Zobrazeno 1 - 10
of 45
pro vyhledávání: '"Hendrik R A, Jonker"'
Autor:
Matthias S. Leisegang, Jasleen Kaur Bains, Sandra Seredinski, James A. Oo, Nina M. Krause, Chao-Chung Kuo, Stefan Günther, Nevcin Sentürk Cetin, Timothy Warwick, Can Cao, Frederike Boos, Judit Izquierdo Ponce, Shaza Haydar, Rebecca Bednarz, Chanil Valasarajan, Dominik C. Fuhrmann, Jens Preussner, Mario Looso, Soni S. Pullamsetti, Marcel H. Schulz, Hendrik R. A. Jonker, Christian Richter, Flávia Rezende, Ralf Gilsbach, Beatrice Pflüger-Müller, Ilka Wittig, Ingrid Grummt, Teodora Ribarska, Ivan G. Costa, Harald Schwalbe, Ralf P. Brandes
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-20 (2022)
Using a composite bioinformatics approach, the DNA:DNA:RNA triplex-forming lncRNAs HIF1α-AS1 was identified in human endothelial cells which recruits an epigenetic silencing complex to limit expression of triplex target genes.
Externí odkaz:
https://doaj.org/article/c3f7ecd225714cd98fa4bafc76a4baa2
Autor:
Amparo Garcia-Lopez, Francesca Tessaro, Hendrik R. A. Jonker, Anna Wacker, Christian Richter, Arnaud Comte, Nikolaos Berntenis, Roland Schmucki, Klas Hatje, Olivier Petermann, Gianpaolo Chiriano, Remo Perozzo, Daniel Sciarra, Piotr Konieczny, Ignacio Faustino, Guy Fournet, Modesto Orozco, Ruben Artero, Friedrich Metzger, Martin Ebeling, Peter Goekjian, Benoît Joseph, Harald Schwalbe, Leonardo Scapozza
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Spinal muscular atrophy (SMA) is an autosomal recessive disorder with no present cure. Here the authors perform an in vitro screening leading to the identification of a small molecule that alters the conformational dynamics of the TSL2 RNA structure
Externí odkaz:
https://doaj.org/article/cc1752fb9d394b0fb636e7fca670afcc
Autor:
Lia-Raluca Olari, Richard Bauer, Marta Gil Miró, Verena Vogel, Laura Cortez Rayas, Rüdiger Groß, Andrea Gilg, Raphael Klevesath, Armando A. Rodríguez Alfonso, Kübra Kaygisiz, Ulrich Rupp, Pradeep Pant, Joel Mieres-Pérez, Lena Steppe, Ramona Schäffer, Lena Rauch-Wirth, Carina Conzelmann, Janis A. Müller, Fabian Zech, Fabian Gerbl, Jana Bleher, Nico Preising, Ludger Ständker, Sebastian Wiese, Dietmar R. Thal, Christian Haupt, Hendrik R. A. Jonker, Manfred Wagner, Elsa Sanchez-Garcia, Tanja Weil, Steffen Stenger, Marcus Fändrich, Jens von Einem, Clarissa Read, Paul Walther, Frank Kirchhoff, Barbara Spellerberg, Jan Münch
Publikováno v:
Cellular and Molecular Life Sciences
Antimicrobial peptides (AMPs) are major components of the innate immune defense. Accumulating evidence suggests that the antibacterial activity of many AMPs is dependent on the formation of amyloid-like fibrils. To identify novel fibril forming AMPs,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9bbe8105cd8417e0164731a868a792e3
https://www.ncbi.nlm.nih.gov/pubmed/37198527
https://www.ncbi.nlm.nih.gov/pubmed/37198527
Autor:
Hendrik R. A. Jonker, Birgit Tiemann, Hans Bakker, Aleksandra Shcherbakova, Krishna Saxena, Harald Schwalbe
Publikováno v:
Angewandte Chemie (International Ed. in English)
Despite the great interest in glycoproteins, structural information reporting on conformation and dynamics of the sugar moieties are limited. We present a new biochemical method to express proteins with glycans that are selectively labeled with NMR
Autor:
Jennifer Vögele, Jasleen Kaur Bains, Sophie Marianne Korn, Tom Landgraf, Hendrik R. A. Jonker, Daniel Hymon, Robbin Schnieders, Daniel Mathieu, Sabrina Toews, Nadide Altincekic, Bozana Knezic, Katharina F. Hohmann, J Tassilo Grün, Julia Wirmer-Bartoschek, Frank Löhr, Elke Duchardt-Ferner, Anna Wacker, Kerstin Witt, Dennis J. Pyper, Alexey Sudakov, Jens Wöhnert, Boris Fürtig, Julia E. Weigand, Stephen A. Peter, Betül Ceylan, Harald Schwalbe, Oliver Binas, Martin Hengesbach, Elke Stirnal, Andreas Schlundt, Nusrat S. Qureshi, Christian Richter, Jan Ferner
Publikováno v:
Biomolecular Nmr Assignments
The stem-loop (SL1) is the 5'-terminal structural element within the single-stranded SARS-CoV-2 RNA genome. It is formed by nucleotides 7–33 and consists of two short helical segments interrupted by an asymmetric internal loop. This architecture is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ca8d91e354fdc03948fa1f0e0e6af4a
http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/63569
http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/63569
Autor:
Nusrat Shahin, Qureshi, Tobias, Matzel, Erhan Can, Cetiner, Robbin, Schnieders, Hendrik R A, Jonker, Harald, Schwalbe, Boris, Fürtig
Publikováno v:
Nucleic Acids Research
The ribosomal S1 protein (rS1) is indispensable for translation initiation in Gram-negative bacteria. rS1 is a multidomain protein that acts as an RNA chaperone and ensures that mRNAs can bind the ribosome in a single-stranded conformation, which cou
Autor:
Hendrik R. A. Jonker, Sandra Schreiber, Krishna Saxena, Anita Marchfelder, Nina Kubatova, Harald Schwalbe, Verena Vogel, Christian Richter
Publikováno v:
ChemBioChem. 21:149-156
Past sequencing campaigns overlooked small proteins as they seemed to be irrelevant due to their small size. However, their occurrence is widespread, and there is growing evidence that these small proteins are in fact functionally very important in o
Autor:
Yvonne Hackmann, Sabine Strahl, Gunter Stier, Klemens Wild, Sofia Mortensen, Antonija Grbavac, Irmgard Sinning, Andrea Schott, Ewa Zatorska, Antonella Chiapparino, Krishna Saxena, Harald Schwalbe, Hendrik R. A. Jonker
Publikováno v:
eLife, Vol 9 (2020)
'eLife ', vol: 9, pages: e61189-1-e61189-23 (2020)
'eLife ', vol: 9, pages: e61189-1-e61189-23 (2020)
Protein O-mannosyltransferases (PMTs) represent a conserved family of multispanning endoplasmic reticulum membrane proteins involved in glycosylation of S/T-rich protein substrates and unfolded proteins. PMTs work as dimers and contain a luminal MIR
Autor:
Antonija Grbavac, Sofia Mortensen, Hendrik R. A. Jonker, Yvonne Hackmann, Sabine Strahl, Klemens Wild, Ewa Zatorska, Antonella Chiapparino, Irmgard Sinning, Gunter Stier, Krishna Saxena, Andrea Schott, Harald Schwalbe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5238f6548e692b7464270ec625128a4b
https://doi.org/10.7554/elife.61189.sa2
https://doi.org/10.7554/elife.61189.sa2
Autor:
Sabine Brantl, Ruth A. Schmitz, Gabriele Klug, Christian Richter, Wolfgang R. Streit, Anita Marchfelder, Vladislav Yu. Orekhov, Elena Evguenieva-Hackenberg, Maxim Mayzel, Wolfgang R. Hess, Dennis J. Pyper, Hendrik R. A. Jonker, Jörg Soppa, Harald Schwalbe, Krishna Saxena, Laura Remmel, Monika Fuxreiter, Nina Kubatova
Publikováno v:
Chembiochem
Proteins encoded by small open reading frames (sORFs) have a widespread occurrence in diverse microorganisms and can be of high functional importance. However, due to annotation biases and their technically challenging direct detection, these small p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f651b5f53b174c9845675c20f4697053
http://hdl.handle.net/11577/3365539
http://hdl.handle.net/11577/3365539