Results 21 to 30 of about 3,645 (164)

Expression of peptidylarginine deiminase 2 and 4 in malignant mesothelioma and its clinical significance [PDF]

open access: yesJichu yixue yu linchuang, 2023
Objective To investigate the expression of peptidylarginine deiminase 2 and 4 (PAD2 and PAD4) in malignant mesothelioma (MM), their correlation with citrullinated proteins and clinical significance.
GAN Yihan, SHEN Wei, CHEN Yitong, YAN Kaili, HU Shuaiyue, JIANG Zhaoqiang, YING Shibo
doaj   +1 more source

Expression of Peptidylarginine Deiminase Type 4 in Ovarian Tumors [PDF]

open access: yesInternational Journal of Biological Sciences, 2010
Peptidylarginine deiminase type 4 (PADI4) converts arginine residues into citrulline. The current study focused on the expression of PADI4 in various subtypes of ovary cancers, and this study investigated the effects of estrogen on PADI4 expression in ...
Lin Wang, Xiaotian Chang, Guangying Yuan, Yan Zhao, Pengcheng Wang
doaj   +3 more sources

Peptidylarginine deiminases and extracellular vesicles: prospective drug targets and biomarkers in central nervous system diseases and repair

open access: yesNeural Regeneration Research, 2021
Peptidylarginine deiminases are a family of calcium-activated enzymes with multifaceted roles in physiological and pathological processes, including in the central nervous system.
Sigrun Lange
doaj   +1 more source

The virtues and vices of protein citrullination

open access: yesRoyal Society Open Science, 2022
The post-translational modification of proteins expands the regulatory scope of the proteome far beyond what is achievable through genome regulation. The field of protein citrullination has seen significant progress in the last two decades.
Maria A. Christophorou
doaj   +1 more source

Putative Roles for Peptidylarginine Deiminases in COVID-19 [PDF]

open access: yesInternational Journal of Molecular Sciences, 2020
Peptidylarginine deiminases (PADs) are a family of calcium-regulated enzymes that are phylogenetically conserved and cause post-translational deimination/citrullination, contributing to protein moonlighting in health and disease. PADs are implicated in a range of inflammatory and autoimmune conditions, in the regulation of extracellular vesicle (EV ...
Elif Damla Arisan   +2 more
openaire   +2 more sources

Insights into peptidylarginine deiminase expression and citrullination pathways

open access: yesTrends in Cell Biology, 2022
Peptidylarginine deiminases (PADs) are calcium-dependent enzymes that mediate citrullination, an irreversible post-translational modification (PTM). PAD enzymes have received increasing attention in (patho-)physiology since multi-omics analysis accelerated their expression profiling.
Yu, Karen, Proost, Paul
openaire   +2 more sources

Current Challenges and Limitations in Antibody-Based Detection of Citrullinated Histones

open access: yesFrontiers in Immunology, 2016
Studies on NETosis demand reliable and convenient markers to monitor the progress of this form of cell death. Because a determining step in the release of nuclear chromatin NETs requires the conversion of arginine residues to citrulline residues in ...
Indira Neeli, Marko Radic
doaj   +1 more source

Deimination and Peptidylarginine Deiminases in Skin Physiology and Diseases [PDF]

open access: yesInternational Journal of Molecular Sciences, 2020
Deimination, also known as citrullination, corresponds to the conversion of the amino acid arginine, within a peptide sequence, into the non-standard amino acid citrulline. This post-translational modification is catalyzed by a family of calcium-dependent enzymes called peptidylarginine deiminases (PADs).
Mechin, Marie-Claire   +2 more
openaire   +3 more sources

Porphyromonas gingivalis exacerbates ulcerative colitis via Porphyromonas gingivalis peptidylarginine deiminase

open access: yesInternational Journal of Oral Science, 2021
Ulcerative Colitis (UC) has been reported to be related to Porphyromonas gingivalis (P. gingivalis). Porphyromonas gingivalis peptidylarginine deiminase (PPAD), a virulence factor released by P. gingivalis, is known to induce inflammatory responses.
Xida Zhao   +10 more
doaj   +1 more source

Functional role of dimerization of human peptidylarginine deiminase 4 (PAD4). [PDF]

open access: yesPLoS ONE, 2011
Peptidylarginine deiminase 4 (PAD4) is a homodimeric enzyme that catalyzes Ca²⁺-dependent protein citrullination, which results in the conversion of arginine to citrulline.
Yi-Liang Liu   +3 more
doaj   +1 more source

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