Disease-linked mutations in factor H reveal pivotal role of cofactor activity in Self-surface–selective regulation of complement activation

10.1074/jbc.M117.795088

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Main Authors:	Kerr, H, Wong, E, Makou, E, Yang, Y, Marchbank, K, Kavanagh, D, Richards, A, Herbert, A.P, Barlow, P.N
Other Authors:	MEDICINE
Format:	Article
Published:	American Society for Biochemistry and Molecular Biology Inc. 2020
Subjects:	Bins Blood Chemical activation Proteins Age-related macular degeneration Cofactor activity Complement activations Complement control proteins Complement systems Sheep erythrocytes Streptococcus pneumoniae Surface selectivity Disease control complement component C3b complement component C3d complement factor H sialic acid alternative complement pathway C3 C5 convertase bacterial protein CFI protein, human complement factor H, human complement factor I hybrid protein immobilized protein peptide fragment amino acid substitution amino terminal sequence animal cell Article binding affinity binding site biological activity carboxy terminal sequence CCP 1 gene complement activation complement mediated hemolysis controlled study decay accelerating activity disease linked mutation erythrocyte factor I cofactor activity gene gene mutation genetic association hemolysis hemolytic uremic syndrome Komagataella pastoris nonhuman priority journal protein cross linking protein domain protein function protein synthesis regulatory mechanism self surface selective regulation sheep structure activity relation surface property animal chemistry comparative study domestic sheep genetics human macular degeneration metabolism mutation solubility Amino Acid Substitution Animals Atypical Hemolytic Uremic Syndrome Bacterial Proteins Binding Sites Complement Activation Complement C3 Convertase, Alternative Pathway Complement C3d Complement Factor H Complement Factor I Erythrocytes Hemolysis Humans Immobilized Proteins Macular Degeneration Mutation Peptide Fragments Protein Interaction Domains and Motifs Recombinant Fusion Proteins Sheep, Domestic Solubility Surface Properties
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/179259
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1792592024-04-18T03:09:08Z Disease-linked mutations in factor H reveal pivotal role of cofactor activity in Self-surface–selective regulation of complement activation Kerr, H Wong, E Makou, E Yang, Y Marchbank, K Kavanagh, D Richards, A Herbert, A.P Barlow, P.N MEDICINE Bins Blood Chemical activation Proteins Age-related macular degeneration Cofactor activity Complement activations Complement control proteins Complement systems Sheep erythrocytes Streptococcus pneumoniae Surface selectivity Disease control complement component C3b complement component C3d complement factor H sialic acid alternative complement pathway C3 C5 convertase bacterial protein CFI protein, human complement component C3d complement factor H complement factor H, human complement factor I hybrid protein immobilized protein peptide fragment amino acid substitution amino terminal sequence animal cell Article binding affinity binding site biological activity carboxy terminal sequence CCP 1 gene complement activation complement mediated hemolysis controlled study decay accelerating activity disease linked mutation erythrocyte factor I cofactor activity gene gene mutation genetic association hemolysis hemolytic uremic syndrome Komagataella pastoris nonhuman priority journal protein cross linking protein domain protein function protein synthesis regulatory mechanism self surface selective regulation sheep Streptococcus pneumoniae structure activity relation surface property animal chemistry comparative study domestic sheep genetics human macular degeneration metabolism mutation solubility Amino Acid Substitution Animals Atypical Hemolytic Uremic Syndrome Bacterial Proteins Binding Sites Complement Activation Complement C3 Convertase, Alternative Pathway Complement C3d Complement Factor H Complement Factor I Erythrocytes Hemolysis Humans Immobilized Proteins Macular Degeneration Mutation Peptide Fragments Protein Interaction Domains and Motifs Recombinant Fusion Proteins Sheep, Domestic Solubility Streptococcus pneumoniae Surface Properties 10.1074/jbc.M117.795088 Journal of Biological Chemistry 292 32 13345-13360 2020-10-23T02:39:08Z 2020-10-23T02:39:08Z 2017 Article Kerr, H, Wong, E, Makou, E, Yang, Y, Marchbank, K, Kavanagh, D, Richards, A, Herbert, A.P, Barlow, P.N (2017). Disease-linked mutations in factor H reveal pivotal role of cofactor activity in Self-surface–selective regulation of complement activation. Journal of Biological Chemistry 292 (32) : 13345-13360. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.M117.795088 0021-9258 https://scholarbank.nus.edu.sg/handle/10635/179259 Attribution 4.0 International http://creativecommons.org/licenses/by/4.0/ American Society for Biochemistry and Molecular Biology Inc. Unpaywall 20201031
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	Bins Blood Chemical activation Proteins Age-related macular degeneration Cofactor activity Complement activations Complement control proteins Complement systems Sheep erythrocytes Streptococcus pneumoniae Surface selectivity Disease control complement component C3b complement component C3d complement factor H sialic acid alternative complement pathway C3 C5 convertase bacterial protein CFI protein, human complement component C3d complement factor H complement factor H, human complement factor I hybrid protein immobilized protein peptide fragment amino acid substitution amino terminal sequence animal cell Article binding affinity binding site biological activity carboxy terminal sequence CCP 1 gene complement activation complement mediated hemolysis controlled study decay accelerating activity disease linked mutation erythrocyte factor I cofactor activity gene gene mutation genetic association hemolysis hemolytic uremic syndrome Komagataella pastoris nonhuman priority journal protein cross linking protein domain protein function protein synthesis regulatory mechanism self surface selective regulation sheep Streptococcus pneumoniae structure activity relation surface property animal chemistry comparative study domestic sheep genetics human macular degeneration metabolism mutation solubility Amino Acid Substitution Animals Atypical Hemolytic Uremic Syndrome Bacterial Proteins Binding Sites Complement Activation Complement C3 Convertase, Alternative Pathway Complement C3d Complement Factor H Complement Factor I Erythrocytes Hemolysis Humans Immobilized Proteins Macular Degeneration Mutation Peptide Fragments Protein Interaction Domains and Motifs Recombinant Fusion Proteins Sheep, Domestic Solubility Streptococcus pneumoniae Surface Properties
spellingShingle	Bins Blood Chemical activation Proteins Age-related macular degeneration Cofactor activity Complement activations Complement control proteins Complement systems Sheep erythrocytes Streptococcus pneumoniae Surface selectivity Disease control complement component C3b complement component C3d complement factor H sialic acid alternative complement pathway C3 C5 convertase bacterial protein CFI protein, human complement component C3d complement factor H complement factor H, human complement factor I hybrid protein immobilized protein peptide fragment amino acid substitution amino terminal sequence animal cell Article binding affinity binding site biological activity carboxy terminal sequence CCP 1 gene complement activation complement mediated hemolysis controlled study decay accelerating activity disease linked mutation erythrocyte factor I cofactor activity gene gene mutation genetic association hemolysis hemolytic uremic syndrome Komagataella pastoris nonhuman priority journal protein cross linking protein domain protein function protein synthesis regulatory mechanism self surface selective regulation sheep Streptococcus pneumoniae structure activity relation surface property animal chemistry comparative study domestic sheep genetics human macular degeneration metabolism mutation solubility Amino Acid Substitution Animals Atypical Hemolytic Uremic Syndrome Bacterial Proteins Binding Sites Complement Activation Complement C3 Convertase, Alternative Pathway Complement C3d Complement Factor H Complement Factor I Erythrocytes Hemolysis Humans Immobilized Proteins Macular Degeneration Mutation Peptide Fragments Protein Interaction Domains and Motifs Recombinant Fusion Proteins Sheep, Domestic Solubility Streptococcus pneumoniae Surface Properties Kerr, H Wong, E Makou, E Yang, Y Marchbank, K Kavanagh, D Richards, A Herbert, A.P Barlow, P.N Disease-linked mutations in factor H reveal pivotal role of cofactor activity in Self-surface–selective regulation of complement activation
description	10.1074/jbc.M117.795088
author2	MEDICINE
author_facet	MEDICINE Kerr, H Wong, E Makou, E Yang, Y Marchbank, K Kavanagh, D Richards, A Herbert, A.P Barlow, P.N
format	Article
author	Kerr, H Wong, E Makou, E Yang, Y Marchbank, K Kavanagh, D Richards, A Herbert, A.P Barlow, P.N
author_sort	Kerr, H
title	Disease-linked mutations in factor H reveal pivotal role of cofactor activity in Self-surface–selective regulation of complement activation
title_short	Disease-linked mutations in factor H reveal pivotal role of cofactor activity in Self-surface–selective regulation of complement activation
title_full	Disease-linked mutations in factor H reveal pivotal role of cofactor activity in Self-surface–selective regulation of complement activation
title_fullStr	Disease-linked mutations in factor H reveal pivotal role of cofactor activity in Self-surface–selective regulation of complement activation
title_full_unstemmed	Disease-linked mutations in factor H reveal pivotal role of cofactor activity in Self-surface–selective regulation of complement activation
title_sort	disease-linked mutations in factor h reveal pivotal role of cofactor activity in self-surface–selective regulation of complement activation
publisher	American Society for Biochemistry and Molecular Biology Inc.
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/179259
_version_	1800914547215695872

Disease-linked mutations in factor H reveal pivotal role of cofactor activity in Self-surface–selective regulation of complement activation

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