Zobrazeno 1 - 10
of 164
pro vyhledávání: '"Richard W. Vachet"'
Autor:
Anya B. Zhong, Isabella H. Muti, Stephen J. Eyles, Richard W. Vachet, Kristen N. Sikora, Cedric E. Bobst, David Calligaris, Sylwia A. Stopka, Jeffery N. Agar, Chin-Lee Wu, Mari A. Mino-Kenudson, Nathalie Y. R. Agar, David C. Christiani, Igor A. Kaltashov, Leo L. Cheng
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
The status of metabolomics as a scientific branch has evolved from proof-of-concept to applications in science, particularly in medical research. To comprehensively evaluate disease metabolomics, multiplatform approaches of NMR combining with mass sp
Externí odkaz:
https://doaj.org/article/5cfbe20407d341d4a29f4d0281cf00e6
Autor:
Xianzhi Zhang, Yuanchang Liu, Jeerapat Doungchawee, Laura J. Castellanos-García, Kristen N. Sikora, Taewon Jeon, Ritabrita Goswami, Stefano Fedeli, Aarohi Gupta, Rui Huang, Cristina-Maria Hirschbiegel, Roberto Cao-Milán, Prabin K.D. Majhi, Yagiz Anil Cicek, Liang Liu, D. Joseph Jerry, Richard W. Vachet, Vincent M. Rotello
Publikováno v:
Journal of Controlled Release. 357:31-39
Autor:
Zachary J. Kirsch, Jeanna M. Blake, Uyen Huynh, Dheeraj K. Agrohia, Catherine Y. Tremblay, Eric M. Graban, Robert C. Vaughan, Richard W. Vachet
Publikováno v:
Analytical Chemistry. 95:7178-7185
Publikováno v:
Journal of the American Society for Mass Spectrometry. 34:82-91
Membrane-associated proteins are important because they mediate interactions between a cell's external and internal environment and they are often targets of therapeutics. Characterizing their structures and binding interactions, however, is challeng
Autor:
Stacey Nash, Richard W. Vachet
Publikováno v:
Journal of the American Chemical Society. 144:22128-22139
Proteins can adopt different conformational states that are important for their biological function and, in some cases, can be responsible for their dysfunction. The essential roles that proteins play in biological systems make distinguishing the str
Publikováno v:
ACS Biomater Sci Eng
The delivery of functional proteins to the intracellular space offers tremendous advantages for the development of new therapeutics but is limited by the passage of these large polar biomacromolecules through the cell membrane. Noncovalent polymer-pr
Publikováno v:
J Am Soc Mass Spectrom
Characterizing antibody-antigen interactions is necessary for properly developing therapeutic antibodies, understanding their mechanisms of action, and patenting new drug molecules. Here, we demonstrate that hydrogen deuterium exchange (HDX) mass spe
Multisite Labeling of Proteins Using the Ligand-Directed Reactivity of Triggerable Michael Acceptors
Autor:
Myrat Kurbanov, Zachary J. Kirsch, Jithu Krishna, Ranit Dutta, Richard W. Vachet, S. Thayumanavan
Publikováno v:
Bioconjugate Chemistry.
Publikováno v:
J Am Soc Mass Spectrom
Covalent labeling mass spectrometry allows for protein structure elucidation via covalent modification and identification of exposed residues. Diethylpyrocarbonate (DEPC) is a commonly used covalent labeling reagent that provides insight into structu