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 …
for O 2 transport in mammals. Less widely recognised is that erythrocyte Hb belongs to a …
Hemoglobin and heme scavenging
Release of hemoglobin into plasma is a physiological phenomenon associated with
intravascular hemolysis. In plasma, stable haptoglobin‐hemoglobin complexes are formed …
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 …
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 …
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 …
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 …
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
The synthesis of haemoglobin A (HbA) is exquisitely coordinated during erythrocyte
development to prevent damaging effects from individual α-and β-subunits,. The α …
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 …
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
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; …
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 …
monitoring the mechanism of acid-induced hemoglobin (Hb) denaturation. The protein for …