Mutations in the putative lipid-interaction domain of complement C9 result in defective secretion of the functional protein.
about
Topology of the membrane-bound form of complement protein C9 probed by glycosylation mapping, anti-peptide antibody binding, and disulfide modification.Perforin: structure, function, and role in human immunopathology.A null mutation in the perforin gene impairs cytolytic T lymphocyte- and natural killer cell-mediated cytotoxicity.The mystery behind membrane insertion: a review of the complement membrane attack complexChimeras of human complement C9 reveal the site recognized by complement regulatory protein CD59.An abnormal but functionally active complement component C9 protein found in an Irish family with subtotal C9 deficiency.
P2860
Mutations in the putative lipid-interaction domain of complement C9 result in defective secretion of the functional protein.
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Mutations in the putative lipi ...... ion of the functional protein.
@en
type
label
Mutations in the putative lipi ...... ion of the functional protein.
@en
prefLabel
Mutations in the putative lipi ...... ion of the functional protein.
@en
P2093
P1433
P1476
Mutations in the putative lipi ...... ion of the functional protein.
@en
P2093
P304
P356
10.1016/0161-5890(93)90430-J
P577
1993-01-01T00:00:00Z