Murine serine proteases MASP-1 and MASP-3, components of the lectin pathway activation complex of complement, are encoded by a single structural gene

Genes and Immunity

Volumn 4, Issue 5, 2003, Pages 374-384

  Stover, C M ^a   Lynch, N J ^a   Dahl, M R ^a   Hanson, S ^a   Takahashi, M ^b   Frankenberger, M ^c   Ziegler Heitbrock, L ^a,c   Eperon, I ^a   Thiel, S ^d   Schwaeble, W J ^a  

^a UNIVERSITY OF LEICESTER   (United Kingdom)

^b FUKUSHIMA MEDICAL UNIVERSITY   (Japan)

^c INSTITUTE OF EPIDEMIOLOGY   (Germany)

^d AARHUS UNIVERSITY   (Denmark)

Author keywords

Alternative splicing polyadenylation; Complement serine proteases; Innate immunity; Lectin pathway

Indexed keywords

COMPLEMENT; COMPLEMENTARY DNA; MANNAN BINDING LECTIN; MESSENGER RNA; SERINE PROTEINASE; MANNAN BINDING LECTIN ASSOCIATED SERINE PROTEINASE; MASP 3 PROTEIN, MOUSE; MASP-3 PROTEIN, MOUSE; PRIMER DNA;

ALTERNATIVE RNA SPLICING; ANIMAL TISSUE; ARTICLE; COMPLEMENT ACTIVATION; COMPLEX FORMATION; CONTROLLED STUDY; COW; GENETIC ASSOCIATION; GENETIC CODE; GENETIC CONSERVATION; GENETIC TRANSCRIPTION; GENOME ANALYSIS; GUINEA PIG; HUMAN; HUMAN TISSUE; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; POLYADENYLATION; PRIORITY JOURNAL; PUFFER FISH; RABBIT; RAT; STRUCTURAL GENE; AMINO ACID SEQUENCE; ANIMAL; COMPARATIVE STUDY; COMPLEMENT LECTIN PATHWAY; DNA SEQUENCE; GENETIC PROCEDURES; GENETICS; METABOLISM; MOLECULAR GENETICS; POLYMERASE CHAIN REACTION; SEQUENCE ALIGNMENT;

CAVIA PORCELLUS; MURINAE; ORYCTOLAGUS CUNICULUS; SUS SCROFA; TETRAODONTIDAE;

ALTERNATIVE SPLICING; AMINO ACID SEQUENCE; ANIMALS; COMPLEMENT PATHWAY, MANNOSE-BINDING LECTIN; CONSERVED SEQUENCE; DNA PRIMERS; DNA, COMPLEMENTARY; MANNOSE-BINDING PROTEIN-ASSOCIATED SERINE PROTEASES; MICE; MOLECULAR PROBE TECHNIQUES; MOLECULAR SEQUENCE DATA; POLYADENYLATION; POLYMERASE CHAIN REACTION; RATS; RNA, MESSENGER; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; SERINE ENDOPEPTIDASES;

EID: 1542602240     PISSN: 14664879     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.gene.6363970     Document Type: Article

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