Neutron scattering study of the (gamma-B) catalytic domains of complement proteases activated C1r and C1s. (Q46843753)

25 December 2017

title

Neutron scattering study of the (gamma-B) catalytic domains of complement proteases activated C1r and C1s. (English)

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25 December 2017

author name string

Zaccaï G

1

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25 December 2017

Aude CA

2

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25 December 2017

Thielens NM

3

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25 December 2017

Arlaud GJ

4

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25 December 2017

language of work or name

English

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publication date

1 August 1990

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25 December 2017

number of pages

4

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based on heuristic

inferred from page(s)

published in

FEBS Letters

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25 December 2017

volume

269

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25 December 2017

issue

1

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25 December 2017

page(s)

19-22

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25 December 2017

The first component of human complement--C1.

cites work

1 reference

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Human complement component C1s. Partial sequence determination of the heavy chain and identification of the peptide bond cleaved during activation

21 January 2018

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Domain structure and associated functions of subcomponents C1r and C1s of the first component of human complement

21 January 2018

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Functional model of subcomponent C1 of human complement

21 January 2018

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Differential elution of Clq, Clr and Cls from human Cl bound to immune aggregates. Use in the rapid purification of Cl subcomponents

21 January 2018

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Complete amino acid sequence of the catalytic chain of human complement subcomponent C1-r

21 January 2018

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The serine proteinase chain of human complement component C̅1s. Cyanogen bromide cleavage and N-terminal sequences of the fragments

21 January 2018

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Nucleotide sequence of the cDNA coding for human complement C1r

21 January 2018

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Cloning and sequencing of full-length cDNA encoding the precursor of human complement component C1r

21 January 2018

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Complete amino acid sequence of the A chain of human complement-classical-pathway enzyme C1r

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Complete cDNA sequence of human complement Cls and close physical linkage of the homologous genes Cls and Clr.

21 January 2018

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Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence

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Small Angle Neutron Scattering

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Isolation and functional characterization of the proenzyme form of the catalytic domains of human C1r.

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Globular conformation of some ribosomal proteins in solution

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The quaternary structure in solution of human complement subcomponent C1r2C1s2.

21 January 2018

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A functional model of the human C1 complex

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Identification of the peptide bond cleaved during activation of human C1r

21 January 2018

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Molecular characterization of the catalytic domains of human complement serine protease C1r

21 January 2018

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21 January 2018

Identifiers

DOI

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25 December 2017

PubMed ID

2143735

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25 December 2017