Claire J Parker Siburt
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Explore the profile of Claire J Parker Siburt including associated specialties, affiliations and a list of published articles.
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11
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117
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Recent Articles
1.
Strader M, Bangle R, Parker Siburt C, Varnado C, Soman J, Benitez Cardenas A, et al.
Biochem J
. 2017 Oct;
474(24):4171-4192.
PMID: 29070524
Previous work suggested that hemoglobin (Hb) tetramer formation slows autoxidation and hemin loss and that the naturally occurring mutant, Hb Providence (HbProv; βK82D), is much more resistant to degradation by...
2.
Banerjee S, Weerasinghe A, Parker Siburt C, Kreulen R, Armstrong S, Brickman T, et al.
Biochemistry
. 2014 May;
53(24):3952-60.
PMID: 24873326
Bordetella pertussis is the causative agent of whooping cough. This pathogenic bacterium can obtain the essential nutrient iron using its native alcaligin siderophore and by utilizing xeno-siderophores such as desferrioxamine...
3.
Weerasinghe A, Amin S, Barker R, Othman T, Romano A, Parker Siburt C, et al.
J Am Chem Soc
. 2013 Sep;
135(39):14504-7.
PMID: 24028339
Boron in the ocean is generally considered a nonbiological element due to its relatively high concentration (0.4 mM) and depth independent concentration profile. Here we report an unexpected role for...
4.
Mollan T, Banerjee S, Wu G, Parker Siburt C, Tsai A, Olson J, et al.
J Biol Chem
. 2012 Dec;
288(6):4288-98.
PMID: 23264625
α-Hemoglobin stabilizing protein (AHSP) is a molecular chaperone that binds monomeric α-subunits of human hemoglobin A (HbA) and modulates heme iron oxidation and subunit folding states. Although AHSP·αHb complexes autoxidize...
5.
Banerjee S, Jia Y, Parker Siburt C, Abraham B, Wood F, Bonaventura C, et al.
Free Radic Biol Med
. 2012 Jul;
53(6):1317-26.
PMID: 22841869
We compared oxygenation and anaerobic oxidation reactions of a purified complex of human hemoglobin (Hb) and haptoglobin (Hb-Hp) to those of uncomplexed Hb. Under equilibrium conditions, Hb-Hp exhibited active-site heterogeneity...
6.
Banerjee S, Parker Siburt C, Mistry S, Noto J, DeArmond P, Fitzgerald M, et al.
Metallomics
. 2012 Mar;
4(4):361-72.
PMID: 22399131
Neisseria gonorrhoeae is an obligate pathogen that hijacks iron from the human iron transport protein, holo-transferrin (Fe(2)-Tf), by expressing TonB-dependent outer membrane receptor proteins, TbpA and TbpB. Homologous to other...
7.
Parker Siburt C, Mietzner T, Crumbliss A
Biochim Biophys Acta
. 2011 Sep;
1820(3):379-92.
PMID: 21933698
Background: Gram negative bacteria require iron for growth and virulence. It has been shown that certain pathogenic bacteria such as Neisseria gonorrhoeae possess a periplasmic protein called ferric binding protein...
8.
Bonaventura C, Henkens R, Friedman J, Parker Siburt C, Kraiter D, Crumbliss A
Biochim Biophys Acta
. 2011 Jul;
1814(10):1261-8.
PMID: 21745602
The structural basis of the extreme pH dependence of oxygen binding to Root effect Hbs is a long-standing puzzle in the field of protein chemistry. A previously unappreciated role of...
9.
Bonaventura C, Henkens R, De Jesus-Bonilla W, Lopez-Garriga J, Jia Y, Alayash A, et al.
Biochim Biophys Acta
. 2010 Jul;
1804(10):1988-95.
PMID: 20601225
The clam Lucina pectinalis supports its symbiotic bacteria by H₂S transport in the open and accessible heme pocket of Lucina Hb I and by O₂ transport in the narrow and...
10.
Parker Siburt C, Lin E, Brandt S, Tinoco A, Valentine A, Crumbliss A
J Inorg Biochem
. 2010 Jun;
104(9):1006-9.
PMID: 20569990
Transferrin, the human iron transport protein, binds Ti(IV) even more tightly than it binds Fe(III). However, the fate of titanium bound to transferrin is not well understood. Here we present...