Structure of the haptoglobin-haemoglobin complex (Q27682043)

8

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Søren Kragh Moestrup

object named as

Søren Kragh Moestrup

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Jan Skov Pedersen

object named as

Jan Skov Pedersen

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author name string

Christian Brix Folsted Andersen

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Morten Torvund-Jensen

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Marianne Jensby Nielsen

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Cristiano Luis Pinto de Oliveira

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Niels Højmark Andersen

A unique loop extension in the serine protease domain of haptoglobin is essential for CD163 recognition of the haptoglobin-hemoglobin complex.

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language of work or name

English

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publication date

20 September 2012

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published in

Nature

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volume

489

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page(s)

456-9

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issue

7416

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cites work

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Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-A. resolution, obtained by X-ray analysis

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Structure of haptoglobin and the haptoglobin-hemoglobin complex by electron microscopy

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Rate of nitric oxide scavenging by hemoglobin bound to haptoglobin

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A haptoglobin-hemoglobin receptor conveys innate immunity to Trypanosoma brucei in humans

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12 December 2020

Hemoglobin. A biologic fenton reagent

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The Binding of Hemoglobin to Haptoglobin and Its Relation to Subunit Dissociation of Hemoglobin

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Haptoglobin preserves the CD163 hemoglobin scavenger pathway by shielding hemoglobin from peroxidative modification

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Quantitative mass spectrometry defines an oxidative hotspot in hemoglobin that is specifically protected by haptoglobin

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OXYGEN EQUILIBRIA OF THE HEMOGLOBIN-HAPTOGLOBIN COMPLEX

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Increased Susceptibility in Hp Knockout Mice During Acute Hemolysis

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A new method for the evaluation of small-angle scattering data

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7 January 2021