Results 191 to 200 of about 112,766 (248)
Oxidative Stress and Iron Addiction: A Comparative Study of 1321N1 Astrocytoma and T98G Glioblastoma Cells with Differential Expression of L-Cysteine-Metabolizing Enzymes. [PDF]
Jurkowska H +5 more
europepmc +1 more source
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Topological chirality of iron-sulfur proteins
Biopolymers, 1997An 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
Iron–sulfur protein folds, iron–sulfur chemistry, and evolution
JBIC Journal of Biological Inorganic Chemistry, 2007An inventory of unique local protein folds around Fe-S clusters has been derived from the analysis of protein structure databases. Nearly 50 such folds have been identified, and over 90% of them harbor low-potential [2Fe-2S](2+,+) or [4Fe-4S](2+,+) clusters. In contrast, high-potential Fe-S clusters, notwithstanding their structural diversity, occur in
openaire +3 more sources
Chemical & Engineering News Archive, 2000
Adecade ago, bioinorganic chemists thought they had pretty much figured out what the iron-sulfur clusters found in many proteins were there for. The prevailing wisdom was that these proteins had one basic function in biology—to move electrons around, says Michael K. Johnson, chemistry professor at the University of Georgia, Athens. Biological processes
openaire +1 more source
Adecade ago, bioinorganic chemists thought they had pretty much figured out what the iron-sulfur clusters found in many proteins were there for. The prevailing wisdom was that these proteins had one basic function in biology—to move electrons around, says Michael K. Johnson, chemistry professor at the University of Georgia, Athens. Biological processes
openaire +1 more source
2007
The sections in this article are 1 Introduction 2 NMR and Hyperfine Coupling in Various FeS Proteins 3 Structural Information on the Diamagnetic Part 4 Biographical Sketches Related ...
BERTINI, IVANO, LUCHINAT, CLAUDIO
openaire +2 more sources
The sections in this article are 1 Introduction 2 NMR and Hyperfine Coupling in Various FeS Proteins 3 Structural Information on the Diamagnetic Part 4 Biographical Sketches Related ...
BERTINI, IVANO, LUCHINAT, CLAUDIO
openaire +2 more sources
Folding properties of iron—sulfur proteins
Inorganica Chimica Acta, 1998Abstract The 1 H NMR spectra in water of HiPIP I from Ectothiorhodospira halophila , the Cys77Ser mutant of the HiPIP from Chromatium vinosum , the 7Fe8S ferredoxin from Bacillus schlegelii , the 8Fe8S ferredoxin from Clostridium pasteurianum and the 2Fe2S ferredoxin from P.
BERTINI, IVANO +3 more
openaire +2 more sources

