Výsledky vyhledávání - "Valerie C. Smith"

Structure-Based Mutagenesis Reveals Critical Residues in the Transferrin Receptor Participating in the Mechanism of pH-Induced Release of Iron from Human Serum Transferrin

Autor: Ashley N. Steere, Anne B. Mason, N. Dennis Chasteen, Valerie C. Smith, Ross T. A. MacGillivray, Brendan F. Miller

Publikováno v: Biochemistry. 51:2113-2121

The recent crystal structure of two monoferric human serum transferrin (Fe(N)hTF) molecules bound to the soluble portion of the homodimeric transferrin receptor (sTFR) has provided new details about this binding interaction that dictates the delivery

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c97ba4d87cc5016a1e3714281c620c43
https://doi.org/10.1021/bi3001038

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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

Autor: Valerie C. Smith, Ross T. A. MacGillivray, Shaina L. Byrne, Anne B. Mason, N. Dennis Chasteen, Ashley N. Steere

Publikováno v: JBIC Journal of Biological Inorganic Chemistry. 15:1341-1352

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 His349 on the TFR interaction, it was replaced by alanine, aspartate, lysine, leucine, trypto

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52dc637e3d367532853133b1ccf5ba9f
https://doi.org/10.1007/s00775-010-0694-2

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Human hephaestin expression is not limited to enterocytes of the gastrointestinal tract but is also found in the antrum, the enteric nervous system, and pancreatic β-cells

Autor: Charles H. Scudamore, David M. Hudson, Susan B. Curtis, Alison M.J. Buchan, Tanya A. M. Griffiths, Valerie C. Smith, Ann Y. K. Wong, Ross T. A. MacGillivray

Publikováno v: American Journal of Physiology-Gastrointestinal and Liver Physiology. 298:G425-G432

Hephaestin (Hp) is a membrane protein with ferroxidase activity that converts Fe(II) to Fe(III) during the absorption of nutritional iron in the gut. Using anti-peptide antibodies to predicted immunogenic regions of rodent Hp, previous immunocytochem

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38c578e2f11fed61802f69825c8d4f00
https://doi.org/10.1152/ajpgi.00453.2009

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A loop in theN-lobe of human serum transferrin is critical for binding to the transferrin receptor as revealed by mutagenesis, isothermal titration calorimetry, and epitope mapping

Autor: Samantha E. Roberts, N. Dennis Chasteen, Banu Kandemir, Shaina L. Byrne, Stephen J. Everse, Anne B. Mason, Valerie C. Smith, Ross T. A. MacGillivray, Fadi Bou-Abdallah

Publikováno v: Journal of Molecular Recognition. 22:521-529

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 its hydrolysis). The iron is delivered to actively dividing cells by receptor mediated endo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::47947dc287b175a44f52e3197654c023
https://doi.org/10.1002/jmr.979

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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

Autor: Shaina L. Byrne, Anne B. Mason, Ross T. A. MacGillivray, Valerie C. Smith, Nicholas G. James, Ashley N. Steere

Publikováno v: Biochemistry. 48:2858-2867

Human serum transferrin (hTF), with two Fe3+ binding lobes, transports iron into cells. Diferric hTF preferentially binds to a specific receptor (TFR) on the surface of cells, and the complex undergoes clathrin dependent receptor-mediated endocytosis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6dc48e9db02e116e8ab9f7d52c42c3ee
https://doi.org/10.1021/bi8022834

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Structural and Functional Consequences of the Substitution of Glycine 65 with Arginine in the N-Lobe of Human Transferrin

Autor: N.D Chasteen, Peter J. Halbrooks, Shaina L. Byrne, Valerie C. Smith, Anne B. Mason, Nicholas G. James, Stephen J. Everse, J.K Grady, Ross T. A. MacGillivray, Igor A. Kaltashov, C.E Bobst

Publikováno v: Biochemistry. 48:1945-1953

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 is hydrogen-bonded to the iron-binding ligand Asp63, it comprises part of the second-shell h

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4dc4e6b31c72ac6c612ae0c641fadbcf
https://doi.org/10.1021/bi802254x

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Genetically engineering transferrin to improve its in vitro ability to deliver cytotoxins

Autor: Valerie C. Smith, Daniel T. Kamei, Dennis J. Yoon, Anne B. Mason, Christopher W. Ng, Edward A. Pham, David M. Hudson, David S.H. Chu, Ross T. A. MacGillivray

Publikováno v: Journal of Controlled Release. 133:178-184

We previously demonstrated that decreasing the iron release rate of transferrin (Tf), by replacing the synergistic anion carbonate with oxalate, increases its in vitro drug carrier efficacy in HeLa cells. In the current work, the utility of this stra

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6c5e807047959601bfa6bbfcc737c21e
https://doi.org/10.1016/j.jconrel.2008.10.006

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Mutational Analysis of C-Lobe Ligands of Human Serum Transferrin: Insights into the Mechanism of Iron Release

Autor: Peter J. Halbrooks, Anne B. Mason, Nicholas G. James, N. Dennis Chasteen, Susan A. Connolly, Valerie C. Smith, Julia R. Larouche, Ross T. A. MacGillivray

Publikováno v: Biochemistry. 44:8013-8021

Each homologous lobe of human serum transferrin (hTF) has one Fe(3+) ion bound by an aspartic acid, a histidine, two tyrosine residues, and two oxygens from the synergistic anion, carbonate. Extensive characterization of these ligands in the N-termin

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c2226f36d7257b4b416c955a6708655
https://doi.org/10.1021/bi050015f

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