Search Results - "Smith, Valerie C"

Helicobacter pylori Infection Targets Adherens Junction Regulatory Proteins and Results in Increased Rates of Migration in Human Gastric Epithelial Cells by Conlin, Victoria S, Curtis, Susan B, Zhao, Ying, Moore, Edwin D W, Smith, Valerie C, Meloche, R Mark, Finlay, B Brett, Buchan, Alison M J

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Investigation of the Mechanism of Iron Release from the C-Lobe of Human Serum Transferrin:  Mutational Analysis of the Role of a pH Sensitive Triad by Halbrooks, Peter J, He, Qing-Yu, Briggs, Sara K, Everse, Stephen J, Smith, Valerie C, MacGillivray, Ross T. A, Mason, Anne B

“…The transferrins (TFs) are a family of proteins that are widely distributed in vertebrates, where they serve a major role in iron binding and transport. Most…”
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Expression, purification, and characterization of authentic monoferric and apo-human serum transferrins by Mason, Anne B., Halbrooks, Peter J., Larouche, Julia R., Briggs, Sara K., Moffett, Marque L., Ramsey, Jon E., Connolly, Susan A., Smith, Valerie C., MacGillivray, Ross T.A.

“…Transferrin is a bilobal protein with the ability to bind iron in two binding sites situated at the bottom of a cleft in each lobe. We have previously…”
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Structure-Based Mutagenesis Reveals Critical Residues in the Transferrin Receptor Participating in the Mechanism of pH-Induced Release of Iron from Human Serum Transferrin by Steere, Ashley N, Chasteen, N. Dennis, Miller, Brendan F, Smith, Valerie C, MacGillivray, Ross T. A, Mason, Anne B

“…The recent crystal structure of two monoferric human serum transferrin (FeNhTF) molecules bound to the soluble portion of the homodimeric transferrin receptor…”
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Ionic Residues of Human Serum Transferrin Affect Binding to the Transferrin Receptor and Iron Release by Steere, Ashley N, Miller, Brendan F, Roberts, Samantha E, Byrne, Shaina L, Chasteen, N. Dennis, Smith, Valerie C, MacGillivray, Ross T. A, Mason, Anne B

“…Efficient delivery of iron is critically dependent on the binding of diferric human serum transferrin (hTF) to its specific receptor (TFR) on the surface of…”
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Genetically engineering transferrin to improve its in vitro ability to deliver cytotoxins by Yoon, Dennis J., Chu, David S.H., Ng, Christopher W., Pham, Edward A., Mason, Anne B., Hudson, David M., Smith, Valerie C., MacGillivray, Ross T.A., Kamei, Daniel T.

“…We previously demonstrated that decreasing the iron release rate of transferrin (Tf), by replacing the synergistic anion carbonate with oxalate, increases its…”
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Inequivalent Contribution of the Five Tryptophan Residues in the C-Lobe of Human Serum Transferrin to the Fluorescence Increase when Iron is Released by James, Nicholas G, Byrne, Shaina L, Steere, Ashley N, Smith, Valerie C, MacGillivray, Ross T. A, Mason, Anne B

“…Human serum transferrin (hTF), with two Fe3+ binding lobes, transports iron into cells. Diferric hTF preferentially binds to a specific receptor (TFR) on the…”
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Intrinsic Fluorescence Reports a Global Conformational Change in the N-Lobe of Human Serum Transferrin following Iron Release by James, Nicholas G, Berger, Christopher L, Byrne, Shaina L, Smith, Valerie C, MacGillivray, Ross T. A, Mason, Anne B

“…Transferrins have been extensively studied in order to understand how they reversibly bind and release iron. Human serum transferrin (hTF) is a single…”
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Evidence that His349 acts as a pH-inducible switch to accelerate receptor-mediated iron release from the C-lobe of human transferrin by Steere, Ashley N, Byrne, Shaina L, Chasteen, N. Dennis, Smith, Valerie C, MacGillivray, Ross T. A, Mason, Anne B

“…His349 in human transferrin (hTF) is a residue critical to transferrin receptor (TFR)-stimulated iron release from the C-lobe. To evaluate the importance of…”
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A loop in the N-lobe of human serum transferrin is critical for binding to the transferrin receptor as revealed by mutagenesis, isothermal titration calorimetry, and epitope mapping by Mason, Anne B., Byrne, Shaina L., Everse, Stephen J., Roberts, Samantha E., Chasteen, N. Dennis, Smith, Valerie C., MacGillivray, Ross T. A., Kandemir, Banu, Bou-Abdallah, Fadi

“…Transferrin (TF) is a bilobal transport protein that acquires ferric iron from the diet and holds it tightly within the cleft of each lobe (thereby preventing…”
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Effect of Glycosylation on the Function of a Soluble, Recombinant Form of the Transferrin Receptor by Byrne, Shaina L, Leverence, Rachael, Klein, Joshua S, Giannetti, Anthony M, Smith, Valerie C, MacGillivray, Ross T. A, Kaltashov, Igor A, Mason, Anne B

“…Production of the soluble portion of the transferrin receptor (sTFR) by baby hamster kidney (BHK) cells is described, and the effect of glycosylation on the…”
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Mutational Analysis of C-Lobe Ligands of Human Serum Transferrin:  Insights into the Mechanism of Iron Release by Mason, Anne B, Halbrooks, Peter J, James, Nicholas G, Connolly, Susan A, Larouche, Julia R, Smith, Valerie C, MacGillivray, Ross T. A, Chasteen, N. Dennis

“…Each homologous lobe of human serum transferrin (hTF) has one Fe3+ ion bound by an aspartic acid, a histidine, two tyrosine residues, and two oxygens from the…”
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Structural and Functional Consequences of the Substitution of Glycine 65 with Arginine in the N-Lobe of Human Transferrin by Mason, Anne B, Halbrooks, Peter J, James, Nicholas G, Byrne, Shaina L, Grady, John K, Chasteen, N. Dennis, Bobst, Cedric E, Kaltashov, Igor A, Smith, Valerie C, MacGillivray, Ross T. A, Everse, Stephen J

“…The G65R mutation in the N-lobe of human transferrin was created to mimic a naturally occurring variant (G394R) found in the homologous C-lobe. Because Gly65…”
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The position of arginine 124 controls the rate of iron release from the N-lobe of human serum transferrin. A structural study by Adams, Ty E, Mason, Anne B, He, Qing-Yu, Halbrooks, Peter J, Briggs, Sara K, Smith, Valerie C, MacGillivray, Ross T A, Everse, Stephen J

“…Human serum transferrin (hTF) is a bilobal iron-binding and transport protein that carries iron in the blood stream for delivery to cells by a pH-dependent…”
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Composition of pH-Sensitive Triad in C-Lobe of Human Serum Transferrin. Comparison to Sequences of Ovotransferrin and Lactoferrin Provides Insight into Functional Differences in Iron Release by Halbrooks, Peter J., Giannetti, Anthony M., Klein, Joshua S., Björkman, Pamela J., Larouche, Julia R., Smith, Valerie C., MacGillivray, Ross T. A., Everse, Stephen J., Mason, Anne B.

“…The transferrins (TF) are a family of bilobal glycoproteins that tightly bind ferric iron. Each of the homologous N- and C-lobes contains a single iron-binding…”
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Properties of a homogeneous C-lobe prepared by introduction of a TEV cleavage site between the lobes of human transferrin by Steere, Ashley N., Roberts, Samantha E., Byrne, Shaina L., Dennis Chasteen, N., Bobst, Cedric E., Kaltashov, Igor A., Smith, Valerie C., MacGillivray, Ross T.A., Mason, Anne B.

“…Essential to iron transport and delivery, human serum transferrin (hTF) is a bilobal glycoprotein capable of reversibly binding one ferric ion in each lobe…”
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Microdeletion Of Exon 3 In The HBA2 Gene Associated With Mild α-Thalassemia Trait by Lambert, Anne, Wong, Ann Y.K., Kominami, Yohji, Smith, Valerie C., Reddy, Suseela, Wadsworth, Louis D., Au, Nicholas H.C., MacGillivray, Ross T.A.

“…A mother and son presented with mild symptoms of thalassemia trait. Polymerase chain reaction (PCR) amplification of their globin genes revealed a previously…”
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Structural and functional consequences of the substitution of glycine 65 by arginine in the N-lobe of human transferrin by Mason, Anne B., Halbrooks, Peter J., James, Nicholas G., Byrne, Shaina L., Grady, John K., Chasteen, N. Dennis, Bobst, Cedric E., Kaltashov, Igor A., Smith, Valerie C., MacGillivray, Ross T. A., Everse, Stephen J.

“…The G65R mutation in the N-lobe of human transferrin was created to mimic a naturally occurring variant (G394R) found in the homologous C-lobe. Because Gly65…”
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Differential Effect of a His Tag at the N- and C-Termini:  Functional Studies with Recombinant Human Serum Transferrin by Mason, Anne B, He, Qing-Yu, Halbrooks, Peter J, Everse, Stephen J, Gumerov, Dmitry R, Kaltashov, Igor A, Smith, Valerie C, Hewitt, Jeff, MacGillivray, Ross T. A

“…Attachment of a cleavable hexa His tag is a common strategy for the production of recombinant proteins. Production of two recombinant nonglycosylated human…”
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Molecular determination of the breakpoints of a 161 556 bp deletion at chromosome 13q34 that presented as severe factor VII deficiency in a neonate by Hewitt, Jeff, Craven, Sharon J., Brown, Lindsay A., Bleackley, Mark R., Ballard, Jennifer N. M., Smith, Valerie C., Ofosu, Frederick A., Huntsman, David G., Wadsworth, Louis D., Wu, John K., MacGillivray, Ross T. A.

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