Structure of a soluble, glycosylated form of the human complement regulatory protein CD59 (Q27729400)

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20 October 2019

title

Structure of a soluble, glycosylated form of the human complement regulatory protein CD59 (English)

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20 October 2019

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2

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20 October 2019

author name string

C M Fletcher

series ordinal

1

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20 October 2019

P J Lachmann

series ordinal

3

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20 October 2019

D Neuhaus

series ordinal

4

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20 October 2019

publication date

1 March 1994

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20 October 2019

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20 October 2019

volume

2

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20 October 2019

issue

3

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20 October 2019

page(s)

185-199

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Membrane defence against complement lysis: the structure and biological properties of CD59.

20 October 2019

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Sequence-specific 1H-NMR assignments and folding topology of human CD59.

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Determination of carboxyl-terminal residue and disulfide bonds of MACIF (CD59), a glycosyl-phosphatidylinositol-anchored membrane protein

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The anatomy and taxonomy of protein structure

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Refined structure of alpha-lytic protease at 1.7 A resolution. Analysis of hydrogen bonding and solvent structure

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CD59, an LY-6-like protein expressed in human lymphoid cells, regulates the action of the complement membrane attack complex on homologous cells

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Identification of the disulfide bonds of human complement C1s.

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Solution structures of two zinc-finger domains from SWI5 obtained using two-dimensional 1H nuclear magnetic resonance spectroscopy. A zinc-finger structure with a third strand of beta-sheet

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Identifiers

DOI

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20 October 2019

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