Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Christopher P. Stuart"'
Autor:
Christopher H Stuart, Kathryn R Riley, Olcay Boyacioglu, Denise M Herpai, Waldemar Debinski, Shadi Qasem, Frank C Marini, Christa L. Colyer, William H Gmeiner
Publikováno v:
Molecular Therapy: Nucleic Acids, Vol 5, Iss C (2016)
Breast cancer (BC) results in ≃40,000 deaths each year in the United States and even among survivors treatment of the disease may have devastating consequences, including increased risk for heart disease and cognitive impairment resulting from the
Externí odkaz:
https://doaj.org/article/c5d25eb2e8074b42a30c604653f5bab8
Autor:
Michael Morgan, Kylia Goodner, James Ross, Angela Z. Poole, Elizabeth Stepp, Christopher H. Stuart, Cydney Wilbanks, Ernesto Weil
Publikováno v:
PeerJ, Vol 3, p e1371 (2015)
Molecular stress responses associated with coral diseases represent an under-studied area of cnidarian transcriptome investigations. Caribbean Yellow Band Disease (CYBD) is considered a disease of Symbiodinium within the tissues of the coral host Orb
Externí odkaz:
https://doaj.org/article/6090f246072640028ce526726520c44d
Autor:
Ilit Noach, Alisdair B. Boraston, Elizabeth Ficko-Blean, Christopher P. Stuart, Warren W. Wakarchuk, Nakita Buenbrazo, Benjamin Pluvinage, Nicole K. Thompson, Hayden McClure
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2021, 118 (10), pp.e2019220118. ⟨10.1073/pnas.2019220118⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2021, 118 (10), pp.e2019220118. ⟨10.1073/pnas.2019220118⟩
International audience; A challenge faced by peptidases is the recognition of highly diverse substrates. A feature of some peptidase families is the capacity to specifically use post-translationally added glycans present on their protein substrates a
Publikováno v:
Molecular Therapy: Nucleic Acids, Vol 2, Iss C (2013)
Treatment with doxorubicin (Dox) results in serious systemic toxicities that limit effectiveness for cancer treatment and cause long-term health issues for cancer patients. We identified a new DNA aptamer to prostate-specific membrane antigen (PSMA)
Externí odkaz:
https://doaj.org/article/7d9b257cd5734385a7b8d4bd3d11c1f0
Autor:
Elizabeth Ficko-Blean, Christopher P Stuart, Michael D Suits, Melissa Cid, Matthew Tessier, Robert J Woods, Alisdair B Boraston
Publikováno v:
PLoS ONE, Vol 7, Iss 3, p e33524 (2012)
CpGH89 is a large multimodular enzyme produced by the human and animal pathogen Clostridium perfringens. The catalytic activity of this exo-α-D-N-acetylglucosaminidase is directed towards a rare carbohydrate motif, N-acetyl-β-D-glucosamine-α-1,4-D
Externí odkaz:
https://doaj.org/article/e051034a95cf40cd84451ba216dbeb77
Autor:
Nakita Buenbrazo, Alisdair B. Boraston, Warren W. Wakarchuk, Benjamin Pluvinage, John E. Burke, Meredith L. Jenkins, Michel Gilbert, Denis Brochu, Christopher P. Stuart, Elizabeth Ficko-Blean, Ilit Noach
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2017, 114 (5), pp.E679-E688. ⟨10.1073/pnas.1615141114⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2017, 114 (5), pp.E679-E688. ⟨10.1073/pnas.1615141114⟩
The vast majority of proteins are posttranslationally altered, with the addition of covalently linked sugars (glycosylation) being one of the most abundant modifications. However, despite the hydrolysis of protein peptide bonds by peptidases being a
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 79:2771-2777
CPF_2247 from Clostridium perfringens ATCC 13124 was identified as a putative carbohydrate-active enzyme by its low sequence identity to endo-β-1,4-glucanases belonging to family 8 of the glycoside hydrolase classification. The X-ray crystal structu
Autor:
Alisdair B. Boraston, Christopher P. Stuart, Michael D. L. Suits, Robert J. Woods, Melissa Cid, Matthew B. Tessier, Elizabeth Ficko-Blean
Publikováno v:
PLoS ONE, Vol 7, Iss 3, p e33524 (2012)
PLoS ONE
PLoS ONE
CpGH89 is a large multimodular enzyme produced by the human and animal pathogen Clostridium perfringens. The catalytic activity of this exo-alpha-D-N-acetylglucosaminidase is directed towards a rare carbohydrate motif, N-acetyl-beta-D-glucosamine-alp
Publikováno v:
Proteins. 79(10)
CPF_2247 from Clostridium perfringens ATCC 13124 was identified as a putative carbohydrate-active enzyme by its low sequence identity to endo-β-1,4-glucanases belonging to family 8 of the glycoside hydrolase classification. The X-ray crystal structu