Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Adam Antoszewski"'
Publikováno v:
The Journal of Physical Chemistry B. 125:11637-11649
Therapeutic preparations of insulin often contain phenolic molecules, which can impact both pharmacokinetics and shelf life. Thus, understanding the interactions of insulin and phenolic molecules can aid in designing improved therapeutics. In this st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a67dffd6b6de456bb20628c7f1546fe7
https://doi.org/10.1021/acs.jpcb.1c06544
https://doi.org/10.1021/acs.jpcb.1c06544
Publikováno v:
Biochemistry
Experimental evidence suggests that monomeric insulin exhibits significant conformational heterogeneity, and modifications of apparently disordered regions affect both biological activity and the longevity of pharmaceutical formulations, presumably t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9d9219eb3ef57d3a4126b63e2c065c0e
http://europepmc.org/articles/PMC8552439
http://europepmc.org/articles/PMC8552439
Publikováno v:
J Phys Chem B
Therapeutic preparations of insulin often contain phenolic molecules, which can impact both pharmacokinetics and shelf life. Thus, understanding the interactions of insulin and phenolic molecules can aid in designing improved therapeutics. In this st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c5f49485282a5a3f3e5e4de02f6f6581
https://pubmed.ncbi.nlm.nih.gov/34648712
https://pubmed.ncbi.nlm.nih.gov/34648712
Autor:
John Strahan, Jonathan Weare, Chatipat Lorpaiboon, Adam Antoszewski, Aaron R. Dinner, Bodhi P. Vani
Publikováno v:
J Chem Theory Comput
Elucidating physical mechanisms with statistical confidence from molecular dynamics simulations can be challenging owing to the many degrees of freedom that contribute to collective motions. To address this issue, we recently introduced a dynamical G
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bf6f78da5ae072565f765187bb3f346
https://pubmed.ncbi.nlm.nih.gov/33908762
https://pubmed.ncbi.nlm.nih.gov/33908762
Autor:
Aaron R. Dinner, Chi-Jui Feng, Andrei Tokmakoff, Bodhi P. Vani, Lu Hong, Jonathan Weare, Erik H. Thiede, Adam Antoszewski
Publikováno v:
J Phys Chem B
The protein hormone insulin exists in various oligomeric forms, and a key step in binding its cellular receptor is dissociation of the dimer. This dissociation process and its corresponding association process have come to serve as a paradigms of cou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe8c9c59f8d8f566ef2a8767d02e9a85
