peptidylarginine deiminase type IV

Known as: Peptidyl Arginine Deiminase, Type V, EC 3.5.3.15, protein arginine deiminase 4 
Protein-arginine deiminase type-4 (663 aa, ~74 kDa) is encoded by the human PADI4 gene. This protein is involved in the deimination of arginine… (More)
National Institutes of Health

Related topics

Related topics

9 relations
Chromatin Remodeling FactorCytoplasmEnzyme GeneHydrolysis
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Broader (1)

Hydrolase

Papers overview

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Highly Cited
2013
Highly Cited
2013
Porphyromonas gingivalis Facilitates the Development and Progression of Destructive Arthritis through Its Unique Bacterial Peptidylarginine Deiminase (PAD)
Rheumatoid arthritis and periodontitis are two prevalent chronic inflammatory diseases in humans and are associated with each… (More)
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Highly Cited
2009
Highly Cited
2009
Histone hypercitrullination mediates chromatin decondensation and neutrophil extracellular trap formation
Peripheral blood neutrophils form highly decondensed chromatin structures, termed neutrophil extracellular traps (NETs), that… (More)
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Highly Cited
2006
Highly Cited
2006
Increased citrullination of histone H3 in multiple sclerosis brain and animal models of demyelination: a role for tumor necrosis factor-induced peptidylarginine deiminase 4 translocation.
Modification of arginine residues by citrullination is catalyzed by peptidylarginine deiminases (PADs), of which five are known… (More)
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2006
2006
Overexpression of peptidylarginine deiminase IV features in apoptosis of haematopoietic cells
Peptidylarginine deiminases (PADIs) convert peptidylarginine into citrulline via posttranslational modification. One member of… (More)
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Highly Cited
2005
Highly Cited
2005
Humoral immune response to citrullinated collagen type II determinants in early rheumatoid arthritis.
Collagen type II (CII) is a relevant joint-specific autoantigen in the pathogenesis of rheumatoid arthritis (RA). Whereas the… (More)
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Highly Cited
2004
Highly Cited
2004
Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6.
Peptidylarginine deiminases (PADs) convert arginine residues in proteins into citrullines. They are suspected to be involved in… (More)
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Highly Cited
2004
Highly Cited
2004
Human PAD4 regulates histone arginine methylation levels via demethylimination.
Methylation of arginine (Arg) and lysine residues in histones has been correlated with epigenetic forms of gene regulation… (More)
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2003
2003
cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I.
Peptidylarginine deiminases (PADs) catalyse a post-translational modification of proteins through the conversion of arginine… (More)
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Highly Cited
2002
Highly Cited
2002
Nuclear localization of peptidylarginine deiminase V and histone deimination in granulocytes.
Peptidylarginine deiminase (PAD) deiminates arginine residues in proteins to citrulline residues Ca(2+) dependently. There are… (More)
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Highly Cited
2001
Highly Cited
2001
Immunocytochemical localization of peptidylarginine deiminase in human eosinophils and neutrophils.
Peptidylarginine deiminase, registered as PAD V in the DDBJ/GenBank/EMBL data banks, is expressed in HL-60 cells differentiated… (More)
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