Mutants of complement component C3 cleaved by the C4-specific C1-s protease. - Wikidata - wikimedia - TriplyDB

Mutants of complement component C3 cleaved by the C4-specific C1-s protease.

Mutants of complement component C3 cleaved by the C4-specific C1-s protease.

http://www.wikidata.org/entity/Q37179898

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Evidence from ion chromatography experiments that met-cars are hollow cage clusters.Identification of residues within the 727-767 segment of human complement component C3 important for its interaction with factor H and with complement receptor 1 (CR1, CD35).

P2860

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P2860

Mutants of complement component C3 cleaved by the C4-specific C1-s protease.

http://www.wikidata.org/entity/Q37179898

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on September 1992

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Mutants of complement component C3 cleaved by the C4-specific C1-s protease.

@en

Mutants of complement component C3 cleaved by the C4-specific C1-s protease.

@nl

type

label

Mutants of complement component C3 cleaved by the C4-specific C1-s protease.

@en

Mutants of complement component C3 cleaved by the C4-specific C1-s protease.

@nl

prefLabel

Mutants of complement component C3 cleaved by the C4-specific C1-s protease.

@en

Mutants of complement component C3 cleaved by the C4-specific C1-s protease.

@nl

P1433

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P2860

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P932

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P356

PNAS.89.17.8125

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Mutants of complement component C3 cleaved by the C4-specific C1-s protease.

@en

P2093

C J Carrillo

http://www.w3.org/2001/XMLSchema#string

N E Zepf

http://www.w3.org/2001/XMLSchema#string

N R Cooper

http://www.w3.org/2001/XMLSchema#string

P Mathias

http://www.w3.org/2001/XMLSchema#string

R T Ogata

http://www.w3.org/2001/XMLSchema#string

P2860

Human complement component C3: cDNA coding sequence and derived primary structure

Complete cDNA sequence of human complement pro-C5. Evidence of truncated transcripts derived from a single copy gene

Molecular organization and function of the complement system

Human complement proteins D, C2, and B. Active site mapping with peptide thioester substrates

Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter

A cDNA cloning vector that permits expression of cDNA inserts in mammalian cells

The coding sequence of the hemolytically inactive C4A6 allotype of human complement component C4 reveals that a single arginine to tryptophan substitution at beta-chain residue 458 is the likely cause of the defect.

Sulfation of tyrosine residues increases activity of the fourth component of complement.

The structural basis of the multiple forms of human complement component C4.

Murine complement component C4 and sex-limited protein: identification of amino acid residues essential for C4 function.

P304

8125-8129

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P31

scholarly article

P356

10.1073/PNAS.89.17.8125

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P407

P433

17

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P478

89

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P577

1992-09-01T00:00:00Z

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P698

1518837

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P932

49869

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