Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Austin T. Weigle"'
Autor:
Austin T. Weigle, Diwakar Shukla
Publikováno v:
Communications Biology, Vol 7, Iss 1, Pp 1-14 (2024)
Abstract Transporters are targeted by endogenous metabolites and exogenous molecules to reach cellular destinations, but it is generally not understood how different substrate classes exploit the same transporter’s mechanism. Any disclosure of plas
Externí odkaz:
https://doaj.org/article/c1bcffc6b3b64d1fb47c104ba591e8b7
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-19 (2024)
Abstract With the diversity of lipid-protein interactions, any observed membrane protein dynamics or functions directly depend on the lipid bilayer selection. However, the implications of lipid bilayer choice are seldom considered unless characterist
Externí odkaz:
https://doaj.org/article/62d8f91a34484f779223f442188c10ff
Autor:
Lars H. Kruse, Austin T. Weigle, Mohammad Irfan, Jesús Martínez‐Gómez, Jason D. Chobirko, Jason E. Schaffer, Alexandra A. Bennett, Chelsea D. Specht, Joseph M. Jez, Diwakar Shukla, Gaurav D. Moghe
Publikováno v:
The Plant journal : for cell and molecular biologyREFERENCES. 111(5)
Large enzyme families catalyze metabolic diversification by virtue of their ability to use diverse chemical scaffolds. How enzyme families attain such functional diversity is not clear. Furthermore, duplication and promiscuity in such enzyme families
Publikováno v:
Journal of chemical theory and computation. 17(8)
The realism and accuracy of lipid bilayer simulations through molecular dynamics (MD) is heavily dependent on the lipid composition. While the field is pushing towards implementing more heterogeneous and realistic membrane compositions, a lack of hig
Autor:
Joseph M. Jez, Jesús Martínez-Gómez, Jason E. Schaffer, Diwakar Shukla, Chelsea D. Specht, Gaurav D. Moghe, Chobirko Jd, Austin T. Weigle, Amelia Bennett, Lars H. Kruse
Large enzyme families catalyze metabolic diversification by virtue of their ability to use diverse chemical scaffolds. How enzyme families attain such functional diversity is not clear. Here, we addressed this question using BAHD acyltransferases as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1c3f9532c8277951e99f436bdb6e5845
https://doi.org/10.1101/2020.11.18.385815
https://doi.org/10.1101/2020.11.18.385815
Autor:
Austin T. Weigle, Hannah C. Huff, Aditi Das, William R. Arnold, Lauren N. Carnevale, Justin S. Kim
Publikováno v:
Pharmacol Ther
Cytochrome P450 (CYP) epoxygenases are a special subset of heme-containing CYP enzymes capable of performing the epoxidation of polyunsaturated fatty acids (PUFA) and the metabolism of xenobiotics. This dual functionality positions epoxygenases along
Autor:
Masad J. Damha, Eman A Ageely, Austin T. Weigle, Annabelle Schofield, Keith T. Gagnon, Daniel O'Reilly, Kushal J. Rohilla, Lauren B DeRossett, Maryam Habibian, Zachary J. Kartje, Elise Malek-Adamian, Christopher L. Barkau
Publikováno v:
Nucleic Acids Research
CRISPR (clustered regularly interspaced short palindromic repeat) endonucleases are at the forefront of biotechnology, synthetic biology and gene editing. Methods for controlling enzyme properties promise to improve existing applications and enable n
Publikováno v:
Biophysical Journal. 120:224a