Biochemical characterization of peptidylarginine deiminase-like orthologs from thermotolerant Emericella dentata and Aspergillus nidulans.
Sign Up to like & getrecommendations! Published in 2019 at "Enzyme and microbial technology"
DOI: 10.1016/j.enzmictec.2019.02.004
Abstract: Peptidylarginine deiminases (PADs) are a group of hydrolases, mediating the deimination of peptidylarginine residues into peptidyl-citrulline. Equivocal protein citrullination by PADs of fungal pathogens has a strong relation to the progression of multiple human diseases,… read more here.
Keywords: peptidylarginine; aspergillus nidulans; dentata nidulans; emericella dentata ... See more keywords
Intrinsic function of the peptidylarginine deiminase PADI4 is dispensable for normal haematopoiesis
Sign Up to like & getrecommendations! Published in 2022 at "Biology Open"
DOI: 10.1242/bio.059143
Abstract: Peptidylarginine deiminases (PADIs) are strongly associated with the development of autoimmunity, neurodegeneration and cancer but their physiological roles are ill-defined. The nuclear deiminase PADI4 regulates pluripotency in the mammalian pre-implantation embryo but its function in… read more here.
Keywords: peptidylarginine; function; padi4 dispensable; development ... See more keywords