Zobrazeno 1 - 10
of 110
pro vyhledávání: '"Yves A. Muller"'
Autor:
Mark Kriegel, Yves A. Muller
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-14 (2023)
Abstract By mediating interatomic interactions, water molecules play a major role in protein–protein, protein–DNA and protein–ligand interfaces, significantly affecting affinity and specificity. This notwithstanding, explicit water molecules ar
Externí odkaz:
https://doaj.org/article/403b5606d9794305a3ad887b9c87b35c
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
Abstract Protein stability limitations often hamper the exploration of proteins as drug targets. Here, we show that the application of PROSS server algorithms to the ligand-binding domain of human estrogen receptor alpha (hERα) enabled the developme
Externí odkaz:
https://doaj.org/article/c81ef6036eec4309827b94dcc2a035d3
Autor:
Franziska Rothemund, Myriam Scherer, Eva-Maria Schilling, Johannes Schweininger, Yves A. Muller, Thomas Stamminger
Publikováno v:
Viruses, Vol 14, Iss 8, p 1626 (2022)
The human cytomegalovirus (CMV) immediate early 1 (IE1) protein has evolved as a multifunctional antagonist of intrinsic and innate immune mechanisms. In addition, this protein serves as a transactivator and potential genome maintenance protein. Rece
Externí odkaz:
https://doaj.org/article/75a7d6da698d4eafac098922a2e86aab
Autor:
Linda Grosche, Ilka Knippertz, Christina König, Dmytro Royzman, Andreas B. Wild, Elisabeth Zinser, Heinrich Sticht, Yves A. Muller, Alexander Steinkasserer, Matthias Lechmann
Publikováno v:
Frontiers in Immunology, Vol 11 (2020)
The CD83 molecule has been identified to be expressed on numerous activated immune cells, including B and T lymphocytes, monocytes, dendritic cells, microglia, and neutrophils. Both isoforms of CD83, the membrane-bound as well as its soluble form are
Externí odkaz:
https://doaj.org/article/fb3c408893074d5eb6e59205ef14a175
Autor:
Sewar Alkhashrom, Jintawee Kicuntod, Sigrun Häge, Johannes Schweininger, Yves A. Muller, Peter Lischka, Manfred Marschall, Jutta Eichler
Publikováno v:
Viruses, Vol 13, Iss 3, p 471 (2021)
Nuclear egress is an essential process in the replication of human cytomegalovirus (HCMV), as it enables the migration of newly formed viral capsids from the nucleus into the cytoplasm. Inhibition of the HCMV core nuclear egress complex (core NEC), c
Externí odkaz:
https://doaj.org/article/ed4e6ba6b5fc4389ab99a2045db689a7
Autor:
Manfred Marschall, Sigrun Häge, Marcus Conrad, Sewar Alkhashrom, Jintawee Kicuntod, Johannes Schweininger, Mark Kriegel, Josephine Lösing, Julia Tillmanns, Frank Neipel, Jutta Eichler, Yves A. Muller, Heinrich Sticht
Publikováno v:
Viruses, Vol 12, Iss 6, p 683 (2020)
Herpesviruses uniquely express two essential nuclear egress-regulating proteins forming a heterodimeric nuclear egress complex (core NEC). These core NECs serve as hexameric lattice-structured platforms for capsid docking and recruit viral and cellul
Externí odkaz:
https://doaj.org/article/1f7f9a819ff04dc3a8da54471832bd4c
Autor:
Jintawee Kicuntod, Sigrun Häge, Josephine Lösing, Serli Kopar, Yves A. Muller, Manfred Marschall
Publikováno v:
Antiviral Research. 212:105557
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1483458eb2585aae228b5e210934a0a7
https://doi.org/10.1016/j.antiviral.2023.105557
https://doi.org/10.1016/j.antiviral.2023.105557
Crystal structures of adenylylated and unadenylylated PIIprotein GlnK fromCorynebacterium glutamicum
Publikováno v:
Acta Crystallographica. Section D, Structural Biology
The crystal structures of adenylylated and unadenylylated GlnK, a PII protein from Corynebacterium glutamicum, indicate that adenylylation of Tyr51 in the T-loop does not interfere with the PII-typical conformational changes that occur in the T-loop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c46b2f5d57189412afe72621b41b5a9
https://doi.org/10.1107/s2059798321000735
https://doi.org/10.1107/s2059798321000735
Autor:
Claudia Egerer-Sieber, Julia Tillmanns, T. Lenac Rovis, Sewar Alkhashrom, Heinrich Sticht, Marcus Conrad, Manfred Marschall, Yves A. Muller, Sigrid Weiler, Johannes Schweininger, A. Decker, Mark Kriegel, Sigrun Häge, Josephine Lösing, Jutta Eichler
Varicella zoster virus (VZV) is a human pathogen from the α-subfamily of herpesviruses. Here, the crystal structure of the VZV Orf24-Orf27 complex is described, representing the essential viral core nuclear egress complex (NEC) that orchestrates the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cef2aa8703f45d087c216452d6a30474
https://doi.org/10.1101/2021.08.23.457313
https://doi.org/10.1101/2021.08.23.457313
Autor:
Johannes Schweininger, Mark Kriegel, Sigrun Häge, Marcus Conrad, Sewar Alkhashrom, Josephine Lösing, Sigrid Weiler, Julia Tillmanns, Claudia Egerer-Sieber, Andrea Decker, Tihana Lenac Roviš, Jutta Eichler, Heinrich Sticht, Manfred Marschall, Yves A. Muller
Publikováno v:
Journal of Biological Chemistry
Volume 298
Issue 3
The journal of biological chemistry 298(3), 101625 (2022). doi:10.1016/j.jbc.2022.101625
Volume 298
Issue 3
The journal of biological chemistry 298(3), 101625 (2022). doi:10.1016/j.jbc.2022.101625
The journal of biological chemistry 298(3), 101625 (2022). doi:10.1016/j.jbc.2022.101625
Varicella-zoster virus (VZV) is a human pathogen from the α-subfamily of herpesviruses. The VZV Orf24-Orf27 complex represents the essential viral core nuc
Varicella-zoster virus (VZV) is a human pathogen from the α-subfamily of herpesviruses. The VZV Orf24-Orf27 complex represents the essential viral core nuc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::925f7b1f9d4ebc672601c4d1e9545692
https://pubmed.ncbi.nlm.nih.gov/35074430
https://pubmed.ncbi.nlm.nih.gov/35074430