Structural basis for sialic acid-mediated self-recognition by complement factor H (Q27696183)

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Jonathan P Hannan

object named as

Jonathan P Hannan

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David Kavanagh

object named as

David Kavanagh

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author name string

Bärbel S Blaum

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Andrew P Herbert

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Dušan Uhrín

Infections of People with Complement Deficiencies and Patients Who Have Undergone Splenectomy

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publication date

January 2015

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published in

Nature Chemical Biology

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volume

11

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issue

1

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page(s)

77-82

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cites work

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Structural basis for engagement by complement factor H of C3b on a self surface

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Dual interaction of factor H with C3d and glycosaminoglycans in host-nonhost discrimination by complement

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Disease-associated sequence variations congregate in a polyanion recognition patch on human factor H revealed in three-dimensional structure

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Structural and functional characterization of the product of disease-related factor H gene conversion

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Mutations in alternative pathway complement proteins in American patients with atypical hemolytic uremic syndrome

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Mutation in the key enzyme of sialic acid biosynthesis causes severe glomerular proteinuria and is rescued by N-acetylmannosamine

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Structural Basis for Complement Evasion by Lyme Disease Pathogen Borrelia burgdorferi

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Structural implications of Siglec-5-mediated sialoglycan recognition

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The Cell Adhesion Molecule “CAR” and Sialic Acid on Human Erythrocytes Influence Adenovirus In Vivo Biodistribution

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A novel sialic acid binding site on factor H mediates serum resistance of sialylated Neisseria gonorrhoeae

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The binding of factor H to a complex of physiological polyanions and C3b on cells is impaired in atypical hemolytic uremic syndrome.

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12 December 2020

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