Zobrazeno 1 - 10
of 94
pro vyhledávání: '"Clara Fronticelli"'
Publikováno v:
Artificial Cells, Blood Substitutes, and Biotechnology. 35:45-52
This paper describes the approaches we have taken to construct a) mutant hemoglobins with different oxygen affinities, and b) mutant hemoglobins and myoglobins that polymerize to high molecular weight aggregates in an effort to prevent extravasation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6510513e71c405d3e2756267ca00f4b8
https://doi.org/10.1080/10731190600974467
https://doi.org/10.1080/10731190600974467
Publikováno v:
Transfusion Alternatives in Transfusion Medicine. 5:516-520
SUMMARY Molecular biology offers the opportunity to construct hemoglobin molecules as blood substitutes tailored to specific therapeutic applications. Oxygen affinity can be manipulated by amino acid substitutions in the heme pocket or on the protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6d2f2bd12ec42195f0c3b553b26bfe29
https://doi.org/10.1111/j.1778-428x.2004.tb00090.x
https://doi.org/10.1111/j.1778-428x.2004.tb00090.x
Autor:
Clara Fronticelli, Michael Karavitis, Maria Teresa Sanna, William S. Brinigar, Kevin M. Bobofchak
Publikováno v:
Biophysical Chemistry. 98:115-126
Previous studies on bovine hemoglobin (HbBv) have suggested amino acid substitutions, which might introduce into human hemoglobin (HbA) functional characteristics of HbBv, namely a low intrinsic oxygen affinity regulated by Cl(-). Accordingly, we hav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e69bdfd26a2e879969676c36a398a22
https://doi.org/10.1016/s0301-4622(02)00089-3
https://doi.org/10.1016/s0301-4622(02)00089-3
Publikováno v:
Proteins: Structure, Function, and Genetics. 44:73-78
The energetic changes that occur on ligand binding in human hemoglobin have been investigated by measurements of the exchange rates of the indole proton of Trpbeta37(C3). The Trpbeta37 residues are located in helices C of the beta-subunits and are in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a81a370b0cb212361fd70564aa684bb6
https://doi.org/10.1002/prot.1074
https://doi.org/10.1002/prot.1074
Autor:
Maurizio Leone, Michael Karavitis, Antonio Cupane, Clara Fronticelli, William S. Brinigar, Gregory B. Vasquez, Valeria Militello
Publikováno v:
Journal of Biological Chemistry. 273:23740-23749
The spectroscopic, conformational, and functional properties of mutant carbonmonoxy hemoglobins in which either the β-globin Val67(E11) or the α-globin Val62(E11) is replaced by threonine have been investigated. The thermal evolution of the Soret a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ee1ae7a1ad6a1babffe96b9534ef12e9
https://doi.org/10.1074/jbc.273.37.23740
https://doi.org/10.1074/jbc.273.37.23740
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 54:355-366
The three-dimensional structure and associated solvent of human carboxyhemoglobin at 2.2 Å resolution are compared with other R-state and T-state human hemoglobin structures. The crystal form is isomorphous with that of the 2.7 Å structure of carbo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f16fd70d1f1058375e871d9aad5e63b5
https://doi.org/10.1107/s0907444997012250
https://doi.org/10.1107/s0907444997012250
Autor:
Xinhua Ji, Gary L. Gilliland, Michael Braxenthaler, John Moult, Enrico Bucci, Clara Fronticelli
Publikováno v:
Proteins: Structure, Function, and Genetics. 30:309-320
The crystal structure of human T state hemoglobin crosslinked with bis(3,5-dibromo-salicyl) sebacate has been determined at 1.9 A resolution. The final crystallographic R factor is 0.168 with root-mean-square deviations (RMSD) from ideal bond distanc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::64cbd8f67c6827a1f7dcd655339fc664
https://doi.org/10.1002/(sici)1097-0134(19980215)30:3<309::aid-prot10>3.0.co
https://doi.org/10.1002/(sici)1097-0134(19980215)30:3<309::aid-prot10>3.0.co
Autor:
Gregory Vasquez, Clara Fronticelli, Michael Karavitis, Xinhua Ji, Herman Kwansa, Anna Razynska, Gary L. Gilliland, Enrico Bucci
Publikováno v:
Biophysical Chemistry. 70:21-34
In the crystal structure of human T-state hemoglobin with a sebacyl residue cross-linking the two beta-subunit Lys82,s (DecHb), the Fe atoms of the alpha-subunit hemes are found to be oxidized with a water molecule bound. The three-dimensional struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29e3d1522d1c44df6e536b10440d991c
https://doi.org/10.1016/s0301-4622(97)00096-3
https://doi.org/10.1016/s0301-4622(97)00096-3
Autor:
Michael Karavitis, Valeria Militello, Fred K. Friedman, Maurizio Leone, William S. Brinigar, Antonio Cupane, Clara Fronticelli, Gregory B. Vasquez, Aditya P. Koley
Publikováno v:
Journal of Biological Chemistry. 272:26271-26278
The dynamic and functional properties of mutant deoxyhemoglobins in which either the β-globin Val67(E11) or the α-globin Val62(E11) is replaced by threonine have been investigated through the thermal evolution of the Soret absorption band in the te
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2f3444274bdf92d3b811d83749510cb9
https://doi.org/10.1074/jbc.272.42.26271
https://doi.org/10.1074/jbc.272.42.26271
Autor:
Aditya P. Koley, Clara Fronticelli, Michael Karavitis, Maria Teresa Sanna, Fred K. Friedman, Irina M. Russu, Anna Razynska, William S. Brinigar
Publikováno v:
Journal of Biological Chemistry. 272:3478-3486
The α-globin of human hemoglobin was expressed in Escherichia coli and was refolded with heme in the presence and in the absence of native β-chains. The functional and structural properties of the expressed α-chains were assessed in the isolated s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3b20f7ad2f40bd47ca9405bfa0c8681e
https://doi.org/10.1074/jbc.272.6.3478
https://doi.org/10.1074/jbc.272.6.3478