Structure and function of haemoglobins

DA Gell - Blood Cells, Molecules, and Diseases, 2018 - Elsevier
Haemoglobin (Hb) is widely known as the iron-containing protein in blood that is essential
for O 2 transport in mammals. Less widely recognised is that erythrocyte Hb belongs to a …

Hemoglobin and heme scavenging

P Ascenzi, A Bocedi, P Visca, F Altruda… - IUBMB …, 2005 - Wiley Online Library
Release of hemoglobin into plasma is a physiological phenomenon associated with
intravascular hemolysis. In plasma, stable haptoglobin‐hemoglobin complexes are formed …

Proline cis-trans isomerization controls autoinhibition of a signaling protein

P Sarkar, C Reichman, T Saleh, RB Birge… - Molecular cell, 2007 - cell.com
Autoinhibition is being widely used in nature to repress otherwise constitutive protein
activities and is typically regulated by extrinsic factors. Here we show that autoinhibition can …

Molecular mechanism of AHSP-mediated stabilization of α-hemoglobin

L Feng, DA Gell, S Zhou, L Gu, Y Kong, J Li, M Hu… - Cell, 2004 - cell.com
Hemoglobin A (HbA), the oxygen delivery system in humans, comprises two α and two β
subunits. Free α-hemoglobin (αHb) is unstable, and its precipitation contributes to the …

Prolyl isomerization and its catalysis in protein folding and protein function

PAM Schmidpeter, FX Schmid - Journal of molecular biology, 2015 - Elsevier
Prolyl isomerizations are intrinsically slow processes. They determine the rates of many
protein folding reactions and control regulatory events in folded proteins. Prolyl isomerases …

An erythroid chaperone that facilitates folding of α-globin subunits for hemoglobin synthesis

X Yu, YI Kong, LC Dore, O Abdulmalik… - The Journal of …, 2007 - Am Soc Clin Investig
Erythrocyte precursors produce abundant α-and β-globin proteins, which assemble with
each other to form hemoglobin A (HbA), the major blood oxygen carrier. αHb-stabilizing …

Structure of oxidized α-haemoglobin bound to AHSP reveals a protective mechanism for haem

L Feng, S Zhou, L Gu, DA Gell, JP Mackay, MJ Weiss… - Nature, 2005 - nature.com
The synthesis of haemoglobin A (HbA) is exquisitely coordinated during erythrocyte
development to prevent damaging effects from individual α-and β-subunits,. The α …

Chaperoning erythropoiesis

MJ Weiss, CO dos Santos - Blood, The Journal of the American …, 2009 - ashpublications.org
Multisubunit complexes containing molecular chaperones regulate protein production,
stability, and degradation in virtually every cell type. We are beginning to recognize how …

The role of alpha-hemoglobin stabilizing protein in redox chemistry, denaturation, and hemoglobin assembly

TL Mollan, X Yu, MJ Weiss, JS Olson - Antioxidants & redox …, 2010 - liebertpub.com
Hemoglobin biosynthesis in erythrocyte precursors involves several steps. The correct ratios
and concentrations of normal alpha (α) and beta (β) globin proteins must be expressed; …

Symmetric behavior of hemoglobin α-and β-subunits during acid-induced denaturation observed by electrospray mass spectrometry

BL Boys, MC Kuprowski, L Konermann - Biochemistry, 2007 - ACS Publications
This work employs electrospray mass spectrometry (ESI-MS) and UV− vis spectroscopy for
monitoring the mechanism of acid-induced hemoglobin (Hb) denaturation. The protein for …