Zobrazeno 1 - 10
of 80
pro vyhledávání: '"Robert C. WOODWORTH"'
Autor:
A. T. Tan, Robert C. Woodworth
Publikováno v:
Journal of Polymer Science Part C: Polymer Symposia. 30:599-606
The stabilities of conalbumin and transition metal-conalbumin complexes toward denaturants were studied by UV absorption and emission spectroscopy. The difference spectra of conalbumin and metal-conalbumins in buffer, pH 8.0 vs. the same species in b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a6e44a9a1c51a52a37d4e61518837ef1
https://doi.org/10.1002/polc.5070300162
https://doi.org/10.1002/polc.5070300162
Publikováno v:
Journal of Biological Chemistry. 276:8829-8835
Several bismuth compounds are currently used as antiulcer drugs, but their mechanism of action is not well established. Proteins are thought to be target sites. In this work we establish that the competitive binding of Bi(3+) to the blood serum prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::581b4b4e6df09b226e218ad64a1ab272
https://doi.org/10.1074/jbc.m004779200
https://doi.org/10.1074/jbc.m004779200
Autor:
Qing-Yu HE, Anne B. MASON, Barbara A. LYONS, Beatrice M. TAM, Vinh NGUYEN, Ross T.A. MACGILLIVRAY, Robert C. WOODWORTH
Publikováno v:
Biochemical Journal. 354:423-429
Human serum transferrin N-lobe (hTF/2N) contains three conserved tryptophan residues, Trp8, Trp128 and Trp264, located in three different environments. The present report addresses the different contributions of the three tryptophan residues to the U
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::76c75f3a52bc67d320dcc00b9c2ff16c
https://doi.org/10.1042/bj3540423
https://doi.org/10.1042/bj3540423
Publikováno v:
Biochemical Journal. 350:909-915
The major function of human transferrin is to deliver iron from the bloodstream to actively dividing cells. Upon iron release, the protein changes its conformation from ‘closed’ to ‘open’. Extensive studies in vitro indicate that iron release
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::550237f819afc3aae80aa84dd44e8da2
https://doi.org/10.1042/bj3500909
https://doi.org/10.1042/bj3500909
Publikováno v:
Biochemical Journal. 344:881-887
The N-lobe of human serum transferrin (hTF/2N) and single point mutants in which each of the five methionine residues was individually mutated have been produced in a mammalian tissue-culture expression system. Since the five methionine residues are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c5a5ed52ae11ef11571b63f6fda119d4
https://doi.org/10.1042/bj3440881
https://doi.org/10.1042/bj3440881
Publikováno v:
Biochemical Journal. 337:105-111
Interactions of recombinant N-lobe of human serum transferrin (hTF/2N) with Bi3+, a metal ion widely used in medicine, have been investigated by both UV and NMR spectroscopy. The bicarbonate-independent stability constant for Bi3+ binding (K*) to hTF
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae27ec247fb541cb722fd35638c53ff6
https://doi.org/10.1042/bj3370105
https://doi.org/10.1042/bj3370105
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
Autor:
Anne B. Mason, John F. Brandts, Ross T. A. MacGillivray, Beatrice M. Tam, Janet A. Lineback, Robert C. Woodworth, Lung-Nan Lin, Brian N. Green, Ronald W. A. Oliver, Kerry J. Savage
Publikováno v:
Biochemical Journal. 326:77-85
The binding of iron by transferrin leads to a significant conformational change in each lobe of the protein. Numerous studies have shown that the transferrin receptor discriminates between iron-saturated and iron-free transferrin and that it modulate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::57f6e2815bfcb8b060d0dbd879f3aa79
https://doi.org/10.1042/bj3260077
https://doi.org/10.1042/bj3260077