Search Results - "Allewell, N. M."

The biochemical and molecular spectrum of ornithine transcarbamylase deficiency by Tuchman, M., Morizono, H., Rajagopal, B. S., Plante, R. J., Allewell, N. M.

“…Ornithine transcarbamylase (OTCase) deficiency, the most commoninherited urea cycle disorder, is transmitted as an X‐linked trait. The clinical phenotype in…”
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Crystal structure of bullfrog M ferritin at 2.8 A resolution: analysis of subunit interactions and the binuclear metal center by Ha, Y, Shi, D, Small, G W, Theil, E C, Allewell, N M

“…Ferritins concentrate and store iron as a mineral in all bacterial, plant, and animal cells. The two ferritin subunit types, H or M (fast) and L (slow), differ…”
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Multigrid solution of the nonlinear Poisson-Boltzmann equation and calculation of titration curves by Oberoi, H., Allewell, N.M.

“…Although knowledge of the pKa values and charge states of individual residues is critical to understanding the role of electrostatic effects in protein…”
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Human ornithine transcarbamylase: crystallographic insights into substrate recognition and conformational changes by Shi, D, Morizono, H, Yu, X, Tong, L, Allewell, N M, Tuchman, M

“…Two crystal structures of human ornithine transcarbamylase (OTCase) complexed with the substrate carbamoyl phosphate (CP) have been solved. One structure,…”
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The clinically variable R40H mutant ornithine carbamoyltransferase shows cytosolic degradation of the precursor protein in CHO cells by Mavinakere, M., Morizono, H., Shi, D., Allewell, N. M., Tuchman, M.

“…Ornithine carbamoyltransferase (OCT) deficiency is now frequently found in adults with hyperammonaemia affected by mutations that cause partial deficiency of…”
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Identification of ‘private’ mutations in patients with ornithine transcarbamylase deficiency by Tuchman, M., Morizono, H., Rajagopal, B. S., Plante, R. J., Allewell, N. M.

“…The majority of cases of ornithine transcarbamylase deficiency are due to novel mutations making it impossible to develop common methods for genetic analysis…”
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Crystallization and structural analysis of bullfrog red cell L-subunit ferritins by Trikha, J, Waldo, G S, Lewandowski, F A, Ha, Y, Theil, E C, Weber, P C, Allewell, N M

“…Ferritin is a 24 subunit protein that controls biomineralization of iron in animals, bacteria, and plants. Rates of mineralization vary among members of the…”
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Preliminary Analysis of Amphibian Red Cell M Ferritin in a Novel Tetragonal Unit Cell by Ha, Y., Theil, E. C., Allewell, N. M.

“…The ferritins are a multigene family of proteins that concentrate and store iron in all prokaryotic and eukaryotic cells. 24 monomeric subunits which fold as…”
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The molecular basis of ornithine transcarbamylase deficiency: modelling the human enzyme and the effects of mutations by Tuchman, M, Morizono, H, Reish, O, Yuan, X, Allewell, N M

“…Human ornithine transcarbamylase is a trimer with 46% amino acid sequence homology to the catalytic subunit of E coli aspartate transcarbamylase. Secondary…”
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Effects of the T→R transition on the electrostatic properties of E. coli aspartate transcarbamylase by Hariharan, M., Allewell, N.M.

“…Aspartate transcarbamylase is a large (310 kD), multisubunit protein that binds substrates cooperatively and undergoes a large change in quaternary structure…”
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Crystallization and preliminary X-ray crystallographic studies of wild-type human ornithine transcarbamylase and two naturally occurring mutants at position 277 by Shi, Dashuang, Morizono, Hiroki, Yu, Xiaolin, Tong, Liang, Allewell, Norma M., Tuchman, Mendel

“…Wild‐type human ornithine transcarbamylase (OTCase) and two mutants (R277Q and R277W) that cause `late‐onset' hyperammonemia were crystallized and a…”
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Electrostatic effects in protein folding, stability, and function by Allewell, N M, Oberoi, H

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‘Late Onset’ Ornithine Transcarbamylase Deficiency: Function of Three Purified Recombinant Mutant Enzymes by Morizono, Hiroki, Listrom, Chad D., Rajagopal, B. S., Aoyagi, Mika, McCann, Mark T., Allewell, Norma M., Tuchman, Mendel

“…Although many mutations in the ornithine transcarbamylase gene have been correlated with ‘late onset’ of hyperammonemia in patients, the effects of these…”
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High-resolution differential scanning calorimetric analysis of the subunits of Escherichia coli aspartate transcarbamoylase by Edge, Victoria, Allewell, Norma M, Sturtevant, Julian M

“…The thermal denaturation of the catalytic (c3) and regulatory (r2) subunits of Escherichia coli aspartate transcarbamoylase (c6r6) in the absence and presence…”
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Localized unfolding at the junction of three ferritin subunits. A mechanism for iron release? by Takagi, H, Shi, D, Ha, Y, Allewell, N M, Theil, E C

“…How and where iron exits from ferritin for cellular use is unknown. Twenty-four protein subunits create a cavity in ferritin where iron is concentrated…”
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Differential scanning calorimetric study of the thermal denaturation of aspartate transcarbamoylase of Escherichia coli by Edge, Victoria, Allewell, Norma M, Sturtevant, Julian M

“…The thermal denaturation of Escherichia coli aspartate transcarbamoylase (c6r6) in the absence and presence of various ligands has been studied by means of…”
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Identification, cloning and expression of the mouse N-acetylglutamate synthase gene by Caldovic, Ljubica, Morizono, Hiroki, Yu, Xiaolin, Thompson, Mark, Shi, Dashuang, Gallegos, Rene, Allewell, Norma M, Malamy, Michael H, Tuchman, Mendel

“…In ureotelic animals, N-acetylglutamate (NAG) is an essential allosteric activator of carbamylphosphate synthetase I (CPSI), the first enzyme in the urea…”
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Ligation alters the pathway of urea‐induced denaturation of the catalytic trimer of Escherichia coli aspartate transcarbamylase by Bromberg, S., Licata, V.J., Mallikarachchi, D., Allewell, N.M.

“…We have examined the pathway and energetics of urea‐induced dissociation and unfolding of the catalytic trimer (C3) of aspartate transcarbamylase from…”
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Changes in the Hydrogen Exchange Kinetics of Escherichia coli Aspartate Transcarbamylase Produced by Effector Binding and Subunit Association by Lennick, M., Allewell, N. M.

“…Large changes in solvent accessibility to aspartate transcarbamylase (aspartate carbamoyltransferase, carbamoylphosphate:L-aspartate carbamoyltransferase, EC…”
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Electrostatic interactions in the assembly of Escherichia coli aspartate transcarbamylase by Glackin, M P, McCarthy, M P, Mallikarachchi, D, Matthew, J B, Allewell, N M

“…Although ionizable groups are known to play important roles in the assembly, catalytic, and regulatory mechanisms of Escherichia coli aspartate…”
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