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Titolo:
THE MOLECULAR-BASIS OF HEREDITARY COMPLEMENT FACTOR-I DEFICIENCY
Autore:
VYSE TJ; MORLEY BJ; BARTOK I; THEODORIDIS EL; DAVIES KA; WEBSTER ADB; WALPORT MJ;
Indirizzi:
HAMMERSMITH HOSP,ROYAL POSTGRAD MED SCH,DEPT MED,RHEUMATOL UNIT,DU CANE RD LONDON W12 0NN ENGLAND HAMMERSMITH HOSP,ROYAL POSTGRAD MED SCH,DEPT MED,RHEUMATOL UNIT LONDON W12 0NN ENGLAND ROYAL FREE HOSP LONDON NW3 ENGLAND
Titolo Testata:
The Journal of clinical investigation
fascicolo: 4, volume: 97, anno: 1996,
pagine: 925 - 933
SICI:
0021-9738(1996)97:4<925:TMOHCF>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
C3B INACTIVATOR DEFICIENCY; RNA SPLICE JUNCTIONS; CRYSTAL-STRUCTURES; THIRD COMPONENT; CELL LINES; FACTOR-H; DNA; PROTEIN; GENE; BIOSYNTHESIS;
Keywords:
COMPLEMENT; FACTOR I; MUTATION; GENETICS; IMMUNODEFICIENCY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
T.J. Vyse et al., "THE MOLECULAR-BASIS OF HEREDITARY COMPLEMENT FACTOR-I DEFICIENCY", The Journal of clinical investigation, 97(4), 1996, pp. 925-933

Abstract

The molecular basis of hereditary complement factor I deficiency is described in two pedigrees. In one pedigree, there were two factor I-deficient siblings, one of whom was asymptomatic and the other suffered from recurrent pyogenic infections. Their factor I mRNA was analyzed by reverse transcription of fibroblast RNA followed by amplification using the polymerase chain reaction. Both siblings were homozygous for the same transversion (adenine to thymine) at nucleotide 1282 in the cDNA. This mutation causes histidine-400 to be replaced by leucine. The altered histidine is a semi-conserved residue within the serine proteinase family, although no function has been ascribed to it. The probandof the second pedigree studied was found to be a compound heterozygote. One allele had the same mutation as the first family, the second allele had a donor splice site mutation that resulted in the deletion ofthe mRNA encoded in the fifth exon (a low-density lipoprotein receptor domain) from its transcript.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 12:32:04