Zobrazeno 1 - 10
of 54
pro vyhledávání: '"William E. Walden"'
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Abstract Comparison of kinetic and thermodynamic properties of IRP1 (iron regulatory protein1) binding to FRT (ferritin) and ACO2 (aconitase2) IRE-RNAs, with or without Mn2+, revealed differences specific to each IRE-RNA. Conserved among animal mRNAs
Externí odkaz:
https://doaj.org/article/4ecaa347360042289277247c71e2651a
Publikováno v:
Biochemistry. 58:2017-2027
The cytosolic iron-sulfur cluster assembly (CIA) scaffold, comprising Nbp35 and Cfd1 in yeast, assembles iron-sulfur (FeS) clusters destined for cytosolic and nuclear enzymes. ATP hydrolysis by the CIA scaffold plays an essential but poorly understoo
Publikováno v:
Journal of Biological Chemistry. 288:23358-23367
P-loop NTPases of the ApbC/Nbp35 family are involved in FeS protein maturation in nearly all organisms and are proposed to function as scaffolds for initial FeS cluster assembly. In yeast and animals, Cfd1 and Nbp35 are homologous P-loop NTPases that
Autor:
Roland Lill, Daili J. A. Netz, Martin Stümpfig, William E. Walden, Eckhard Bill, Anil K. Sharma, Leif J. Pallesen, Antonio J. Pierik
Publikováno v:
Journal of Biological Chemistry. 287:12365-12378
The essential P-loop NTPases Cfd1 and Nbp35 of the cytosolic iron-sulfur (Fe-S) protein assembly machinery perform a scaffold function for Fe-S cluster synthesis. Both proteins contain a nucleotide binding motif of unknown function and a C-terminal m
Publikováno v:
FEBS Letters. 586:32-35
Iron responsive elements (IREs) are short stem-loop structures found in several mRNAs encoding proteins involved in cellular iron metabolism. Iron regulatory proteins (IRPs) control iron homeostasis through differential binding to the IREs, accommoda
Publikováno v:
Journal of Biological Chemistry. 285:26745-26751
FeS cluster biogenesis is an essential process in virtually all forms of life. Complex protein machineries that are conserved from bacteria through higher eukaryotes facilitate assembly of the FeS cofactor in proteins. In the last several years, sign
Autor:
Tanya Bondar, Pradip Raychaudhuri, William E. Walden, Sergei M. Mirkin, Ekaterina V. Mirkin, David S. Ucker
Publikováno v:
Journal of Biological Chemistry. 278:37006-37014
Schizosaccharomyces pombe Ddb1 is homologous to the mammalian DDB1 protein, which has been implicated in damaged-DNA recognition and global genomic repair. However, a recent study suggested that the S. pombe Ddb1 is involved in cell division and chro
Autor:
Richard S. Eisenstein, William E. Antholine, Nina Brown, William E. Walden, M. Claire Kennedy
Publikováno v:
Journal of Biological Chemistry. 277:7246-7254
Interconversion of iron regulatory protein 1 (IRP1) with cytosolic aconitase (c-aconitase) occurs via assembly/disassembly of a [4Fe-4S] cluster. Recent evidence implicates oxidants in cluster disassembly. We investigated H2O2-initiated Fe-S cluster
Publikováno v:
Journal of Biological Chemistry. 275:16227-16234
Iron regulatory proteins (IRP) are sequence-specific RNA-binding proteins that mediate iron-responsive gene regulation in animals. IRP1 is also the cytosolic isoform of aconitase (c-aconitase). This latter activity could complement a mitochondrial ac
Publikováno v:
Journal of Biological Chemistry. 273:23637-23640
A family of noncoding mRNA sequences, iron-responsive elements (IREs), coordinately regulate several mRNAs through binding a family of mRNA-specific proteins, iron regulatory proteins (IRPs). IREs are hairpins with a constant terminal loop and base-p