Presumably, this
is mostly driven by the adsorption of human serum albumin, which at pH 6 adsorbs
more readily and thereby replaces other proteins with lower surface affinities
in the resulting multiprotein film.
article_number: '6060'
author:
- first_name: Jingyuan
full_name: Huang, Jingyuan
last_name: Huang
- first_name: Yunshu
full_name: Qiu, Yunshu
last_name: Qiu
- first_name: Felix
full_name: Lücke, Felix
last_name: Lücke
- first_name: Jiangling
full_name: Su, Jiangling
last_name: Su
- first_name: Guido
full_name: Grundmeier, Guido
id: '194'
last_name: Grundmeier
- first_name: Adrian
full_name: Keller, Adrian
id: '48864'
last_name: Keller
orcid: 0000-0001-7139-3110
citation:
ama: Huang J, Qiu Y, Lücke F, Su J, Grundmeier G, Keller A. Multiprotein Adsorption
from Human Serum at Gold and Oxidized Iron Surfaces Studied by Atomic Force Microscopy
and Polarization-Modulation Infrared Reflection Absorption Spectroscopy. Molecules.
2023;28(16). doi:10.3390/molecules28166060
apa: Huang, J., Qiu, Y., Lücke, F., Su, J., Grundmeier, G., & Keller, A. (2023).
Multiprotein Adsorption from Human Serum at Gold and Oxidized Iron Surfaces Studied
by Atomic Force Microscopy and Polarization-Modulation Infrared Reflection Absorption
Spectroscopy. Molecules, 28(16), Article 6060. https://doi.org/10.3390/molecules28166060
bibtex: '@article{Huang_Qiu_Lücke_Su_Grundmeier_Keller_2023, title={Multiprotein
Adsorption from Human Serum at Gold and Oxidized Iron Surfaces Studied by Atomic
Force Microscopy and Polarization-Modulation Infrared Reflection Absorption Spectroscopy},
volume={28}, DOI={10.3390/molecules28166060},
number={166060}, journal={Molecules}, publisher={MDPI AG}, author={Huang, Jingyuan
and Qiu, Yunshu and Lücke, Felix and Su, Jiangling and Grundmeier, Guido and Keller,
Adrian}, year={2023} }'
chicago: Huang, Jingyuan, Yunshu Qiu, Felix Lücke, Jiangling Su, Guido Grundmeier,
and Adrian Keller. “Multiprotein Adsorption from Human Serum at Gold and Oxidized
Iron Surfaces Studied by Atomic Force Microscopy and Polarization-Modulation Infrared
Reflection Absorption Spectroscopy.” Molecules 28, no. 16 (2023). https://doi.org/10.3390/molecules28166060.
ieee: 'J. Huang, Y. Qiu, F. Lücke, J. Su, G. Grundmeier, and A. Keller, “Multiprotein
Adsorption from Human Serum at Gold and Oxidized Iron Surfaces Studied by Atomic
Force Microscopy and Polarization-Modulation Infrared Reflection Absorption Spectroscopy,”
Molecules, vol. 28, no. 16, Art. no. 6060, 2023, doi: 10.3390/molecules28166060.'
mla: Huang, Jingyuan, et al. “Multiprotein Adsorption from Human Serum at Gold and
Oxidized Iron Surfaces Studied by Atomic Force Microscopy and Polarization-Modulation
Infrared Reflection Absorption Spectroscopy.” Molecules, vol. 28, no. 16,
6060, MDPI AG, 2023, doi:10.3390/molecules28166060.
short: J. Huang, Y. Qiu, F. Lücke, J. Su, G. Grundmeier, A. Keller, Molecules 28
(2023).
date_created: 2023-08-16T10:51:48Z
date_updated: 2023-08-16T10:53:08Z
department:
- _id: '302'
doi: 10.3390/molecules28166060
intvolume: ' 28'
issue: '16'
keyword:
- Chemistry (miscellaneous)
- Analytical Chemistry
- Organic Chemistry
- Physical and Theoretical Chemistry
- Molecular Medicine
- Drug Discovery
- Pharmaceutical Science
language:
- iso: eng
publication: Molecules
publication_identifier:
issn:
- 1420-3049
publication_status: published
publisher: MDPI AG
status: public
title: Multiprotein Adsorption from Human Serum at Gold and Oxidized Iron Surfaces
Studied by Atomic Force Microscopy and Polarization-Modulation Infrared Reflection
Absorption Spectroscopy
type: journal_article
user_id: '48864'
volume: 28
year: '2023'
...
---
_id: '30739'
author:
- first_name: Julia
full_name: Ring, Julia
last_name: Ring
- first_name: Jelena
full_name: Tadic, Jelena
last_name: Tadic
- first_name: Selena
full_name: Ristic, Selena
last_name: Ristic
- first_name: Michael
full_name: Poglitsch, Michael
last_name: Poglitsch
- first_name: Martina
full_name: Bergmann, Martina
last_name: Bergmann
- first_name: Nemanja
full_name: Radic, Nemanja
last_name: Radic
- first_name: Dirk
full_name: Mossmann, Dirk
last_name: Mossmann
- first_name: YongTian
full_name: Liang, YongTian
last_name: Liang
- first_name: Marta
full_name: Maglione, Marta
last_name: Maglione
- first_name: Andrea
full_name: Jerkovic, Andrea
last_name: Jerkovic
- first_name: Roozbeh
full_name: Hajiraissi, Roozbeh
last_name: Hajiraissi
- first_name: Marcel
full_name: Hanke, Marcel
last_name: Hanke
- first_name: Victoria
full_name: Küttner, Victoria
last_name: Küttner
- first_name: Heimo
full_name: Wolinski, Heimo
last_name: Wolinski
- first_name: Andreas
full_name: Zimmermann, Andreas
last_name: Zimmermann
- first_name: Lana
full_name: Domuz Trifunović, Lana
last_name: Domuz Trifunović
- first_name: Leonie
full_name: Mikolasch, Leonie
last_name: Mikolasch
- first_name: Daiana N
full_name: Moretti, Daiana N
last_name: Moretti
- first_name: Filomena
full_name: Broeskamp, Filomena
last_name: Broeskamp
- first_name: Julia
full_name: Westermayer, Julia
last_name: Westermayer
- first_name: Claudia
full_name: Abraham, Claudia
last_name: Abraham
- first_name: Simon
full_name: Schauer, Simon
last_name: Schauer
- first_name: Christopher
full_name: Dammbrueck, Christopher
last_name: Dammbrueck
- first_name: Sebastian J
full_name: Hofer, Sebastian J
last_name: Hofer
- first_name: Mahmoud
full_name: Abdellatif, Mahmoud
last_name: Abdellatif
- first_name: Guido
full_name: Grundmeier, Guido
id: '194'
last_name: Grundmeier
- first_name: Guido
full_name: Kroemer, Guido
last_name: Kroemer
- first_name: Ralf J
full_name: Braun, Ralf J
last_name: Braun
- first_name: Niklas
full_name: Hansen, Niklas
last_name: Hansen
- first_name: Cornelia
full_name: Sommer, Cornelia
last_name: Sommer
- first_name: Mirjana
full_name: Ninkovic, Mirjana
last_name: Ninkovic
- first_name: Sandra
full_name: Seba, Sandra
last_name: Seba
- first_name: Patrick
full_name: Rockenfeller, Patrick
last_name: Rockenfeller
- first_name: Friederike‐Nora
full_name: Vögtle, Friederike‐Nora
last_name: Vögtle
- first_name: Jörn
full_name: Dengjel, Jörn
last_name: Dengjel
- first_name: Chris
full_name: Meisinger, Chris
last_name: Meisinger
- first_name: Adrian
full_name: Keller, Adrian
id: '48864'
last_name: Keller
orcid: 0000-0001-7139-3110
- first_name: Stephan J
full_name: Sigrist, Stephan J
last_name: Sigrist
- first_name: Tobias
full_name: Eisenberg, Tobias
last_name: Eisenberg
- first_name: Frank
full_name: Madeo, Frank
last_name: Madeo
citation:
ama: Ring J, Tadic J, Ristic S, et al. The HSP40 chaperone Ydj1 drives amyloid beta
42 toxicity. EMBO Molecular Medicine. 2022;14:e13952. doi:10.15252/emmm.202113952
apa: Ring, J., Tadic, J., Ristic, S., Poglitsch, M., Bergmann, M., Radic, N., Mossmann,
D., Liang, Y., Maglione, M., Jerkovic, A., Hajiraissi, R., Hanke, M., Küttner,
V., Wolinski, H., Zimmermann, A., Domuz Trifunović, L., Mikolasch, L., Moretti,
D. N., Broeskamp, F., … Madeo, F. (2022). The HSP40 chaperone Ydj1 drives amyloid
beta 42 toxicity. EMBO Molecular Medicine, 14, e13952. https://doi.org/10.15252/emmm.202113952
bibtex: '@article{Ring_Tadic_Ristic_Poglitsch_Bergmann_Radic_Mossmann_Liang_Maglione_Jerkovic_et
al._2022, title={The HSP40 chaperone Ydj1 drives amyloid beta 42 toxicity}, volume={14},
DOI={10.15252/emmm.202113952},
journal={EMBO Molecular Medicine}, publisher={EMBO}, author={Ring, Julia and Tadic,
Jelena and Ristic, Selena and Poglitsch, Michael and Bergmann, Martina and Radic,
Nemanja and Mossmann, Dirk and Liang, YongTian and Maglione, Marta and Jerkovic,
Andrea and et al.}, year={2022}, pages={e13952} }'
chicago: 'Ring, Julia, Jelena Tadic, Selena Ristic, Michael Poglitsch, Martina Bergmann,
Nemanja Radic, Dirk Mossmann, et al. “The HSP40 Chaperone Ydj1 Drives Amyloid
Beta 42 Toxicity.” EMBO Molecular Medicine 14 (2022): e13952. https://doi.org/10.15252/emmm.202113952.'
ieee: 'J. Ring et al., “The HSP40 chaperone Ydj1 drives amyloid beta 42 toxicity,”
EMBO Molecular Medicine, vol. 14, p. e13952, 2022, doi: 10.15252/emmm.202113952.'
mla: Ring, Julia, et al. “The HSP40 Chaperone Ydj1 Drives Amyloid Beta 42 Toxicity.”
EMBO Molecular Medicine, vol. 14, EMBO, 2022, p. e13952, doi:10.15252/emmm.202113952.
short: J. Ring, J. Tadic, S. Ristic, M. Poglitsch, M. Bergmann, N. Radic, D. Mossmann,
Y. Liang, M. Maglione, A. Jerkovic, R. Hajiraissi, M. Hanke, V. Küttner, H. Wolinski,
A. Zimmermann, L. Domuz Trifunović, L. Mikolasch, D.N. Moretti, F. Broeskamp,
J. Westermayer, C. Abraham, S. Schauer, C. Dammbrueck, S.J. Hofer, M. Abdellatif,
G. Grundmeier, G. Kroemer, R.J. Braun, N. Hansen, C. Sommer, M. Ninkovic, S. Seba,
P. Rockenfeller, F. Vögtle, J. Dengjel, C. Meisinger, A. Keller, S.J. Sigrist,
T. Eisenberg, F. Madeo, EMBO Molecular Medicine 14 (2022) e13952.
date_created: 2022-04-04T14:27:15Z
date_updated: 2022-05-09T12:28:24Z
department:
- _id: '302'
doi: 10.15252/emmm.202113952
intvolume: ' 14'
keyword:
- Molecular Medicine
language:
- iso: eng
page: e13952
publication: EMBO Molecular Medicine
publication_identifier:
issn:
- 1757-4676
- 1757-4684
publication_status: published
publisher: EMBO
status: public
title: The HSP40 chaperone Ydj1 drives amyloid beta 42 toxicity
type: journal_article
user_id: '48864'
volume: 14
year: '2022'
...
---
_id: '32323'
abstract:
- lang: eng
text: Genetic correlations suggest a coexisting genetic predisposition to
both low leptin levels and risk for anorexia nervosa (AN). To investigate the
causality and direction of these associations, we performed bidirectional two-sample
Mendelian randomization (MR) analyses using data of the most recent genome-wide
association study (GWAS) for AN and both a GWAS and an exome-wide-association-study
(EWAS) for leptin levels. Most MR methods with genetic instruments from GWAS showed
a causal effect of lower leptin levels on higher risk of AN (e.g. IVW b = −0.923,
p = 1.5 × 10−4). Because most
patients with AN are female, we additionally performed analyses using leptin GWAS
data of females only. Again, there was a significant effect of leptin levels on
the risk of AN (e.g. IVW b = −0.826, p = 1.1 × 10−04).
MR with genetic instruments from EWAS showed no overall effect of leptin levels
on the risk for AN. For the opposite direction, MR revealed no causal effect of
AN on leptin levels. If our results are confirmed in extended GWAS data sets,
a low endogenous leptin synthesis represents a risk factor for developing AN.
author:
- first_name: Triinu
full_name: Peters, Triinu
last_name: Peters
- first_name: Jochen
full_name: Antel, Jochen
last_name: Antel
- first_name: Roaa
full_name: Naaresh, Roaa
last_name: Naaresh
- first_name: Björn-Hergen
full_name: Laabs, Björn-Hergen
last_name: Laabs
- first_name: Manuel
full_name: Föcker, Manuel
last_name: Föcker
- first_name: Nicola
full_name: Albers, Nicola
last_name: Albers
- first_name: Judith
full_name: Bühlmeier, Judith
last_name: Bühlmeier
- first_name: Anke
full_name: Hinney, Anke
last_name: Hinney
- first_name: Lars
full_name: Libuda, Lars
last_name: Libuda
- first_name: Johannes
full_name: Hebebrand, Johannes
last_name: Hebebrand
citation:
ama: 'Peters T, Antel J, Naaresh R, et al. Suggestive Evidence for Causal Effect
of Leptin Levels on Risk for Anorexia Nervosa: Results of a Mendelian Randomization
Study. Frontiers in Genetics. 2021;12. doi:10.3389/fgene.2021.733606'
apa: 'Peters, T., Antel, J., Naaresh, R., Laabs, B.-H., Föcker, M., Albers, N.,
Bühlmeier, J., Hinney, A., Libuda, L., & Hebebrand, J. (2021). Suggestive
Evidence for Causal Effect of Leptin Levels on Risk for Anorexia Nervosa: Results
of a Mendelian Randomization Study. Frontiers in Genetics, 12. https://doi.org/10.3389/fgene.2021.733606'
bibtex: '@article{Peters_Antel_Naaresh_Laabs_Föcker_Albers_Bühlmeier_Hinney_Libuda_Hebebrand_2021,
title={Suggestive Evidence for Causal Effect of Leptin Levels on Risk for Anorexia
Nervosa: Results of a Mendelian Randomization Study}, volume={12}, DOI={10.3389/fgene.2021.733606},
journal={Frontiers in Genetics}, publisher={Frontiers Media SA}, author={Peters,
Triinu and Antel, Jochen and Naaresh, Roaa and Laabs, Björn-Hergen and Föcker,
Manuel and Albers, Nicola and Bühlmeier, Judith and Hinney, Anke and Libuda, Lars
and Hebebrand, Johannes}, year={2021} }'
chicago: 'Peters, Triinu, Jochen Antel, Roaa Naaresh, Björn-Hergen Laabs, Manuel
Föcker, Nicola Albers, Judith Bühlmeier, Anke Hinney, Lars Libuda, and Johannes
Hebebrand. “Suggestive Evidence for Causal Effect of Leptin Levels on Risk for
Anorexia Nervosa: Results of a Mendelian Randomization Study.” Frontiers in
Genetics 12 (2021). https://doi.org/10.3389/fgene.2021.733606.'
ieee: 'T. Peters et al., “Suggestive Evidence for Causal Effect of Leptin
Levels on Risk for Anorexia Nervosa: Results of a Mendelian Randomization Study,”
Frontiers in Genetics, vol. 12, 2021, doi: 10.3389/fgene.2021.733606.'
mla: 'Peters, Triinu, et al. “Suggestive Evidence for Causal Effect of Leptin Levels
on Risk for Anorexia Nervosa: Results of a Mendelian Randomization Study.” Frontiers
in Genetics, vol. 12, Frontiers Media SA, 2021, doi:10.3389/fgene.2021.733606.'
short: T. Peters, J. Antel, R. Naaresh, B.-H. Laabs, M. Föcker, N. Albers, J. Bühlmeier,
A. Hinney, L. Libuda, J. Hebebrand, Frontiers in Genetics 12 (2021).
date_created: 2022-07-06T15:10:40Z
date_updated: 2022-08-30T13:11:49Z
department:
- _id: '35'
doi: 10.3389/fgene.2021.733606
intvolume: ' 12'
keyword:
- Genetics (clinical)
- Genetics
- Molecular Medicine
language:
- iso: eng
publication: Frontiers in Genetics
publication_identifier:
issn:
- 1664-8021
publication_status: published
publisher: Frontiers Media SA
status: public
title: 'Suggestive Evidence for Causal Effect of Leptin Levels on Risk for Anorexia
Nervosa: Results of a Mendelian Randomization Study'
type: journal_article
user_id: '88682'
volume: 12
year: '2021'
...