Zobrazeno 1 - 10
of 28
pro vyhledávání: '"Mitesh, Nagar"'
Publikováno v:
Frontiers in Immunology, Vol 10 (2019)
Protein citrullination is a post-translational modification catalyzed by the protein arginine deiminases (PADs). This modification plays a crucial role in the pathophysiology of numerous autoimmune disorders including RA. Recently, there has been a g
Externí odkaz:
https://doaj.org/article/925855d84a1c41ce82489417d765eb49
Autor:
Mitesh Nagar, Joshua A. Hayden, Einat Sagey, George Worthen, Mika Park, Amar Nath Sharma, Christopher M. Fetter, Oliver P. Kuehm, Stephen L. Bearne
Publikováno v:
Archives of biochemistry and biophysics. 718
The enolase superfamily (ENS) has served as a paradigm for understanding how enzymes that share a conserved structure, as well as a common partial reaction (i.e., metal-assisted, Brønsted base-catalyzed enol(ate) formation), evolved from a common pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e24f538d321659a0dfd09e884a8f0f0c
https://pubmed.ncbi.nlm.nih.gov/35016855
https://pubmed.ncbi.nlm.nih.gov/35016855
Autor:
Sangram S. Parelkar, Li Zheng, Mitesh Nagar, Eranthie Weerapana, Daniel J. Slade, Aaron J. Maurais, Paul R. Thompson, Scott A. Coonrod
Publikováno v:
Biochemistry
Protein arginine deiminases (PADs) are calcium-dependent enzymes that mediate the post-translational conversion of arginine into citrulline. Dysregulated PAD activity is associated with numerous autoimmune disorders and cancers. In breast cancer, PAD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b0d8642df9623a4637b0505744cf7f02
https://doi.org/10.1021/acs.biochem.9b00225
https://doi.org/10.1021/acs.biochem.9b00225
Autor:
Christopher M. Fetter, Mitesh Nagar, Colin D. Douglas, Stephen L. Bearne, Zachary A. Morrison
Publikováno v:
Archives of Biochemistry and Biophysics. 666:116-126
Mandelate racemase (MR) catalyzes the interconversion of the enantiomers of mandelate using a two-base mechanism with Lys 166 acting as the Bronsted base to abstract the α-proton from (S)-mandelate. The resulting intermediate is subsequently re-prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::390c51138419f35d503ed091853eaeb0
https://doi.org/10.1016/j.abb.2019.03.011
https://doi.org/10.1016/j.abb.2019.03.011
Publikováno v:
Protein Engineering, Design and Selection. 31:135-145
Mandelate racemase (MR) serves as a paradigm for our understanding of enzyme-catalyzed deprotonation of a carbon acid substrate. To facilitate structure-function studies on MR using non-natural amino acid substitutions, we engineered the Cys92Ser/Cys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dff5be29441be4bd2cffc422d23419e2
https://doi.org/10.1093/protein/gzy011
https://doi.org/10.1093/protein/gzy011
Autor:
Venkataraman Subramanian, Aaron Muth, Sangram S. Parelkar, Mitesh Nagar, Philip S. Kerry, Kathleen W. Clancy, Hema Srinath, Paul A. McEwan, Paul R. Thompson, Edward Beaumont
Publikováno v:
Journal of Medicinal Chemistry. 60:3198-3211
Protein arginine deiminase 2 (PAD2) plays a key role in the onset and progression of multiple sclerosis, rheumatoid arthritis, and breast cancer. To date, no PAD2-selective inhibitor has been developed. Such a compound will be critical for elucidatin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::561b77dfe7b0e745cc01ee7ec0fb4140
https://doi.org/10.1021/acs.jmedchem.7b00274
https://doi.org/10.1021/acs.jmedchem.7b00274
Publikováno v:
International Journal of Entrepreneurship and Small Business. 43:1
Micro, small and medium enterprises (MSMEs) worldwide differ on the parameters of definitions and the set of challenges faced. Although MSMEs continuously enhance the economic activity of a country, the difficulty in accessing finance slows down thei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4746e1ee13f50977c58b2d03ee7ee55
https://doi.org/10.1504/ijesb.2021.10035619
https://doi.org/10.1504/ijesb.2021.10035619
Autor:
Christopher M, Fetter, Zachary A, Morrison, Mitesh, Nagar, Colin D, Douglas, Stephen L, Bearne
Publikováno v:
Archives of biochemistry and biophysics. 666
Mandelate racemase (MR) catalyzes the interconversion of the enantiomers of mandelate using a two-base mechanism with Lys 166 acting as the Brønsted base to abstract the α-proton from (S)-mandelate. The resulting intermediate is subsequently re-pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::eb65a29bd177504140c6be2eb0e01124
https://pubmed.ncbi.nlm.nih.gov/30935886
https://pubmed.ncbi.nlm.nih.gov/30935886
Publikováno v:
ACS chemical biology. 13(4)
Protein arginine deiminases (PADs) play an important role in the pathogenesis of various diseases, including rheumatoid arthritis, multiple sclerosis, lupus, ulcerative colitis, and breast cancer. Therefore, the development of PAD inhibitors has draw
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::730d54ed2d4d3d33af75446057df2842
https://pubmed.ncbi.nlm.nih.gov/29517899
https://pubmed.ncbi.nlm.nih.gov/29517899
Autor:
Stephen L. Bearne, Mitesh Nagar
Publikováno v:
Biochemistry. 54:6743-6752
Mandelate racemase (MR) catalyzes the interconversion of the enantiomers of mandelate and serves as a paradigm for understanding the enzyme-catalyzed abstraction of an α-proton from a carbon acid substrate with a high pKa. The enzyme utilizes a two-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b91add81e0c41c7156745ca186d95c6b
https://doi.org/10.1021/acs.biochem.5b00982
https://doi.org/10.1021/acs.biochem.5b00982