Results 331 to 340 of about 286,555 (389)
Some of the next articles are maybe not open access.
Ferritin: The role of aluminum in ferritin function
Neurobiology of Aging, 1991We previously showed that human brain ferritin (HBF) binds aluminum (Al) in vivo and in vitro and HBF isolated from Alzheimer's brain had more Al bound compared to aged matched controls (7). To further understand the role ferritin may play in Al neurotoxicity, we have studied in vitro the effect of Al on the function of human ferritin isolated from ...
J T, Fleming, J G, Joshi
openaire +2 more sources
Biomineralization-Inspired Synthesis of Copper Sulfide–Ferritin Nanocages as Cancer Theranostics
ACS Nano, 2016 Yijing Liu, Lisen Lin, Jing Lin
exaly +2 more sources
Nature, 1968
ELECTROPHORETIC studies of ferritins—iron containing proteins—from horse, man and HeLa cells have already been recorded1,2. This communication describes the electrophoretic patterns of a plant ferritin known as phytoferritin3 and of ferritins from pig, ox and guinea-pig, compared with human and horse ferritin.
I, Zamiri, J, Mason
openaire +2 more sources
ELECTROPHORETIC studies of ferritins—iron containing proteins—from horse, man and HeLa cells have already been recorded1,2. This communication describes the electrophoretic patterns of a plant ferritin known as phytoferritin3 and of ferritins from pig, ox and guinea-pig, compared with human and horse ferritin.
I, Zamiri, J, Mason
openaire +2 more sources
The Lancet, 1973
FERRITIN is the major iron storage protein in the body. Although it is found in all tissues there is little quantitative information about its distribution.
G M, Addison +3 more
openaire +2 more sources
FERRITIN is the major iron storage protein in the body. Although it is found in all tissues there is little quantitative information about its distribution.
G M, Addison +3 more
openaire +2 more sources
Archives of Biochemistry and Biophysics, 1989
Apoferritins prepared from horse spleen and heart and rat heart and liver were dissociated by treatment with acetic acid (pH 1.3-3.0). Sedimentation velocity studies showed that apoferritins of spleen and liver (16-17 S) and heart (18-19 S) dissociated into material sedimenting near 3.2 S.
M C, Linder +4 more
openaire +2 more sources
Apoferritins prepared from horse spleen and heart and rat heart and liver were dissociated by treatment with acetic acid (pH 1.3-3.0). Sedimentation velocity studies showed that apoferritins of spleen and liver (16-17 S) and heart (18-19 S) dissociated into material sedimenting near 3.2 S.
M C, Linder +4 more
openaire +2 more sources
Science, 1942
Publisher Summary In 1894, Schmiedeberg prepared an iron-containing protein from pig's liver, containing about 7% iron. This poorly defined compound was obtained in a denatured condition. The first decisive step was made with Laufberger's discovery of a readily crystallizable protein, containing as much as about 20% of iron, in the ferric state.
S, Granick, L, Michaelis
openaire +2 more sources
Publisher Summary In 1894, Schmiedeberg prepared an iron-containing protein from pig's liver, containing about 7% iron. This poorly defined compound was obtained in a denatured condition. The first decisive step was made with Laufberger's discovery of a readily crystallizable protein, containing as much as about 20% of iron, in the ferric state.
S, Granick, L, Michaelis
openaire +2 more sources
Clinica Chimica Acta, 2005
Iron, an essential element for many important cellular functions in all living organisms, can catalyze the formation of potentially toxic free radicals. Excessive iron is sequestered by ferritin in a nontoxic and readily available form in a cell.
Sun-Ah, You, Qing, Wang
openaire +2 more sources
Iron, an essential element for many important cellular functions in all living organisms, can catalyze the formation of potentially toxic free radicals. Excessive iron is sequestered by ferritin in a nontoxic and readily available form in a cell.
Sun-Ah, You, Qing, Wang
openaire +2 more sources
Blood Reviews, 1990
The iron storage protein ferritin is found in all cells of the body as multiple isoferritins composed of 24 sub units of two types. The structure is well understood from increasingly detailed analysis by X-ray crystallography. Genes for the principal subunits (called H and L) have been cloned and are located on chromosomes 11q and 19q respectively. The
openaire +2 more sources
The iron storage protein ferritin is found in all cells of the body as multiple isoferritins composed of 24 sub units of two types. The structure is well understood from increasingly detailed analysis by X-ray crystallography. Genes for the principal subunits (called H and L) have been cloned and are located on chromosomes 11q and 19q respectively. The
openaire +2 more sources
The International Journal of Biochemistry & Cell Biology, 2004
A novel ferritin type specifically targeted to mitochondria has been recently found in human and mouse. It is structurally and functionally similar to the cytosolic ferritins, well-characterized molecules found in most living systems which are designed to store and detoxify cellular iron.
LEVI S, AROSIO, Paolo
openaire +4 more sources
A novel ferritin type specifically targeted to mitochondria has been recently found in human and mouse. It is structurally and functionally similar to the cytosolic ferritins, well-characterized molecules found in most living systems which are designed to store and detoxify cellular iron.
LEVI S, AROSIO, Paolo
openaire +4 more sources