Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Marcus Fislage"'
Autor:
Mike Sleutel, Ephrem Debebe Zegeye, Ann-Katrin Llarena, Brajabandhu Pradhan, Marcus Fislage, Kristin O’Sullivan, Nani Van Gerven, Marina Aspholm, Han Remaut
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-12 (2024)
Abstract In pathogenic Bacillota, spores can form an infectious particle and can take up a central role in the environmental persistence and dissemination of disease. A poorly understood aspect of spore-mediated infection is the fibrous structures or
Externí odkaz:
https://doaj.org/article/b81f5346c8fa4f41ae18966c2b82440f
Autor:
Christian Galicia, Giambattista Guaitoli, Marcus Fislage, Christian Johannes Gloeckner, Wim Versées
Publikováno v:
eLife, Vol 13 (2024)
Roco proteins entered the limelight after mutations in human LRRK2 were identified as a major cause of familial Parkinson’s disease. LRRK2 is a large and complex protein combining a GTPase and protein kinase activity, and disease mutations increase
Externí odkaz:
https://doaj.org/article/fe28b461f98542a583630c69b7b7ff59
Publikováno v:
IUCrJ, Vol 7, Iss 4, Pp 707-718 (2020)
Single-particle cryo-EM has become an indispensable structural biology method. It requires regular access to high-resolution electron cryogenic microscopes. To fully utilize the capacity of the expensive high-resolution instruments, the time used for
Externí odkaz:
https://doaj.org/article/bf7a7f27ac3148f099068e5475a36687
Publikováno v:
IUCrJ
IUCrJ, Vol 7, Iss 4, Pp 707-718 (2020)
IUCrJ, Vol 7, Iss 4, Pp 707-718 (2020)
This paper presents a detailed assessment of the performance of the CRYO ARM 300 electron microscope in a multiuser cryo-EM facility setting. It is shown that the microscope can be used for reliable automated data collection. The strengths and weakne
Autor:
Chandra Sekhar Mandava, Joachim Frank, Zuben P. Brown, Suparna Sanyal, Marcus Fislage, Jingji Zhang, Måns Ehrenberg
Publikováno v:
Nucleic Acids Research
The GTPase EF-Tu in ternary complex with GTP and aminoacyl-tRNA (aa-tRNA) promotes rapid and accurate delivery of cognate aa-tRNAs to the ribosomal A site. Here we used cryo-EM to study the molecular origins of the accuracy of ribosome-aided recognit
Publikováno v:
Biopolymers. 105:568-579
MnmE is a multi-domain GTPase that is conserved from bacteria to man. Together with its partner protein MnmG it is involved in the synthesis of a tRNA wobble uridine modification. The orthologues of these proteins in eukaryotes are targeted to mitoch
Autor:
Els Pardon, Wim Versées, Vittorio Bellotti, Saskia Vanderhaegen, Marcus Fislage, Jan Steyaert, Katarzyna Domanska
Publikováno v:
Protein Science. 22:1349-1357
To investigate early intermediates of β2-microglobulin (β2m) amyloidogenesis, we solved the structure of β2m containing the amyloidogenic Pro32Gly mutation by X-ray crystallography. One nanobody (Nb24) that efficiently blocks fibril elongation was
Autor:
Ines Taes, Marcus Fislage, Wim Versées, André Bento-Abreu, Stephan J. Sigrist, Wim Robberecht, Katarzyna Miśkiewicz, Jaroslaw Kasprowicz, Patrik Verstreken, Liya E. Jose, Jef Swerts
Publikováno v:
Vrije Universiteit Brussel
Neuron; Vol 72
Neuron; Vol 72
Elongator protein 3 (ELP3) acetylates histones in the nucleus but also plays a role in the cytoplasm. Here, we report that in Drosophila neurons, ELP3 is necessary and sufficient to acetylate the ELKS family member Bruchpilot, an integral component o
Publikováno v:
Vrije Universiteit Brussel
Methyltransferases form a major class of tRNA-modifying enzymes that are needed for the proper functioning of tRNA. Here, the expression, purification and crystallization of two related putative tRNA methyltransferases from two kingdoms of life are r
Autor:
Saskia, Vanderhaegen, Marcus, Fislage, Katarzyna, Domanska, Wim, Versées, Els, Pardon, Vittorio, Bellotti, Jan, Steyaert
Publikováno v:
Protein science : a publication of the Protein Society. 22(10)
To investigate early intermediates of β2-microglobulin (β2m) amyloidogenesis, we solved the structure of β2m containing the amyloidogenic Pro32Gly mutation by X-ray crystallography. One nanobody (Nb24) that efficiently blocks fibril elongation was