Zobrazeno 1 - 10
of 281
pro vyhledávání: '"Roland Lill"'
Autor:
Vinzent Schulz, Ralf Steinhilper, Jonathan Oltmanns, Sven-A. Freibert, Nils Krapoth, Uwe Linne, Sonja Welsch, Maren H. Hoock, Volker Schünemann, Bonnie J. Murphy, Roland Lill
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract Maturation of iron-sulfur proteins in eukaryotes is initiated in mitochondria by the core iron-sulfur cluster assembly (ISC) complex, consisting of the cysteine desulfurase sub-complex NFS1-ISD11-ACP1, the scaffold protein ISCU2, the electro
Externí odkaz:
https://doaj.org/article/8ffd93ab41574bbc8173c92d34b5c889
Autor:
Paul J. J. Mandigers, Oliver Stehling, Manon Vos-Loohuis, Frank G. Van Steenbeek, Roland Lill, Peter A. Leegwater
Publikováno v:
Frontiers in Genetics, Vol 14 (2023)
Introduction: Hereditary necrotizing myelopathy (HNM) in young Kooiker dogs is characterized by progressive ataxia and paralysis with autosomal recessive inheritance. The basic genetic defect is unknown. We investigated the possible cause by a genome
Externí odkaz:
https://doaj.org/article/d1325bf7daab4901ab61cf1d7d57bde5
Autor:
Sven-A. Freibert, Michal T. Boniecki, Claudia Stümpfig, Vinzent Schulz, Nils Krapoth, Dennis R. Winge, Ulrich Mühlenhoff, Oliver Stehling, Miroslaw Cygler, Roland Lill
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
[2Fe-2S] protein cofactors are essential for life and are synthesized on ISCU2 scaffolds. Here, the authors show that hydrophobic interaction of two conserved N-terminal tyrosines induces ISCU2 dimerization and concomitant [2Fe-2S] cluster synthesis.
Externí odkaz:
https://doaj.org/article/c031fda3199f4ae4ade00e57b4490d02
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-18 (2019)
Higher organisms regulate cellular iron concentrations through Iron Regulatory Proteins (IRPs), which regulate specific messenger RNAs. Here Huynh et al. show that IRP1 requires a Glycogen Branching Enzyme for proper function, and that IRP1 has addit
Externí odkaz:
https://doaj.org/article/4e8b650540394120baea3a101dd8b36d
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-9 (2019)
Interactions between metabolites and transcription factors are known to control gene expression but analyzing these events at genome-scale is challenging. Here, the authors integrate dynamic metabolome and transcriptome data from E.coli to predict re
Externí odkaz:
https://doaj.org/article/40a4273f4f2f49d69ac21e2945fcb595
Autor:
Roland Lill, Oliver Stehling
Publikováno v:
HemaSphere, Vol 2, Pp 76-79 (2018)
Externí odkaz:
https://doaj.org/article/df1b09c1da614f518152bfa90f15ae5c
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-15 (2017)
Fe/S clusters are synthesized by the mitochondrial iron-sulfur cluster assembly (ISC) machinery. Here the authors combine crystallography and small angle X-ray scattering measurements to structurally characterize the core ISC complex and give functio
Externí odkaz:
https://doaj.org/article/380f33a1b9c943c18f6f4d959f2218f2
Autor:
Sven-A. Freibert, Alina V. Goldberg, Christian Hacker, Sabine Molik, Paul Dean, Tom A. Williams, Sirintra Nakjang, Shaojun Long, Kacper Sendra, Eckhard Bill, Eva Heinz, Robert P. Hirt, John M Lucocq, T. Martin Embley, Roland Lill
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
The functions of the highly reduced mitochondria (mitosomes) of microsporidians are not well-characterized. Here, the authors show that theTrachipleistophora hominismitosome is the site of iron–sulfur cluster assembly and that its retention is like
Externí odkaz:
https://doaj.org/article/e78ff76691884b4cabe49d811630fe3d
Autor:
Maiko Luis Tonini, Priscila Peña-Diaz, Alexander C Haindrich, Somsuvro Basu, Eva Kriegová, Antonio J Pierik, Roland Lill, Stuart A MacNeill, Terry K Smith, Julius Lukeš
Publikováno v:
PLoS Pathogens, Vol 14, Iss 10, p e1007326 (2018)
Fe-S clusters are ubiquitous cofactors of proteins involved in a variety of essential cellular processes. The biogenesis of Fe-S clusters in the cytosol and their insertion into proteins is accomplished through the cytosolic iron-sulphur protein asse
Externí odkaz:
https://doaj.org/article/f4e0f016786d4b6d86c031945d8cebf8
Publikováno v:
mBio, Vol 8, Iss 5 (2017)
ABSTRACT Copper (Cu) ions serve as catalytic cofactors to drive key biochemical processes, and yet Cu levels that exceed cellular homeostatic control capacity are toxic. The underlying mechanisms for Cu toxicity are poorly understood. During pulmonar
Externí odkaz:
https://doaj.org/article/cf5d3641b1104700a491f77f81386edc