Results 101 to 110 of about 54,320 (150)

Approximate size and preliminary composition of the low-mass zinc pool in the cytosol of Saccharomyces cerevisiae. [PDF]

J Biol Chem
Kreinbrink AC, Lindahl PA.
europepmc   +1 more source

Iron Sulfides Produced by Thermococcales: An Iron Detoxification Mechanism. [PDF]

Environ Microbiol
Mariotte T, Coudray R, Toffano-Nioche C, Guyot F, Gorlas A.   +4 more
europepmc   +1 more source

Receptor-substrate competition for the TonB homolog FusB suggests a model for ferredoxin import. [PDF]

J Biol Chem
Wojnowska M, Flores V, Yelland T, Fisher SR, Bogucka A, Stott K, Walker D.   +6 more
europepmc   +1 more source

Identification and characterization of <i>CsYP</i> in regulating chloroplast development and cucumber peel color. [PDF]

Hortic Res
Cui Y, Li S, Wu H, Zhao X, Zhang X, Dong Y, Wang Y, An M, Yang L, Chen X, Weng Y, Ren H, Liu X.   +12 more
europepmc   +1 more source

Iron-sulfur clusters in proteins : synthesis of a model compound for three-iron-sulfur proteins

, 1986
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Maturation of cytosolic and nuclear iron–sulfur proteins

Trends in Cell Biology, 2014
Eukaryotic cells contain numerous cytosolic and nuclear iron-sulfur (Fe/S) proteins that perform key functions in metabolic catalysis, iron regulation, protein translation, DNA synthesis, and DNA repair. Synthesis of Fe/S clusters and their insertion into apoproteins are essential for viability and are conserved in eukaryotes.
Antonio J Pierik, Roland Lill, Oliver Stehling   +2 more
exaly   +4 more sources

Iron–sulfur proteins in health and disease

Trends in Endocrinology & Metabolism, 2010
Iron-sulfur (Fe/S) proteins are a class of ubiquitous components that assist in vital and diverse biochemical tasks in virtually every living cell. These tasks include respiration, iron homeostasis and gene expression. The past decade has led to the discovery of novel Fe/S proteins and insights into how their Fe/S cofactors are formed and incorporated ...
Sheftel, A., Stehling, O., Lill, R.
openaire   +3 more sources

Topological chirality of iron-sulfur proteins

Biopolymers, 1997
An examination of x-ray structures of single-cluster [4Fe-4S] proteins in the Protein Data Bank has revealed that all redox proteins and the glutamine 5-phosphoribosyl-l-pyrophosphate amidotransferase from Bacillus subtilis have a topological configuration arbitrarily designated as D, whereas the DNA repair enzyme endonuclease III from Escherichia coli
C, Liang, K, Mislow
openaire   +2 more sources