Zobrazeno 1 - 10 of 25 pro vyhledávání: '"Jeremy J. Keusch"'
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Akademický článek
Evolutionary plasticity of the NHL domain underlies distinct solutions to RNA recognition
Autor: Pooja Kumari, Florian Aeschimann, Dimos Gaidatzis, Jeremy J. Keusch, Pritha Ghosh, Anca Neagu, Katarzyna Pachulska-Wieczorek, Janusz M. Bujnicki, Heinz Gut, Helge Großhans, Rafal Ciosk
Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
The C. elegans LIN-41 and its homologs, including human TRIM71/LIN41, contain the RNA binding NHL domain. Here the authors combine computational analysis, structural biology and in vivo studies, to explain how these proteins bind RNA and how rapid ev
Externí odkaz: https://doaj.org/article/5a8959f36aff458cb62b172ede6df265
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2
Influenza virus uses transportin 1 for vRNP debundling during cell entry
Autor: Ulrike Kutay, Yasuyuki Miyake, Laure Decamps, Yohei Yamauchi, Sho Iketani, Ari Helenius, Heinz Gut, Hung Ho-Xuan, Jeremy J. Keusch
Publikováno v: Miyake, Y, Keusch, J J, Decamps, L, Ho-Xuan, H, Iketani, S, Gut, H, Kutay, U, Helenius, A & Yamauchi, Y 2019, ' Influenza virus uses transportin 1 for vRNP debundling during cell entry ', Nature Microbiology, vol. 4, no. 4, pp. 578-586 . https://doi.org/10.1038/s41564-018-0332-2
Influenza A virus is a pathogen of great medical impact. To develop novel antiviral strategies, it is essential to understand the molecular aspects of virus–host cell interactions in detail. During entry, the viral ribonucleoproteins (vRNPs) that c
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::099d93fb5bb5086399d65a23d89fd015
https://doi.org/10.1038/s41564-018-0332-2
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3
Evolutionary plasticity of the NHL domain underlies distinct solutions to RNA recognition
Autor: Dimos Gaidatzis, Pooja Kumari, Anca Neagu, Pritha Ghosh, Janusz M. Bujnicki, Rafal Ciosk, Heinz Gut, Katarzyna Pachulska-Wieczorek, Helge Großhans, Jeremy J. Keusch, Florian Aeschimann
Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
Nature Communications
RNA-binding proteins regulate all aspects of RNA metabolism. Their association with RNA is mediated by RNA-binding domains, of which many remain uncharacterized. A recently reported example is the NHL domain, found in prominent regulators of cellular
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd577be1f99c457faf98f7e78c486366
https://doaj.org/article/5a8959f36aff458cb62b172ede6df265
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5
The Sir4 H‐BRCT domain interacts with phospho‐proteins to sequester and repress yeast heterochromatin
Autor: Heinz Gut, Jeremy J. Keusch, Kiran Challa, Ishan Deshpande, Susan M. Gasser, Vytautas Iesmantavicius
Publikováno v: EMBO J
In Saccharomyces cerevisiae, the silent information regulator (SIR) proteins Sir2/3/4 form a complex that suppresses transcription in subtelomeric regions and at the homothallic mating-type (HM) loci. Here, we identify a non-canonical BRCA1 C-termina
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf21c0b74c63fc6932fc6774d5189ad8
https://europepmc.org/articles/PMC6792019/
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6
Structural insights into HDAC6 tubulin deacetylation and its selective inhibition
Autor: Patrick Matthias, Daniel Hess, Makoto Saito, Longlong Wang, Heinz Gut, Paul Helquist, Yasuyuki Miyake, Xiaoning Wang, Jeremy J. Keusch, Bruce J. Melancon
Publikováno v: Nature Chemical Biology. 12:748-754
We report crystal structures of zebrafish histone deacetylase 6 (HDAC6) catalytic domains in tandem or as single domains in complex with the (R) and (S) enantiomers of trichostatin A (TSA) or with the HDAC6-specific inhibitor nexturastat A. The tande
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1c21daff64cd5d4f0396a8a35bafb79e
https://doi.org/10.1038/nchembio.2140
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7
Influenza virus uses transportin 1 for vRNP debundling during cell entry
Autor: Yasuyuki, Miyake, Jeremy J, Keusch, Laure, Decamps, Hung, Ho-Xuan, Sho, Iketani, Heinz, Gut, Ulrike, Kutay, Ari, Helenius, Yohei, Yamauchi
Publikováno v: Nature microbiology. 4(4)
Influenza A virus is a pathogen of great medical impact. To develop novel antiviral strategies, it is essential to understand the molecular aspects of virus-host cell interactions in detail. During entry, the viral ribonucleoproteins (vRNPs) that car
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d02d915ba777b71e7d9e50279d907243
https://pubmed.ncbi.nlm.nih.gov/30692667
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8
Dimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formation
Autor: Mariano Oppikofer, Susan M. Gasser, Markus Hassler, Andreas G. Ladurner, Jeremy J. Keusch, Heinz Gut, Stephanie Kueng
Publikováno v: The EMBO journal
Gene silencing in budding yeast relies on the binding of the Silent Information Regulator (Sir) complex to chromatin, which is mediated by extensive interactions between the Sir proteins and nucleosomes. Sir3, a divergent member of the AAA+ ATPase-li
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab4ac7c2affb27f8e94aa24b9b6e7bd4
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9
Peters Plus syndrome is a new congenital disorder of glycosylation and involves defective Omicron-glycosylation of thrombospondin type 1 repeats
Autor: Daniel Hess, Saskia A J Lesnik Oberstein, Jeremy J. Keusch, Jan Hofsteenge, Raoul C.M. Hennekam
Publikováno v: Journal of biological chemistry, 283(12), 7354-7360. American Society for Biochemistry and Molecular Biology Inc.
Peters Plus syndrome is an autosomal recessive disorder characterized by anterior eye chamber defects, disproportionate short stature, developmental delay, and cleft lip and/or palate. It is caused by splice site mutations in what was thought to be a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63a1e4a753ed5aa834a7164d504e61c2
https://doi.org/10.1074/jbc.m710251200
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10
Structural Basis of Mec1-Ddc2-RPA Assembly and Activation on Single-Stranded DNA at Sites of Damage
Autor: Kenji Shimada, Andrew Seeber, Heinz Gut, Susan M. Gasser, Ishan Deshpande, Jeremy J. Keusch
Publikováno v: Molecular Cell. 68:431-445.e5
Mec1-Ddc2 (ATR-ATRIP) is a key DNA-damage-sensing kinase that is recruited through the single-stranded (ss) DNA-binding replication protein A (RPA) to initiate the DNA damage checkpoint response. Activation of ATR-ATRIP in the absence of DNA damage i
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f282b3e01a6f5dacb7dd8d77cbe92326
https://doi.org/10.1016/j.molcel.2017.09.019
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