Results 11 to 20 of about 1,668 (171)

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

Frontiers in Cellular and Infection Microbiology, 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 ...
Bruno Gavinho, Bruna Sabatke, Veronica Feijoli, Izadora Volpato Rossi, Janaina Macedo da Silva, Ingrid Evans-Osses, Giuseppe Palmisano, Sigrun Lange, Marcel Ivan Ramirez, Marcel Ivan Ramirez   +9 more
doaj   +2 more sources

In vivo expression of peptidylarginine deiminase in Drosophila melanogaster.

PLoS ONE, 2020
Peptidylarginine deiminase (PAD) modifies peptidylarginine and converts it to peptidylcitrulline in the presence of elevated calcium. Protein modification can lead to severe changes in protein structure and function, and aberrant PAD activity is linked ...
Olena Mahneva, Monica G Risley, Ciny John, Sarah L Milton, Ken Dawson-Scully, William W Ja   +5 more
doaj   +2 more sources

Peptidylarginine deiminase (PAD) 6 is essential for oocyte cytoskeletal sheet formation and female fertility [PDF]

Molecular and Cellular Endocrinology, 2007
Peptidylarginine deiminase 6 (PAD6) is an enzyme that is uniquely expressed in male and female germ cells. To study the function of this enzyme in vivo we generated mice deficient for PAD6. Here we show that inactivation of the PAD6 gene in mice leads to female infertility whereas male fertility is not affected.
Esposito, G., Vitale, A., Leitjen, F., Strik, A., Koonen-Reemst, A. B., Yurttas, P., Robben, T. A., Coonrod, S., Gossen, J.   +8 more
openaire   +5 more sources

Release of active peptidylarginine deiminase into the circulation during acute inflammation induced by coronary artery bypass surgery

Journal of Inflammation Research, 2019
Anne Vejlstrup,1 Ann Merete Møller,2 Claus Henrik Nielsen,1,3,* Dres Damgaard1,3,*1Institute for Inflammation Research, Center for Rheumatology and Spine Diseases, Copenhagen University Hospital, Rigshospitalet, Copenhagen, Denmark; 2Department of
Vejlstrup A, Møller AM, Nielsen CH, Damgaard D   +3 more
doaj   +1 more source

Beyond PAD Inhibition: Emerging Avenues and Natural Products for Targeting Citrullination in Immune Diseases [PDF]

Biomedicines
Immune-mediated inflammatory diseases, such as rheumatoid arthritis, multiple sclerosis, and systemic lupus erythematosus, impose a severe and growing global health burden, where current therapies are limited by poor specificity and significant side ...
Qilei Chen, Yuhang Ma, Yingyi Liu, Xiaojie Wang, Guanhua Huang, Yizhao Yang, Joshua Ka-Shun Ko, Hubiao Chen   +7 more
doaj   +2 more sources

Porphyromonas gingivalis peptidylarginine deiminase, a key contributor in the pathogenesis of experimental periodontal disease and experimental arthritis. [PDF]

PLoS ONE, 2014
ObjectivesTo investigate the suggested role of Porphyromonas gingivalis peptidylarginine deiminase (PAD) in the relationship between the aetiology of periodontal disease and experimentally induced arthritis and the possible association between these two ...
Neville Gully, Richard Bright, Victor Marino, Ceilidh Marchant, Melissa Cantley, David Haynes, Catherine Butler, Stuart Dashper, Eric Reynolds, Mark Bartold   +9 more
doaj   +3 more sources

Crystal structure of human peptidylarginine deiminase type VI (PAD6) provides insights into its inactivity [PDF]

IUCrJ
Human peptidylarginine deiminase isoform VI (PAD6), which is predominantly limited to cytoplasmic lattices in the mammalian oocytes in ovarian tissue, is essential for female fertility.
Fanomezana M. Ranaivoson, Rieke Bande, Isabell Cardaun, Antonio De Riso, Annette Gärtner, Pui Loke, Christina Reinisch, Prasuna Vogirala, Edward Beaumont   +8 more
doaj   +2 more sources

Peptidylarginine Deiminase Inhibitors Reduce Bacterial Membrane Vesicle Release and Sensitize Bacteria to Antibiotic Treatment [PDF]

Frontiers in Cellular and Infection Microbiology, 2019
Outer membrane and membrane vesicles (OMV/MV) are released from bacteria and participate in cell communication, biofilm formation and host-pathogen interactions. Peptidylarginine deiminases (PADs) are phylogenetically conserved enzymes that catalyze post-
Uchini S. Kosgodage, Paul Matewele, Giulia Mastroianni, Igor Kraev, Dominik Brotherton, Brigitte Awamaria, Anthony P. Nicholas, Sigrun Lange, Jameel M. Inal   +8 more
doaj   +2 more sources

Activation of Peptidylarginine Deiminase in the Salivary Glands of Balb/c Mice Drives the Citrullination of Ro and La Ribonucleoproteins [PDF]

Journal of Immunology Research, 2017
The goal of the present study was to determine whether peptidylarginine deiminase PAD2 and PAD4 enzymes are present in Balb/c mouse salivary glands and whether they are able to citrullinate Ro and La ribonucleoproteins.
Mayra Rodríguez-Rodríguez, Rafael Herrera-Esparza, Juan-José Bollain y Goytia, María-Elena Pérez-Pérez, Deyanira Pacheco-Tovar, Jessica Murillo-Vázquez, Guadalupe Pacheco-Tovar, Esperanza Avalos-Díaz   +7 more
doaj   +2 more sources

Generation and characterisation of Porphyromonas gingivalis mutant lacking peptidylarginine deiminase activity

Journal of Oral Microbiology, 2017
Porphyromonas gingivalis peptidylarginine deiminase (PPAD) is the focus of several studies due to its ability to citrullinate in vitro human proteins, which have been linked to the aetiopathogenesis of rheumatoid arthritis (RA).
Estefanía Muñoz-Atienza, Joseph Aduse-Opoku, Magdalena B. Flak, Nikolay A. Paramonov, Costantino Pitzalis, Michael A. Curtis   +5 more
doaj   +2 more sources