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
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Published: American Society for Biochemistry and Molecular Biology Inc. 2020
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Online Access:https://scholarbank.nus.edu.sg/handle/10635/179259
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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