(Q28246156)

1

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P N Hawkins

2

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M C Bickerstaff

3

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J Herbert

4

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A E Bygrave

5

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A McBride

6

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W L Hutchinson

7

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G A Tennent

8

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M J Walport

9

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M B Pepys

https://scigraph.springernature.com/pub.10.1038/nm0897-855

10

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language of work or name

English

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publication date

August 1997

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published in

Nature Medicine

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volume

3

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page(s)

855-9

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issue

8

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exact match

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cites work

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Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix

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Amyloid P component. A critical review

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Imaging amyloidosis with radiolabelled SAP

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Specific chemical dissociation of fibrillar and non-fibrillar components of amyloid deposits

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Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure

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Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis

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Studies in vivo and in vitro of serum amyloid P component in normals and in a patient with AA amyloidosis

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A protease‐sensitive site in the proposed Ca2+‐binding region of human serum amyloid P component and other pentraxins

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The pentraxins, C-reactive protein and serum amyloid P component, are cleared and catabolized by hepatocytes in vivo

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Serum amyloid P component in chronic renal failure and dialysis

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Amyloidosis and female protein in the Syrian hamster. Concurrent regulation by sex hormones

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A primed state exists in vivo following histological regression of amyloidosis

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Unaltered susceptibility to BSE in transgenic mice expressing human prion protein.

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Serum amyloid P-component is an acute-phase reactant in the mouse

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