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439 results on '"Boehringer, Daniel"'

5. An evolutionarily conserved mechanism controls reversible amyloids of pyruvate kinase via pH-sensing regions

Author

Cereghetti, Gea, Kissling, Vera M., Koch, Lisa M., Arm, Alexandra, Schmidt, Claudia C., Thüringer, Yannik, Zamboni, Nicola, Afanasyev, Pavel, Linsenmeier, Miriam, Eichmann, Cédric, Kroschwald, Sonja, Zhou, Jiangtao, Cao, Yiping, Pfizenmaier, Dorota M., Wiegand, Thomas, Cadalbert, Riccardo, Gupta, Govind, Boehringer, Daniel, Knowles, Tuomas P.J., Mezzenga, Raffaele, Arosio, Paolo, Riek, Roland, and Peter, Matthias

Published
2024
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9. Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER

Author

Lee, Jae Ho, Jomaa, Ahmad, Chung, SangYoon, Hwang Fu, Yu-Hsien, Qian, Ruilin, Sun, Xuemeng, Hsieh, Hao-Hsuan, Chandrasekar, Sowmya, Bi, Xiaotian, Mattei, Simone, Boehringer, Daniel, Weiss, Shimon, Ban, Nenad, and Shan, Shu-Ou

Subjects
Biochemistry and Cell Biology, Biological Sciences, Generic health relevance
Abstract

The conserved signal recognition particle (SRP) cotranslationally delivers ~30% of the proteome to the eukaryotic endoplasmic reticulum (ER). The molecular mechanism by which eukaryotic SRP transitions from cargo recognition in the cytosol to protein translocation at the ER is not understood. Here, structural, biochemical, and single-molecule studies show that this transition requires multiple sequential conformational rearrangements in the targeting complex initiated by guanosine triphosphatase (GTPase)-driven compaction of the SRP receptor (SR). Disruption of these rearrangements, particularly in mutant SRP54G226E linked to severe congenital neutropenia, uncouples the SRP/SR GTPase cycle from protein translocation. Structures of targeting intermediates reveal the molecular basis of early SRP-SR recognition and emphasize the role of eukaryote-specific elements in regulating targeting. Our results provide a molecular model for the structural and functional transitions of SRP throughout the targeting cycle and show that these transitions provide important points for biological regulation that can be perturbed in genetic diseases.

Published
2021

13. Classification of Histologically Proven Inflammation in Clinically Inactive Corneal Scars: Implications for Graft Outcomes After Penetrating Keratoplasty.

Author

Schliffka, Max, Siegel, Helena, Auw-Haedrich, Claudia, van Oterendorp, Christian, Boehringer, Daniel, and Reinhard, Thomas

Subjects
GRAFT rejection, HERPES simplex virus, SCARS, CORNEA, CORNEA surgery
Abstract

Background/Objectives: Clinically inactive corneal scars have repeatedly been shown to exhibit histological inflammation. This study aimed to evaluate the degree of histological inflammation in clinically inactive corneal scars of different origins and its correlation with graft rejection and failure following penetrating keratoplasty. Methods: The study included 205 primary corneal explants with clinically inactive central scars resulting from herpes simplex virus keratitis (HSV, n = 55), keratoconus (n = 39), mechanical trauma (n = 27), scrophulosa (n = 22) or other/unknown causes (n = 62). Central histological sections were categorized by the degree of inflammation, and an overall inflammation score (IS) was calculated. Results: HSV-associated scars exhibited a trend towards more graft rejection with higher IS (p = 0.074). Keratoconus-associated scars showed no IS-dependent differences in graft rejection or failure. The rejection rate in this group was 13/39. Scars resulting from mechanical trauma, such as perforating injuries, demonstrated a trend towards higher graft rejection (p = 0.15) and failure rates (p = 0.089) with increasing IS. The rejection rate in this group was 11/27. Scrophulosa-associated scars had significantly higher graft rejection rates (p = 0.041) at a lower cut-off of 0.06 compared to the cut-off of 0.36 for the other groups. Scars of other or unknown causes showed no IS-dependent differences in graft rejection or failure. Conclusions: Histological inflammation in HSV scars and scars resulting from mechanical trauma appeared to contribute to graft rejection. Despite low IS, the rejection rate in keratoconus scars and scars following mechanical trauma was unexpectedly high, indicating the presence of other influencing factors. While some correlations did not reach statistical significance due to small sample sizes in the subgroups, the observed trends should be considered clinically relevant. The study may have been "underpowered", as histopathologically inflamed specimens with clinically inactive corneal scars are relatively rare. [ABSTRACT FROM AUTHOR]

Published
2025
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24. An inhibitory segment within G-patch activators tunes Prp43-ATPase activity during ribosome assembly

Author

Portugal-Calisto, Daniela; https://orcid.org/0000-0003-1591-5812, Geiger, Alexander Gregor; https://orcid.org/0000-0002-1372-1929, Rabl, Julius, Vadas, Oscar; https://orcid.org/0000-0003-3511-6479, Oborská-Oplová, Michaela; https://orcid.org/0000-0003-0976-4341, Mazur, Jarosław; https://orcid.org/0000-0002-1677-011X, Richina, Federica, Klingauf-Nerurkar, Purnima, Michel, Erich; https://orcid.org/0000-0002-5252-5429, Leitner, Alexander; https://orcid.org/0000-0003-4126-0725, Boehringer, Daniel; https://orcid.org/0000-0002-6666-8447, Panse, Vikram Govind; https://orcid.org/0000-0002-4770-7068, Portugal-Calisto, Daniela; https://orcid.org/0000-0003-1591-5812, Geiger, Alexander Gregor; https://orcid.org/0000-0002-1372-1929, Rabl, Julius, Vadas, Oscar; https://orcid.org/0000-0003-3511-6479, Oborská-Oplová, Michaela; https://orcid.org/0000-0003-0976-4341, Mazur, Jarosław; https://orcid.org/0000-0002-1677-011X, Richina, Federica, Klingauf-Nerurkar, Purnima, Michel, Erich; https://orcid.org/0000-0002-5252-5429, Leitner, Alexander; https://orcid.org/0000-0003-4126-0725, Boehringer, Daniel; https://orcid.org/0000-0002-6666-8447, and Panse, Vikram Govind; https://orcid.org/0000-0002-4770-7068

Abstract

Mechanisms by which G-patch activators tune the processive multi-tasking ATP-dependent RNA helicase Prp43 (DHX15 in humans) to productively remodel diverse RNA:protein complexes remain elusive. Here, a comparative study between a herein and previously characterized activators, Tma23 and Pxr1, respectively, defines segments that organize Prp43 function during ribosome assembly. In addition to the activating G-patch, we discover an inhibitory segment within Tma23 and Pxr1, I-patch, that restrains Prp43 ATPase activity. Cryo-electron microscopy and hydrogen-deuterium exchange mass spectrometry show how I-patch binds to the catalytic RecA-like domains to allosterically inhibit Prp43 ATPase activity. Tma23 and Pxr1 contain dimerization segments that organize Prp43 into higher-order complexes. We posit that Prp43 function at discrete locations on pre-ribosomal RNA is coordinated through toggling interactions with G-patch and I-patch segments. This could guarantee measured and timely Prp43 activation, enabling precise control over multiple RNA remodelling events occurring concurrently during ribosome formation.

Published
2024

35. Retinal layer segmentation in multiple sclerosis: a systematic review and meta-analysis

Author

Aktas, Orhan, Albrecht, Philipp, Ashworth, Jane, Asgari, Nasrin, Balcer, Laura, Balk, Lisanne, Black, Graeme, Boehringer, Daniel, Behbehani, Raed, Benson, Leslie, Bermel, Robert, Bernard, Jacqueline, Brandt, Alexander, Burton, Jodie, Calabresi, Peter, Calkwood, Jonathan, Cordano, Christian, Costello, Fiona, Courtney, Ardith, Cruz-Herranz, Andrés, Diem, Ricarda, Daly, Avril, Dollfus, Helene, Fasser, Christina, Finke, Carsten, Frederiksen, Jette, Frohman, Elliot, Frohman, Teresa, Garcia-Martin, Elenaw, Suárez, Inés González, Pihl-Jensen, Gorm, Graves, Jennifer, Green, Ari, Havla, Joachim, Hemmer, Bernhard, Huang, Su-Chun, Imitola, Jaime, Jiang, Hong, Keegan, David, Kildebeck, Eric, Klistorner, Alexander, Knier, Benjamin, Kolbe, Scott, Korn, Thomas, LeRoy, Bart, Leocani, Letizia, Leroux, Dorothee, Levin, Netta, Liskova, Petra, Lorenz, Birgit, Preiningerova, Jana Lizrova, Martínez-Lapiscina, Elena Hernández, Mikolajczak, Janine, Montalban, Xavier, Morrow, Mark, Nolan, Rachel, Oberwahrenbrock, Timm, Oertel, Frederike Cosima, Oreja-Guevara, Celia, Osborne, Benjamin, Outteryck, Olivier, Papadopoulou, Athina, Paul, Friedemann, Petzold, Axel, Ringelstein, Marius, Saidha, Shiv, Sanchez-Dalmau, Bernardo, Sastre-Garriga, Jaume, Schippling, Sven, Shin, Robert, Shuey, Neil, Soelberg, Kerstin, Toosy, Ahmed, Torres, Rubén, Vidal-Jordana, Angela, Villoslada, Pablo, Waldman, Amy, White, Owen, Yeh, Ann, Wong, Sui, Zimmermann, Hanna, Balcer, Laura J, Calabresi, Peter A, Frohman, Teresa C, Frohman, Elliot M, Martinez-Lapiscina, Elena H, Green, Ari J, Kardon, Randy, Vermersch, Patrik, and Balk, Lisanne J

Published
2017
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41. Unique features of mammalian mitochondrial translation initiation revealed by cryo-EM

Author

Kummer, Eva, Leibundgut, Marc, Rackham, Oliver, Lee, Richard G., Boehringer, Daniel, Filipovska, Aleksandra, and Ban, Nenad

Subjects
Research, Mitochondria -- Research, Translation (Genetics) -- Research, Messenger RNA -- Research, Genetic research, Bacteria, Peptides, Transfer RNA, Electron microscopy, RNA, Codons, Proteins, Membrane proteins, Microscopy, Protein synthesis, Resveratrol, Nucleotides
Abstract

Author(s): Eva Kummer [sup.1] , Marc Leibundgut [sup.1] , Oliver Rackham [sup.2] , Richard G. Lee [sup.2] , Daniel Boehringer [sup.1] , Aleksandra Filipovska [sup.2] , Nenad Ban [sup.1] Author [...], Mitochondria maintain their own specialized protein synthesis machinery, which in mammals is used exclusively for the synthesis of the membrane proteins responsible for oxidative phosphorylation.sup.1,2. The initiation of protein synthesis in mitochondria differs substantially from bacterial or cytosolic translation systems. Mitochondrial translation initiation lacks initiation factor 1, which is essential in all other translation systems from bacteria to mammals.sup.3,4. Furthermore, only one type of methionyl transfer RNA (tRNA.sup.Met) is used for both initiation and elongation.sup.4,5, necessitating that the initiation factor specifically recognizes the formylated version of tRNA.sup.Met (fMet-tRNA.sup.Met). Lastly, most mitochondrial mRNAs do not possess 5' leader sequences to promote mRNA binding to the ribosome.sup.2. There is currently little mechanistic insight into mammalian mitochondrial translation initiation, and it is not clear how mRNA engagement, initiator-tRNA recruitment and start-codon selection occur. Here we determine the cryo-EM structure of the complete translation initiation complex from mammalian mitochondria at 3.2 Å. We describe the function of an additional domain insertion that is present in the mammalian mitochondrial initiation factor 2 (mtIF2). By closing the decoding centre, this insertion stabilizes the binding of leaderless mRNAs and induces conformational changes in the rRNA nucleotides involved in decoding. We identify unique features of mtIF2 that are required for specific recognition of fMet-tRNA.sup.Met and regulation of its GTPase activity. Finally, we observe that the ribosomal tunnel in the initiating ribosome is blocked by insertion of the N-terminal portion of mitochondrial protein mL45, which becomes exposed as the ribosome switches to elongation mode and may have an additional role in targeting of mitochondrial ribosomes to the protein-conducting pore in the inner mitochondrial membrane.A cryo-electron microscopy structure of the mammalian mitochondrial translation initiation complex reveals unique features that are necessary to initiate mitochondrial translation and highlights a possible membrane-targeting peptide.

Published
2018
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46. Ribosomal protein RPL39L is an efficiency factor in the cotranslational folding of proteins with alpha helical domains

Author

Banerjee, Arka, primary, Ataman, Meric, additional, Smialek, Maciej Jerzy, additional, Mookherjee, Debdatto, additional, Rabl, Julius, additional, Mironov, Aleksei, additional, Mues, Lea, additional, Enkler, Ludovic, additional, Coto-Llerena, Mairene, additional, Schmidt, Alexander, additional, Boehringer, Daniel, additional, Piscuoglio, Salvatore, additional, Spang, Anne, additional, Mittal, Nitish, additional, and Zavolan, Mihaela, additional

Published
2023
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47. Architecture of human mTOR complex 1

Author

Aylett, Christopher H. S., Sauer, Evelyn, Imseng, Stefan, Boehringer, Daniel, Hall, Michael N., Ban, Nenad, and Maier, Timm

Published
2016

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