Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Valerie T Ressler"'
Autor:
Emily A. Torio, Valerie T. Ressler, Virginia A. Kincaid, Robin Hurst, Mary P. Hall, Lance P. Encell, Kristopher Zimmerman, Stuart K. Forsyth, William M. Rehrauer, Molly A. Accola, Chia-Chang Hsu, Thomas Machleidt, Melanie L. Dart
Publikováno v:
Frontiers in Microbiology, Vol 13 (2022)
Point-of-care tests are highly valuable in providing fast results for medical decisions for greater flexibility in patient care. Many diagnostic tests, such as ELISAs, that are commonly used within clinical laboratory settings require trained technic
Externí odkaz:
https://doaj.org/article/9343fd9d3e9b4dcaa378e95d0d22ecaf
Autor:
Stuart K Forsyth, Emily Jost, Monika G. Wood, Valerie T Ressler, Dan Lazar, Kris Zimmermann, Connor Fitzgerald, Thomas A. Kirkland, Mary P. Hall, Thomas Machleidt, Thomas P. Smith, Kincaid Virginia, Keith V. Wood, Robin Hurst, Lance P. Encell, Melanie Dart
Publikováno v:
Analytical Chemistry. 93:5177-5184
Enzyme-linked immunosorbent assays (ELISAs) are used extensively for the detection and quantification of biomolecules in clinical diagnostics as well as in basic research. Although broadly used, the inherent complexities of ELISAs preclude their util
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f25f1b91446dc05c2258e15579e5bb58
https://doi.org/10.1021/acs.analchem.0c05074
https://doi.org/10.1021/acs.analchem.0c05074
Publikováno v:
ACS Chemical Biology. 14:599-602
A major hurdle in chemical biology is the delivery of native proteins into the cytosol of mammalian cells. Herein, we report that esterification of the carboxyl groups of an enzyme with a diazo compound enables not only its passage into the cytosol,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8d98eac9dd018df0e7ebd87f39382c16
https://doi.org/10.1021/acschembio.9b00033
https://doi.org/10.1021/acschembio.9b00033
Publikováno v:
PMC
Biochemistry
Biochemistry
Copyright © 2020 American Chemical Society. Glycosylation is a common modification that can endow proteins with altered physical and biological properties. Ribonuclease 1 (RNase 1), which is the human homologue of the archetypal enzyme RNase A, unde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67a722e4c962c5b15200305c42c242c7
https://hdl.handle.net/1721.1/132605
https://hdl.handle.net/1721.1/132605
Publikováno v:
RNA. 24:1018-1027
Angiogenin (ANG) is a secretory ribonuclease that promotes the proliferation of endothelial cells, leading to angiogenesis. This function relies on its ribonucleolytic activity, which is low for simple RNA substrates. Upon entry into the cytosol, ANG
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c550b3f51defb2a7df1eea43b0f550bd
https://doi.org/10.1261/rna.065516.117
https://doi.org/10.1261/rna.065516.117
Publikováno v:
The FASEB Journal. 33
Dextrans have proven to be a widely useful class of polysaccharides, with applications ranging from antithrombotic agents to enhancers of vaccine stability. We have examined an unprecedented proper...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::60eb7ba287bedf955709d69040c2a521
https://doi.org/10.1096/fasebj.2019.33.1_supplement.634.7
https://doi.org/10.1096/fasebj.2019.33.1_supplement.634.7
Autor:
Valerie T. Ressler, Ronald T. Raines
Ribonuclease 1 (RNase 1) is the most prevalent human homolog of the archetypal enzyme, RNase A. RNase 1 contains sequons for N-linked glycosylation at Asn34, Asn76, and Asn88 and is N-glycosylated at all three sites in vivo. The effect of N-glycosyla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dabfc594e1872b854bd52de313bacf27
https://europepmc.org/articles/PMC6380942/
https://europepmc.org/articles/PMC6380942/
Autor:
Torio, Emily A., Ressler, Valerie T., Kincaid, Virginia A., Hurst, Robin, Hall, Mary P., Encell, Lance P., Zimmerman, Kristopher, Forsyth, Stuart K., Rehrauer, William M., Accola, Molly A., Hsu, Chia-Chang, Machleidt, Thomas, Dart, Melanie L.
Publikováno v:
Frontiers in Microbiology; 10/26/2022, Vol. 13, p1-13, 13p
Thesis: Ph. D., Massachusetts Institute of Technology, Department of Chemistry, 2019
Cataloged from PDF version of thesis.
Includes bibliographical references (pages 220-236).
Protein modifications are ubiquitous in nature, introducing
Cataloged from PDF version of thesis.
Includes bibliographical references (pages 220-236).
Protein modifications are ubiquitous in nature, introducing
Externí odkaz:
https://hdl.handle.net/1721.1/121784