Zobrazeno 1 - 10
of 153
pro vyhledávání: '"A. O. Stevens"'
Publikováno v:
Pathogens, Vol 13, Iss 10, p 902 (2024)
Endocytosis plays a complex role in pathogen-host interactions. It serves as a pathway for pathogens to enter the host cell and acts as a part of the immune defense mechanism. Endocytosis involves the formation of lipid membrane vesicles and the resh
Externí odkaz:
https://doaj.org/article/6ffa2ff543304e5cbc5bd2d7d4187d86
Publikováno v:
Biology, Vol 12, Iss 6, p 796 (2023)
The canonical ASC domains, PYD and CARD, are interconnected by a lengthy, semi-flexible linker. The molecular basis and purpose of ASC’s highly dynamic feature remain elusive. In this study, all-atom molecular dynamics simulations were utilized to
Externí odkaz:
https://doaj.org/article/eb90a114407f42ff80accd35a8ed950a
Publikováno v:
Cells, Vol 11, Iss 15, p 2451 (2022)
The PDZ family has drawn attention as possible drug targets because of the domains’ wide ranges of function and highly conserved binding pockets. The PICK1 PDZ domain has been proposed as a possible drug target because the interactions between the
Externí odkaz:
https://doaj.org/article/a817c33f3ee24961a30d9f7b8ed34db8
Autor:
Amy O. Stevens, Yi He
Publikováno v:
Biomolecules, Vol 12, Iss 7, p 985 (2022)
The inhibition of protein–protein interactions is a growing strategy in drug development. In addition to structured regions, many protein loop regions are involved in protein–protein interactions and thus have been identified as potential drug ta
Externí odkaz:
https://doaj.org/article/f3801f2eba4c4188b0e07e7b86006b74
Autor:
Amy O. Stevens, Yi He
Publikováno v:
Frontiers in Molecular Biosciences, Vol 7 (2021)
PICK1 is a multi-domain scaffolding protein that is uniquely comprised of both a PDZ domain and a BAR domain. While previous experiments have shown that the PDZ domain and the linker positively regulate the BAR domain and the C-terminus negatively re
Externí odkaz:
https://doaj.org/article/aa14ecf36b774bc480c88513db1f47e3
Autor:
Amy O. Stevens, Yi He
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 3, p 1454 (2022)
Dynamic allosterism allows the propagation of signal throughout a protein. The PDZ (PSD-95/Dlg1/ZO-1) family has been named as a classic example of dynamic allostery in small modular domains. While the PDZ family consists of more than 200 domains, pr
Externí odkaz:
https://doaj.org/article/4c4bab59feb549f482fb208aae6a493b
Autor:
O Stevens
Publikováno v:
Critical and Radical Social Work. 10:422-437
This rapid review explores research that relates to trans people and social work, with the aim of investigating the experiences of trans people in social work. The article is concerned exclusively with research that platforms the voices of trans peop
Autor:
Tongtong Li, Stefano Motta, Amy O. Stevens, Shenghan Song, Emily Hendrix, Alessandro Pandini, Yi He
Publikováno v:
JACS Au. 2:1935-1945
Supporting Information: The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/jacsau.2c00358. MD and SMD simulation parameters, data analysis details of all 50 replicas of SMD simulations, all pre-processed simula
Publikováno v:
Current Protein & Peptide Science. 24
Introduction: Bin/Amphiphysin/Rvs167 (BAR) domain superfamily proteins are considered to be able to induce membrane curvature. PICK1 is a unique protein consisting of both a PDZ and a BAR domain that has been associated with many diseases. PICK1 can
Publikováno v:
Protein science : a publication of the Protein Society. 31(12)
The PDZ family is comprised of small modular domains that play critical roles in the allosteric modulation of many cellular signaling processes by binding to the C-terminal tail of different proteins. As dominant modular proteins that interact with a