Zobrazeno 1 - 10
of 12
pro vyhledávání: '"John K. Grady"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1800:858-870
Ferritin exhibits complex behavior in the ultracentrifuge due to variability in iron core size among molecules. A comprehensive study was undertaken to develop procedures for obtaining more uniform cores and assessing their homogeneity.Analytical ult
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b4c2427a588aa36a9be75e1ccf128e9
https://doi.org/10.1016/j.bbagen.2010.03.012
https://doi.org/10.1016/j.bbagen.2010.03.012
Autor:
Qing-Yu He, Robert C. Woodworth, N. Dennis Chasteen, Beatrice M. Tam, Ross T. A. MacGillivray, Anne B. Mason, John K. Grady
Publikováno v:
Journal of Biological Chemistry. 273:17018-17024
The x-ray crystal structure of the N-lobe of human serum transferrin has shown that there is a hydrogen bond network, the so-called “second shell,” around the transferrin iron binding site. Tyrosine at position 85 and glutamic acid at position 83
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c77cf6b15043aa02d1996eec72a5405a
https://doi.org/10.1074/jbc.273.27.17018
https://doi.org/10.1074/jbc.273.27.17018
Autor:
Beatrice M. Tam, N. Dennis Chasteen, Anne B. Mason, Qing-Yu He, and John K. Grady, Ross T. A. MacGillivray, Robert C. Woodworth
Publikováno v:
Biochemistry. 36:14853-14860
Human serum transferrin N-lobe (hTF/2N) has four iron-binding ligands, including one histidine, one aspartate, and two tyrosines. The present report elucidates the inequivalence of the two tyrosine ligands (Tyr 95 and Tyr 188) on the metal-binding pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef5bbe5ca6884e4bce157ee8eae55270
https://doi.org/10.1021/bi9719556
https://doi.org/10.1021/bi9719556
Publikováno v:
Journal of inorganic biochemistry. 80(1-2)
During its metabolism, vanadium is known to become associated with the iron storage protein, ferritin. To elucidate probable vanadium binding sites on the protein, VO 2+ binding to mammalian ferritins was studied using site-directed mutagenesis and E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e709eb466552dd583899a03ef962338f
https://pubmed.ncbi.nlm.nih.gov/10885470
https://pubmed.ncbi.nlm.nih.gov/10885470
The effects of site-directed mutation and salt on the iron(III)-binding site of the recombinant half-molecule of the N-terminal lobe (hTf/2N) of human transferrin was studied by EPR spectroscopy. Changes were observed in the EPR spectra of all varian
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08259084ee74066b3ca8dc3f050fb0f8
https://europepmc.org/articles/PMC1135746/
https://europepmc.org/articles/PMC1135746/
Publikováno v:
Lactoferrin Structure and Function ISBN: 9780306447341
Salts are known to have a pronounced effect on the spectroscopic, thermodynamic and kinetic properties of human serum transferrin. The present study was undertaken to examine the effect of NaCl on the related proteins ovotransferrin and lactoferrin.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::367176783889751432c17bb2808e93a1
https://doi.org/10.1007/978-1-4615-2548-6_5
https://doi.org/10.1007/978-1-4615-2548-6_5
Publikováno v:
Biochimica et biophysica acta. 1076(2)
Diferric transferrin was modified using aquopentaammine ruthenium(II), a reagent for surface-accessible uncoordinated histidines. Introduction of the cationic Ru(III) (NH 3 ) 5 3+ group on the imidazole of only 5.5 of the 17 uncoordinated histidines
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a1a5019828e64105cf97bd00aea59680
https://pubmed.ncbi.nlm.nih.gov/1998724
https://pubmed.ncbi.nlm.nih.gov/1998724
Autor:
John K. Grady, N. Dennis Chasteen
Publikováno v:
Iron Biominerals ISBN: 9781461366997
A number of recent studies have implicated the involvement of ferritin iron in oxygen radical reactions. Hemosiderin has long been thought to be a degradation product of ferritin. A recent series of papers have indicated that oxygen radical damage to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2c8abaebd9d6dcdc30e8c994bb8c1f98
https://doi.org/10.1007/978-1-4615-3810-3_22
https://doi.org/10.1007/978-1-4615-3810-3_22
Publikováno v:
Inorganic Chemistry. 25:2754-2760
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::44ce90975f0510d42698bde4e66e6278
https://doi.org/10.1021/ic00236a021
https://doi.org/10.1021/ic00236a021
Publikováno v:
Journal of Biological Chemistry. 264:20224-20229
The chemistry of oxidative deposition of iron(III) in ferritin and apoferritin is poorly understood. This study was undertaken to look for radicals formed as the hydrous ferric oxide core is developed from Fe(II) and O2. Radicals were observed indire
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::75439da488bdf53aec073dffc5d9afc4
https://doi.org/10.1016/s0021-9258(19)47050-6
https://doi.org/10.1016/s0021-9258(19)47050-6