C1 inhibitor hinge region mutations produce dysfunction by different mechanisms.
about
Association between the SERPING1 gene and age-related macular degeneration: a two-stage case-control studyPartitioning of serpin-proteinase reactions between stable inhibition and substrate cleavage is regulated by the rate of serpin reactive center loop insertion into beta-sheet A.Crucial residues in the carboxy-terminal end of C1 inhibitor revealed by pathogenic mutants impaired in secretion or function.Exhaustive mutation scanning by fluorescence-assisted mismatch analysis discloses new genotype-phenotype correlations in angiodemaMechanism of action of anti-C1-inhibitor autoantibodies: prevention of the formation of stable C1s-C1-inh complexesGenetic Investigation of Complement Pathway Genes in Type 2 Diabetic Retinopathy: An Inflammatory PerspectiveThe functional integrity of the serpin domain of C1-inhibitor depends on the unique N-terminal domain, as revealed by a pathological mutant.How we manage persons with hereditary angioedema.Serpins in arthropod biology.Unique C1 inhibitor dysfunction in a kindred without angioedema. II. Identification of an Ala443-->Val substitution and functional analysis of the recombinant mutant protein.COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization.Probing the serpin structural-transition mechanism in ovalbumin mutant R339T by proteolytic-cleavage kinetics of the reactive-centre loop.Residues in the human corticosteroid-binding globulin reactive center loop that influence steroid binding before and after elastase cleavage.Association of CFH and SERPING1 polymorphisms with anterior uveitis.
P2860
Q28296326-D14A40A0-2B1D-452C-BC44-DD0C563CDF86Q33179776-5DC8BC17-3A33-4EBF-AC64-8AD31706726DQ34195958-F32B3259-5DE5-4871-92D8-FE361896638FQ35881940-B9283C04-16C9-42A0-80FC-12C031F01B57Q36438218-77DB64C2-B153-4309-9D62-96DE8CA25738Q36632944-3C40680E-027C-450C-ADA9-8D7A879367DCQ38354158-5136328C-F200-40B9-BEBF-0B6B543FD98BQ38806437-20F07171-0228-432C-8F66-FF5CE1C2C7BAQ38948359-4CE79EB8-83A4-44B1-AFD0-033BE93856F2Q41010300-689B2907-918C-4BC2-830D-273F24E85D05Q41370342-A2322C20-2A2D-4551-BA4C-A4B805937A1DQ42157634-13B2744C-7FB1-49F5-943C-7B2DFB3E957CQ45163059-1B4F8BAC-16E2-4C57-9992-7CF59DBCFF74Q45280992-971E31EA-69B0-4DF6-ACC2-1CC92969ED9C
P2860
C1 inhibitor hinge region mutations produce dysfunction by different mechanisms.
description
1992 nî lūn-bûn
@nan
1992 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
name
C1 inhibitor hinge region mutations produce dysfunction by different mechanisms.
@ast
C1 inhibitor hinge region mutations produce dysfunction by different mechanisms.
@en
C1 inhibitor hinge region mutations produce dysfunction by different mechanisms.
@nl
type
label
C1 inhibitor hinge region mutations produce dysfunction by different mechanisms.
@ast
C1 inhibitor hinge region mutations produce dysfunction by different mechanisms.
@en
C1 inhibitor hinge region mutations produce dysfunction by different mechanisms.
@nl
prefLabel
C1 inhibitor hinge region mutations produce dysfunction by different mechanisms.
@ast
C1 inhibitor hinge region mutations produce dysfunction by different mechanisms.
@en
C1 inhibitor hinge region mutations produce dysfunction by different mechanisms.
@nl
P2093
P2860
P356
P1433
P1476
C1 inhibitor hinge region mutations produce dysfunction by different mechanisms.
@en
P2093
Davis AE 3rd
Eldering E
Stecklein HP
P2860
P2888
P304
P356
10.1038/NG0892-354
P407
P577
1992-08-01T00:00:00Z
P6179
1015684306