Výsledky vyhledávání - "MESH: Citrulline / metabolism"

Peptidylarginine Deiminase Inhibitor Cl-Amidine Attenuates Cornification and Interferes with the Regulation of Autophagy in Reconstructed Human Epidermis

Autor: Paul R. Thompson, Hidenari Takahara, Laura Cau, Guy Serre, Michel Simon, Marie-Claire Méchin

Publikováno v: Journal of Investigative Dermatology
Journal of Investigative Dermatology, 2019, 139 (9), pp.1889-1897.e4. ⟨10.1016/j.jid.2019.02.026⟩
Journal of Investigative Dermatology, Nature Publishing Group, 2019, 139 (9), pp.1889-1897.e4. ⟨10.1016/j.jid.2019.02.026⟩
J Invest Dermatol

International audience; Deimination, a post-translational modification catalyzed by a family of enzymes called peptidylarginine deiminases (PADs), is the conversion of arginine into citrulline residues in a protein. Deimination has been associated wi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93f9749a5b19b13328a286eb478c2584
https://ut3-toulouseinp.hal.science/hal-03156447/document

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Peptidylarginine deiminases and deiminated proteins at the epidermal barrier

Autor: Laura Cau, Marie-Claire Méchin, Michel Simon

Publikováno v: Experimental Dermatology
Experimental Dermatology, Wiley, 2018, 27 (8), pp.852-858. ⟨10.1111/exd.13684⟩

International audience; Deimination 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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3daf24eddf486c89abbd25e731b97a9b
https://pubmed.ncbi.nlm.nih.gov/29756256

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Immune tolerance induction with multiepitope peptide derived from citrullinated autoantigens attenuates arthritis manifestations in adjuvant arthritis rats

Autor: Howard Amital, Yehuda Shoenfeld, Smadar Gertel, Guy Serre

Publikováno v: Journal of Immunology
Journal of Immunology, Publisher : Baltimore : Williams & Wilkins, c1950-. Latest Publisher : Bethesda, MD : American Association of Immunologists, 2015, 194 (12), pp.5674-5680. ⟨10.4049/jimmunol.1402457⟩
Journal of Immunology, 2015, 194 (12), pp.5674-5680. ⟨10.4049/jimmunol.1402457⟩

Citrullinated peptides are major targets of disease-specific autoantibodies in rheumatoid arthritis. Currently, citrullinated peptides are used as biomarkers for diagnosing rheumatoid arthritis by measuring anti-citrullinated protein Ab (ACPA) titers

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::39d48c500831826e67c9549df5de0617
https://pubmed.ncbi.nlm.nih.gov/25964493

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The fibrin-derived citrullinated peptide β60–74Cit 60,72,74 bears the major ACPA epitope recognised by the rheumatoid arthritis-specific anticitrullinated fibrinogen autoantibodies and anti-CCP2 antibodies

Autor: Adeline Ruyssen-Witrand, Leonor Nogueira, Ferenc Hudecz, M Cornillet, Anna Magyar, Fruzsina Babos, Alain Cantagrel, Guy Serre, Mireille Sebbag, E Verrouil

Publikováno v: Annals of the Rheumatic Diseases
Annals of the Rheumatic Diseases, BMJ Publishing Group, 2014, 73 (6), pp.1246-1252. ⟨10.1136/annrheumdis-2012-202868⟩

Objectives To evaluate the proportions of rheumatoid arthritis (RA) sera containing anticitrullinated proteins autoantibodies (ACPA) reactive to α36–50Cit 38,42 and/or β60–74Cit 60,72,74 , two peptides identified as bearing the immunodominant e

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3585764dcf2a928c19b3514cf1be60d
https://hal-univ-tlse3.archives-ouvertes.fr/hal-03154569

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