Results 21 to 30 of about 6,832 (204)

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 deiminase 2 regulates expression of DGCR8 affecting miRNA biogenesis in gonadotrope cells. [PDF]

open access: yesReproduction, 2023
In brief: DGCR8 microprocessor complex, which is important for miRNA biogenesis, is regulated by peptidylarginine deiminase 2 and expression fluctuates in gonadotrope cells across the mouse estrous cycle.
Ralston BA   +8 more
europepmc   +2 more sources

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

Peptidylarginine Deiminase Inhibition Abolishes the Production of Large Extracellular Vesicles From Giardia intestinalis, Affecting Host-Pathogen Interactions by Hindering Adhesion to Host Cells [PDF]

open access: yes, 2020
Giardia intestinalis is a microaerophilic protozoan that is an important etiologic agent of diarrhea worldwide. There is evidence that under diverse conditions, the parasite is capable of shedding extracellular vesicles (EVs) which modulate the ...
Palmisano. G.   +19 more
core   +1 more source

Peptidylarginine Deiminase 2 in Host Immunity: Current Insights and Perspectives

open access: yesFrontiers in Immunology, 2021
Peptidylarginine deiminases (PADs) are a group of enzymes that catalyze post-translational modifications of proteins by converting arginine residues into citrullines. Among the five members of the PAD family, PAD2 and PAD4 are the most frequently studied
Zhenyu Wu   +10 more
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

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

Peptidylarginine deiminases and deiminated proteins at the epidermal barrier [PDF]

open access: yesExperimental Dermatology, 2018
AbstractDeimination or citrullination is a post‐translational modification catalysed by a family of calcium‐dependent enzymes called peptidylarginine deiminases (PADs). It corresponds to the transformation of arginine residues within a peptide sequence into citrulline residues. Deimination induces a decreased net charge of targeted proteins; therefore,
Cau, Laura   +2 more
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

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