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Akademický článek

CX-5461 causes nucleolar compaction, alteration of peri- and intranucleolar chromatin arrangement, an increase in both heterochromatin and DNA damage response

Autor: Luc Snyers, Sylvia Laffer, Renate Löhnert, Klara Weipoltshammer, Christian Schöfer

Publikováno v: Scientific Reports, Vol 12, Iss 1, Pp 1-15 (2022)

Abstract In this study, we characterize the changes in nucleolar morphology and its dynamics induced by the recently introduced compound CX-5461, an inhibitor of ribosome synthesis. Time-lapse imaging, immunofluorescence and ultrastructural analysis

Externí odkaz: https://doaj.org/article/5f710e763361427892274b73686d9c71

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LEM4/ANKLE-2 deficiency impairs post-mitotic re-localization of BAF, LAP2α and LaminA to the nucleus, causes nuclear envelope instability in telophase and leads to hyperploidy in HeLa cells

Autor: Sylvia Laffer, Luc Snyers, Klara Weipoltshammer, Renate Erhart, Christian Schöfer, Oliver Pusch

Publikováno v: European journal of cell biology. 97(1)

The human LEM-domain protein family is involved in fundamental aspects of nuclear biology. The LEM-domain interacts with the barrier-to-autointegration factor (BAF), which itself binds DNA. LEM-domain proteins LAP2, emerin and MAN1 are proteins of th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::105b1ceb4f9d23127387480199f964c8
https://pubmed.ncbi.nlm.nih.gov/29254732

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Distinct chromatin signature of histone H3 variant H3.3 in human cells

Autor: Klara Weipoltshammer, Luc Snyers, Marlene Almeder, Christian Schöfer, Anja Stoisser, Gordin Zupkovitz, Marianne Fliesser

Publikováno v: Nucleus

Actively transcribed regions of the genome have been found enriched for the histone H3 variant H3.3. This variant is incorporated into nucleosomes throughout the cell cycle whereas the canonical isoforms are predominately deposited in association wit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::43407f39faeeb4d083b39e54871a3d0e
https://doi.org/10.4161/nucl.36229

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Lamina-associated polypeptide 2α forms complexes with heat shock proteins Hsp70 and Hsc70 in vivo

Autor: Christian Schöfer, Luc Snyers

Publikováno v: Biochemical and Biophysical Research Communications. 368:767-771

Lamina-associated polypeptide 2alpha (LAP2alpha), one of the alternatively spliced isoforms of the LAP2 gene, is a nucleoplasmic protein which forms oligomers and presumably associates to chromosomes via the LEM- and LEM-like regions. To characterize

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11c7ad4c2d401328b973fc7ca1fd5d15
https://doi.org/10.1016/j.bbrc.2008.01.139

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Lamina-associated Polypeptide 2-α Forms Homo-trimers via Its C Terminus, and Oligomerization Is Unaffected by a Disease-causing Mutation

Autor: Roland Foisner, Darko Skegro, Luc Snyers, Barbara Korbei, Christian Schöfer, Thomas Dechat, Sylvia Vlcek, Olga Mayans, Andreas Gajewski

Publikováno v: Journal of Biological Chemistry. 282:6308-6315

The nucleoplasmic protein, Lamina-associated polypeptide (LAP) 2alpha, is one of six alternatively spliced products of the LAP2gene, which share a common N-terminal region. In contrast to the other isoforms, which also share most of their C termini,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e90a290da6af1e48536f6c8a743490c
https://doi.org/10.1074/jbc.m605782200

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A Mutation in the First Ligand-Binding Repeat of the Human Very-Low-Density Lipoprotein Receptor Results in High-Affinity Binding of the Single V1 Module to Human Rhinovirus 2

Autor: Luc Snyers, Nathalie Landstetter, Stephane Nizet, Dieter Blaas, Juergen Wruss

Publikováno v: Journal of Virology. 79:14730-14736

Minor group human rhinoviruses (HRVs) bind members of the low-density lipoprotein receptor family for cell entry. The ligand-binding domains of these membrane proteins are composed of various numbers of direct repeats of about 40 amino acids in lengt

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8914a5bd348d70e4ca5a5eb77a671e48
https://doi.org/10.1128/jvi.79.23.14730-14736.2005

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Neutralization of a common cold virus by concatemers of the third ligand binding module of the VLDL-receptor strongly depends on the number of modules

Autor: Dieter Blaas, Juergen Wruss, Luc Snyers, Rosita Moser, Jesús Angulo, Hanne Peters, Thomas Peters

Publikováno v: Virology. 338:259-269

Concatemers of various numbers of the third ligand binding repeat of human very-low density lipoprotein receptor arranged in tandem were fused to maltose-binding protein and expressed as soluble polypeptides. These artificial receptors protected HeLa

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b363b06bf8b636d1661e4db8504a70b8
https://doi.org/10.1016/j.virol.2005.05.016

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The Minor Receptor Group of Human Rhinovirus (HRV) Includes HRV23 and HRV25, but the Presence of a Lysine in the VP1 HI Loop Is Not Sufficient for Receptor Binding

Autor: Dieter Blaas, Tapani Hovi, Luc Snyers, Pia Laine, Irene Goesler, Manuela Reithmayer, Merja Roivainen, Marketa Vlasak

Publikováno v: Journal of Virology. 79:7389-7395

Human rhinoviruses (HRVs), the main causative agents of common cold, were originally classified as acid-sensitive picornaviruses (34). Later, based on competition for cellular binding sites, two different groups of viruses using nonidentical receptor

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f534a380b7ed292bd53176f0d28728c
https://doi.org/10.1128/jvi.79.12.7389-7395.2005

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Identification of the Human Rhinovirus Serotype 1A Binding Site on the Murine Low-Density Lipoprotein Receptor by Using Human-Mouse Receptor Chimeras

Autor: Dieter Blaas, Peter Hinterdorfer, Barbara Herdy, Luc Snyers, Manuela Reithmayer

Publikováno v: Journal of Virology. 78:6766-6774

Human rhinovirus serotype 1A (HRV1A) binds more strongly to the mouse low-density lipoprotein receptor (LDLR) than to the human homologue (M. Reithmayer, A. Reischl, L. Snyers, and D. Blaas, J. Virol. 76: 6957-6965, 2002). Here, we used this fact to

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08b0a974f2be6ec58f3942ee3c4da2c3
https://doi.org/10.1128/jvi.78.13.6766-6774.2004

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Species-Specific Receptor Recognition by a Minor-Group Human Rhinovirus (HRV): HRV Serotype 1A Distinguishes between the Murine and the Human Low-Density Lipoprotein Receptor

Autor: Andrea Reischl, Manuela Reithmayer, Luc Snyers, Dieter Blaas

Publikováno v: Journal of Virology. 76:6957-6965

Human rhinoviruses (HRV) of the minor receptor group use several members of the low-density lipoprotein receptor superfamily for cell entry. These proteins are evolutionarily highly conserved throughout species and are almost ubiquitously expressed.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e74a30c0a76719f7c62b0b6a283416a4
https://doi.org/10.1128/jvi.76.14.6957-6965.2002

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