Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Ari J. Salinger"'
Autor:
Gloria Griffante, Francesca Gugliesi, Selina Pasquero, Valentina Dell’Oste, Matteo Biolatti, Ari J. Salinger, Santanu Mondal, Paul R. Thompson, Eranthie Weerapana, Robert J. Lebbink, Jasper A. Soppe, Thomas Stamminger, Virginie Girault, Andreas Pichlmair, Gábor Oroszlán, Donald M. Coen, Marco De Andrea, Santo Landolfo
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Citrullination is a posttranslational modification of arginines. Here, the authors show that HCMV infection increases citrullination of host and virus proteins to promote infection and that citrullinated interferon-inducible protein IFIT1 is impaired
Externí odkaz:
https://doaj.org/article/d9f89f1cfaed42dc92c156e171d58d7e
Autor:
Micaela Tobin, Scott A. Shaffer, Paul R. Thompson, Ari J. Salinger, Aaron J. Maurais, Eranthie Weerapana
Publikováno v:
Biochemistry
Citrullination is an enzyme-catalyzed post-translational modification (PTM) that is essential for a host of biological processes, including gene regulation, programmed cell death, and organ development. While this PTM is required for normal cellular
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::18da52f8262b29b05dba15e1609d5b13
https://pubmed.ncbi.nlm.nih.gov/34491035
https://pubmed.ncbi.nlm.nih.gov/34491035
Autor:
Santanu Mondal, Xuefeng Gong, Xiaoqian Zhang, Ari J. Salinger, Li Zheng, Sudeshna Sen, Eranthie Weerapana, Xuesen Zhang, Paul R. Thompson
Publikováno v:
Angewandte Chemie. 131:12606-12610
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a938f13fda9009e619f0f46e58bf8323
https://doi.org/10.1002/ange.201906334
https://doi.org/10.1002/ange.201906334
Autor:
Santo Landolfo, Jasper A. Soppe, Donald M. Coen, Marco De Andrea, Virginie Girault, Gloria Griffante, Gábor Oroszlán, Thomas Stamminger, Robert Jan Lebbink, Andreas Pichlmair, Santanu Mondal, Ari J. Salinger, Selina Pasquero, Eranthie Weerapana, Matteo Biolatti, Valentina Dell'Oste, Paul R. Thompson, Francesca Gugliesi
Publikováno v:
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
Citrullination is the conversion of arginine-to-citrulline by protein arginine deiminases (PADs), whose dysregulation is implicated in the pathogenesis of various types of cancers and autoimmune diseases. Consistent with the ability of human cytomega
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c678321b2c6cbca792467c5214e13473
Autor:
Venkatesh V. Nemmara, Sarah Gutch, Ronak Tilvawala, Archie C. Reyes, Nicoletta Sorvillo, Denisa D. Wagner, Deya Cherpokova, Paul R. Thompson, Ari J. Salinger, Saeko Fukui
Publikováno v:
Cell Chem Biol
Summary Aberrant protein citrullination is associated with many pathologies; however, the specific effects of this modification remain unknown. We have previously demonstrated that serine protease inhibitors (SERPINs) are highly citrullinated in rheu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6e6ebb43527063d7083d7d8145cce67
https://doi.org/10.1016/j.chembiol.2021.07.009
https://doi.org/10.1016/j.chembiol.2021.07.009
Autor:
Xiaoqian Zhang, Xuefeng Gong, Sudeshna Sen, Ari J. Salinger, Xuesen Zhang, Li Zheng, Paul R. Thompson, Eranthie Weerapana, Santanu Mondal
Publikováno v:
Angew Chem Int Ed Engl
Protein arginine deiminases (PADs) hydrolyze the side chain of arginine to form citrulline. Aberrant PAD activity is associated with rheumatoid arthritis, multiple sclerosis, lupus, and certain cancers. These pathologies established the PADs as thera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2fb4e8e537372710d0e0fd0f649c9a5
https://europepmc.org/articles/PMC6713606/
https://europepmc.org/articles/PMC6713606/
Autor:
Daniella M. Mizurini, Robert J. Seward, Nicoletta Sorvillo, Nathan I. Shapiro, Paul R. Thompson, Ronak Tilvawala, Catherine E. Costello, Caleb Staudinger, Denisa D. Wagner, Eranthie Weerapana, Deya Cherpokova, Carmen H. Coxon, Kimberly Martinod, Ari J. Salinger
Publikováno v:
Circulation research. 125(5)
Rationale: PAD4 (peptidylarginine deiminase type IV), an enzyme essential for neutrophil extracellular trap formation (NETosis), is released together with neutrophil extracellular traps into the extracellular milieu. It citrullinates histones and hol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a0b0670fc1466d7df9806da628b7070
https://pubmed.ncbi.nlm.nih.gov/31415230
https://pubmed.ncbi.nlm.nih.gov/31415230
Autor:
Bo Sun, Paul R. Thompson, Ari J. Salinger, Eranthie Weerapana, Hui-Hsin Chang, Miriam A. Shelef, Mandar Bawadekar, Caitlyn L. Holmes, Beverly Tomita, I-Cheng Ho
Publikováno v:
JCI insight. 4(22)
Dysregulated citrullination, a unique form of posttranslational modification catalyzed by the peptidylarginine deiminases (PADs), has been observed in several human diseases, including rheumatoid arthritis. However, the physiological roles of PADs in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19854ffb31e76b7370fa604b347446c4
https://pubmed.ncbi.nlm.nih.gov/31723060
https://pubmed.ncbi.nlm.nih.gov/31723060
Autor:
Michelle L. Dubuke, Mariana J. Kaplan, A. J. Maurais, Scott A. Shaffer, Carmelo Carmona-Rivera, Paul R. Thompson, Ari J. Salinger, Eranthie Weerapana
Publikováno v:
Sci Immunol
Rheumatoid arthritis (RA) is characterized by synovial joint inflammation and by development of pathogenic humoral and cellular autoimmunity to citrullinated proteins. Neutrophil extracellular traps (NETs) are a source of citrullinated autoantigens a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d35be0574a2e97f0c12de7541b091d23
https://pubmed.ncbi.nlm.nih.gov/28649674
https://pubmed.ncbi.nlm.nih.gov/28649674
Autor:
Sudeshna Sen, Eranthie Weerapana, Li Zheng, Walter Fast, Ari J. Salinger, Paul R. Thompson, Santanu Mondal
Publikováno v:
ACS chemical biology. 14(4)
Nicotinamide N-methytransferase (NNMT) catalyzes the S-adenosyl-L-methionine (SAM)-dependent methylation of nicotinamide (NAM) to form N-methylnicotinamide (Me-NAM). This enzyme detoxifies xenobiotics and regulates NAD(+) biosynthesis. Additionally,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1ad27a2d13d5df282d42595eaba758a
https://pubmed.ncbi.nlm.nih.gov/30933557
https://pubmed.ncbi.nlm.nih.gov/30933557