Search results for: Thomas Brittain

Items from 1 to 20 out of 23 results

article

An analysis approach to identify specific functional sites in orthologous proteins using sequence and structural information: Application to neuroserpin reveals regions that differentially regulate inhibitory activity

Tet Woo Lee, Annie Shu‐Ping Yang, Thomas Brittain, Nigel P. Birch

Proteins: Structure, Function, and Bioinformatics > 83 > 1 > 135 - 152

The analysis of sequence conservation is commonly used to predict functionally important sites in proteins. We have developed an approach that first identifies highly conserved sites in a set of orthologous sequences using a weighted substitution‐matrix‐based conservation score and then filters these conserved sites based on the pattern of conservation present in a wider alignment of sequences from...

article

Novel haemoglobin mutation (α127Lys→Glu) increases oxygen affinity and has a minor effect on haptoglobin binding

Stephen O. Brennan, Beverley Pullon, Maurice C. Owen, Thomas Brittain

Clinical Biochemistry > 2012 > 45 > 18 > 1587-1590

To determine if a new haemoglobin (Hb) variant was the underlying cause of erythrocytosis in a subject with a high apparent HbA ₁ c.Haemolysate was analysed by ESI MS, and individual components purified by ion exchange and reverse phase chromatography. Peptide mapping was used to pinpoint the substitution and DNA sequencing to confirm the precise mutation. Oxygen affinity was measured and...

article

Extended survival of SH‐SY5Y cells following overexpression of Lys67Glu neuroglobin is associated with stabilization of Δψ_M

Joanna Skommer, Thomas Brittain

Cytometry Part A > 81A > 7 > 602 - 610

Overwhelming evidence indicates that a high level of expression of the protein neuroglobin protects neurons in vitro, in animal models, and in humans, against cell death associated with hypoxic and amyloid insult. We have previously showed that neuroglobin protects neuronal cells from the mitochondrial pathway of apoptosis induced by the BH3 mimetic, by preventing cytochrome c‐triggered activation...

article

Nonlinear regulation of commitment to apoptosis by simultaneous inhibition of Bcl-2 and XIAP in leukemia and lymphoma cells

Joanna Skommer, Somkanya C. Das, Arjun Nair, Thomas Brittain, more

Apoptosis > 2011 > 16 > 6 > 619-626

Apoptosis is a complex pathway regulated by the concerted action of multiple pro- and anti-apoptotic molecules. The intrinsic (mitochondrial) pathway of apoptosis is governed up-stream of mitochondria, by the family of Bcl-2 proteins, and down-stream of mitochondria, by low-probability events, such as apoptosome formation, and by feedback circuits involving caspases and inhibitor of apoptosis proteins...

article

Neuroglobin protects nerve cells from apoptosis by inhibiting the intrinsic pathway of cell death

Subhadip Raychaudhuri, Joanna Skommer, Kristen Henty, Nigel Birch, more

Apoptosis > 2010 > 15 > 4 > 401-411

In the past few years, overwhelming evidence has accrued that a high level of expression of the protein neuroglobin protects neurons in vitro, in animal models, and in humans, against cell death associated with hypoxic and amyloid insult. However, until now, the exact mechanism of neuroglobin’s protective action has not been determined. Using cell biology and biochemical approaches we demonstrate...

article

Characterization of the hemoglobins of the Australian lungfish Neoceratodus forsteri (Krefft)

Jonas R. Rasmussen, Rufus M.G. Wells, Kristen Henty, Timothy D. Clark, more

Comparative Biochemistry and Physiology, Part A > 2009 > 152 > 2 > 162-167

We examined for the first time the hemoglobin components of the blood of the Australian lungfish, Neoceratodus forsteri and their functional responses to pH and the allosteric modulators adenosine triphosphate (ATP), guanosine triphosphate (GTP), 2,3-bisphosphoglyceric acid (BPG) and inositol hexaphosphate (IHP) at 25 °C. Lysates prepared from stripped, unfractionated hemolysate produced sigmoidal...

article

Characterization of the hemoglobins of the neonatal brushtailed possum Trichosurus vulpecula (Kerr): Evidence for a highly cooperative, aggregated isoform of hemoglobin

Kristen Henty, Rufus M.G. Wells, Thomas Brittain

Comparative Biochemistry and Physiology, Part A > 2008 > 150 > 1 > 52-57

The red blood cells of the neonatal brushtailed possum exhibit unusually strong cooperativity at high levels of oxygen saturation (n=5.4) which appear to arise from a concentration dependent aggregation of one of the neonatal hemoglobin isoforms. Red blood cells from neonatal pouched young exhibit a Bohr factor of −0.36. Stripped hemolysate is sensitive to added 2,3-bisphosphoglycerate (BPG) (apparent...

article

Characterization of the hemoglobins of the adult brushtailed possum, Trichosurus vulpecula (Kerr) reveals non-genetic heterogeneity

Kristen Henty, Rufus M.G. Wells, Thomas Brittain

Comparative Biochemistry and Physiology, Part A > 2007 > 148 > 3 > 498-503

The hemoglobins contained within the red blood cells of the adult brushtail possum exhibited cooperative (n=2.6) oxygen binding curves with an associated p ₅₀ of 38 mm Hg at pH 7.4 and a large Bohr effect (−0.60). Stripped hemolysate showed a Bohr effect of −0.27, and was sensitive to added DPG (K=56 μmol L ⁻¹ ), ATP (K=130 μmol L ⁻¹ ), and chloride ions. Four isoforms of hemoglobin...

article

Activation of the cytochrome c peroxidase of Pseudomonas aeruginosa. The role of a heme-linked protein loop: A mutagenesis studies

Hsi-Chen Hsiao, Svetlana Boycheva, Nicholas J. Watmough, Thomas Brittain

Journal of Inorganic Biochemistry > 2007 > 101 > 8 > 1133-1139

Mutagenesis studies have been used to investigate the role of a heme ligand containing protein loop (67–79) in the activation of di-heme peroxidases. Two mutant forms of the cytochrome c peroxidase of Pseudomonas aeruginosa have been produced. One mutant (loop mutant) is devoid of the protein loop and the other (H71G) contains a non-ligating Gly at the normal histidine ligand site. Spectroscopic data...

article

The reaction of neuroglobin with potential redox protein partners cytochrome b5 and cytochrome c

Angela Fago, Antony J. Mathews, Luc Moens, Sylvia Dewilde, more

FEBS Letters > 2006 > 580 > 20 > 4884-4888

Previously identified, potentially neuroprotective reactions of neuroglobin require the existence of yet unknown redox partners. We show here that the reduction of ferric neuroglobin by cytochrome b ₅ is relatively slow (k=6×10 ² M ⁻¹ s ⁻¹ at pH 7.0) and thus is unlikely to be of physiological significance. In contrast, the reaction between ferrous neuroglobin and ferric...

article

The reactions of neuroglobin with CO: Evidence for two forms of the ferrous protein

Angela Fago, Antony J. Mathews, Sylvia Dewilde, Luc Moens, more

Journal of Inorganic Biochemistry > 2006 > 100 > 8 > 1339-1343

The normally hexa coordinate ferrous form of neuroglobin binds CO by replacement of the heme-linked distal histidine residue. We have studied this reaction in detail using stopped flow techniques. The reaction time courses are complex at all the wavelengths studied. Specifically the reaction with CO occurs in two temporally separable phases, each of which shows a hyperbolic dependence of rate on CO...

article

Root effect hemoglobins

Thomas Brittain

Journal of Inorganic Biochemistry > 2005 > 99 > 1 > 120-129

The Root effect describes an extreme pH sensitivity expressed in the hemoglobins of certain fish, in which it plays a unique physiological role. This review describes our general understanding of the effect of protons on the oxygen binding properties of hemoglobin and the particular properties which characterize Root effect proteins. The development of our understanding of the molecular origins of...

article

Complex Interactions of Carbon Monoxide with Reduced Cytochrome cbb ₃ Oxidase from Pseudomonas stutzeri ^†

Robert S. Pitcher, Thomas Brittain, Nicholas J. Watmough

Biochemistry > 2003 > 42 > 38 > 11263 - 11271

article

Molecular aspects of embryonic hemoglobin function

Thomas Brittain

Molecular Aspects of Medicine > 2002 > 23 > 4 > 293-342

In order to provide the appropriate level of oxygen transport to respiring tissues, we need to produce a molecular oxygen transporting system to supplement oxygen diffusion and solubility. This supplementation is provided by hemoglobin. The role of hemoglobin in providing oxygen transport from lung to tissues in the adult is well-documented and functional characteristics of the fetal hemoglobin, which...

article

Electron transfer between cytochrome b ₅ and some oxidised haemoglobins: the role of ionic strength

Thomas Brittain, Richard D. Kidd, Edward. N. Baker

Journal of Inorganic Biochemistry > 2002 > 88 > 3-4 > 328-334

We have compared experimental measurements and Brownian dynamic calculations for the reduction of oxidised adult human haemoglobin by reduced bovine cytochrome b ₅ over a range of ionic strengths. Our calculations suggest that the presence of molecular electrostatic fields have a significant role to play in the formation of the electron transfer complexes. These results predict that electron...

article

The Role of β Chains in the Control of the Hemoglobin Oxygen Binding Function: Chimeric Human/Mouse Proteins, Structure, and Function ^‡

Richard D. Kidd, J. Eric Russell, Nicholas J. Watmough, Edward N. Baker, more

Biochemistry > 2001 > 40 > 51 > 15669 - 15675

article

A modeling study of the interaction and electron transfer between cytochrome b5 and some oxidized haemoglobins

Richard Kidd, Edward Baker, Thomas Brittain

JBIC Journal of Biological Inorganic Chemistry > 2002 > 7 > 1-2

Abstract. Using Brownian motion simulations we have studied the formation of docked complexes of reduced cytochrome b5 and oxidized haemoglobin. Our results indicate that the presence of molecular electrostatic fields has a significant role to play in the formation of these complexes. In contrast to previous modeling studies on this system, we clearly identify electron transfer within an ensemble...

article

A modeling study of the interaction and electron transfer between cytochrome b ₅ and some oxidized haemoglobins

Richard D. Kidd, Edward N. Baker, Thomas Brittain

JBIC Journal of Biological Inorganic Chemistry > 2002 > 7 > 1-2 > 23-30

. Using Brownian motion simulations we have studied the formation of docked complexes of reduced cytochrome b ₅ and oxidized haemoglobin. Our results indicate that the presence of molecular electrostatic fields has a significant role to play in the formation of these complexes. In contrast to previous modeling studies on this system, we clearly identify electron transfer within an ensemble...

article

The ferric form of the three human embryonic hemoglobins and their reactions with azide ions

Thomas Brittain

Journal of Inorganic Biochemistry > 2000 > 81 > 1-2 > 99-103

The ferric forms of the three human embryonic hemoglobins exhibit pH titration's with pK _a values in the range 8.25-8.6, which correlate with the reduced proteins affinity for oxygen. Azide ions bind to each ferric protein in a process consisting of two separate binding steps. The equilibrium constants for this process are in the 10-30 μM range and can be assigned to the individual chain within...

article

Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form of gower II (α2ϵ2) haemoglobin at 2.9 å resolution11Edited by K. Nagai

Andrew J Sutherland-Smith, Heather M Baker, Oliver M Hofmann, Thomas Brittain, more

Journal of Molecular Biology > 1998 > 280 > 3 > 475-484

The production of recombinant embryonic haemoglobins via a yeast expression system has enabled structural and functional studies to be conducted on these proteins. As part of a programme aimed at understanding the properties of the embryonic haemoglobins we have crystallized the human α₂ϵ₂ (Gower II) embryonic haemoglobin in its carbonmonoxy form, and determined its structure by X-ray crystallography...

Publication date

Set your own date range

INFONA - science communication portal

Search results for: Thomas Brittain

An analysis approach to identify specific functional sites in orthologous proteins using sequence and structural information: Application to neuroserpin reveals regions that differentially regulate inhibitory activity

Novel haemoglobin mutation (α127Lys→Glu) increases oxygen affinity and has a minor effect on haptoglobin binding

Extended survival of SH‐SY5Y cells following overexpression of Lys67Glu neuroglobin is associated with stabilization of Δψ_M

Nonlinear regulation of commitment to apoptosis by simultaneous inhibition of Bcl-2 and XIAP in leukemia and lymphoma cells

Neuroglobin protects nerve cells from apoptosis by inhibiting the intrinsic pathway of cell death

Characterization of the hemoglobins of the Australian lungfish Neoceratodus forsteri (Krefft)

Characterization of the hemoglobins of the neonatal brushtailed possum Trichosurus vulpecula (Kerr): Evidence for a highly cooperative, aggregated isoform of hemoglobin

Characterization of the hemoglobins of the adult brushtailed possum, Trichosurus vulpecula (Kerr) reveals non-genetic heterogeneity

Activation of the cytochrome c peroxidase of Pseudomonas aeruginosa. The role of a heme-linked protein loop: A mutagenesis studies

The reaction of neuroglobin with potential redox protein partners cytochrome b5 and cytochrome c

The reactions of neuroglobin with CO: Evidence for two forms of the ferrous protein

Root effect hemoglobins

Complex Interactions of Carbon Monoxide with Reduced Cytochrome cbb ₃ Oxidase from Pseudomonas stutzeri ^†

Molecular aspects of embryonic hemoglobin function

Electron transfer between cytochrome b ₅ and some oxidised haemoglobins: the role of ionic strength

The Role of β Chains in the Control of the Hemoglobin Oxygen Binding Function: Chimeric Human/Mouse Proteins, Structure, and Function ^‡

A modeling study of the interaction and electron transfer between cytochrome b5 and some oxidized haemoglobins

A modeling study of the interaction and electron transfer between cytochrome b ₅ and some oxidized haemoglobins

The ferric form of the three human embryonic hemoglobins and their reactions with azide ions

Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form of gower II (α2ϵ2) haemoglobin at 2.9 å resolution11Edited by K. Nagai

Filter options

Publication date

Content availability

Keywords

Data set

Journal

INFONA - science communication portal

Search results for: Thomas Brittain

Add recipient

Sending message cancelled

Are you sure you want to cancel sending this message?

Send message

Filter options

Publication date

Date range setting

Set the date range to filter the displayed results. You can set a starting date, ending date or both. You can enter the dates manually or choose them from the calendar.

Content availability

Keywords

Data set

Journal

Reporting an error / abuse

Sending the report failed

Accessibility options