Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Franklin A, Hays"'
Publikováno v:
Journal of Cardiovascular Development and Disease, Vol 9, Iss 11, p 385 (2022)
Reactive oxygen species (ROS) dysregulation exacerbates many pathologies but must remain within normal ranges to maintain cell function. Since ROS-mediated pathology and routine cell function are coupled, in vivo models evaluating low-ROS background
Externí odkaz:
https://doaj.org/article/1605b33465214434b3a3673b0c630947
Publikováno v:
Cells, Vol 11, Iss 11, p 1855 (2022)
p66Shc is a widely expressed protein that governs a variety of cardiovascular pathologies by generating, and exacerbating, pro-apoptotic ROS signals. Here, we review p66Shc’s connections to reactive oxygen species, expression, localization, and dis
Externí odkaz:
https://doaj.org/article/756a670fb7824329ae9fd195702f9cc3
Autor:
Yingjun Ding, Junxiong Chen, Shuping Li, Jonathan D. Wren, Akhilesh K. Bajpai, Jie Wang, Takemi Tanaka, Heather C. Rice, Franklin A. Hays, Lu Lu, Xin A. Zhang
Publikováno v:
Oncogene. 42:861-868
Publikováno v:
Journal of Extracellular Vesicles, Vol 9, Iss 1 (2020)
Tumour metastasis suppressor KAI1/CD82 inhibits tumour cell movement. As a transmembrane protein, tetraspanin CD82 bridges the interactions between membrane microdomains of lipid rafts and tetraspanin-enriched microdomains (TEMs). In this study, we f
Externí odkaz:
https://doaj.org/article/127229a4e50b4cb88ec76e5bf9f3470b
Autor:
Landon Haslem, Jennifer M. Hays, Hannah Schmitz, Satoshi Matsuzaki, Virginie Sjoelund, Stephanie D. Byrum, Kenneth M. Humphries, J. Kimble Frazer, Borries Demeler, Doris M. Benbrook, Ryan M. Tierney, Kelli D. Duggan, Franklin A. Hays
SUMMARYp66Shc is an oxidoreductase that responds to cell stress by translocating to mitochondria, where p66Shc produces pro-apoptotic reactive oxygen species (ROS). This study identifies ROS-active p66Shc as a monomer that produces superoxide anion i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7d04777717399a20a94b7ee8ef221511
https://doi.org/10.1101/2022.04.14.487897
https://doi.org/10.1101/2022.04.14.487897
Publikováno v:
Methods in Molecular Biology ISBN: 9781071623671
Methods Mol Biol
Methods Mol Biol
Membrane protein (MP) functional and structural characterization requires large quantities of high-purity protein for downstream studies. Barriers to MP characterization include ample overexpression, solubilization, and purification of target protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a40335973dd110fc2822fc9cd88fe727
https://doi.org/10.1007/978-1-0716-2368-8_8
https://doi.org/10.1007/978-1-0716-2368-8_8
Publikováno v:
Molecules, Vol 23, Iss 4, p 732 (2018)
Equilibrative nucleoside transporters (ENTs) are polytopic membrane transporters responsible for the translocation of nucleosides, nucleobases—to a lesser extent—and nucleoside analog therapeutics across cellular membranes. ENTs function in a dif
Externí odkaz:
https://doaj.org/article/1511e5e8a297441081fac0ca02a99cec
Autor:
Landon Haslem, Jennifer M. Hays, Hannah Schmitz, Satoshi Matsuzaki, Virginie Sjoelund, Stephanie D. Byrum, Kenneth M. Humphries, J. Kimble Frazer, Borries Demeler, Doris M. Benbrook, Ryan M. Tierney, Kelli D. Duggan, Franklin Alan Hays
Publikováno v:
SSRN Electronic Journal.
Autor:
Jennifer M, Johnson, Franklin A, Hays
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2025
This chapter outlines a protocol to assess viability for large-scale protein production and purification for selected targets from an initial medium-throughput cloning strategy. Thus, one can assess a broad number of potential candidate proteins, mut
Autor:
Alessandro Senes, Feng He, Xuejun C. Zhang, Justin Kale, Jingzhen Ding, Suzanne M. Lapolla, Samson G.F. Condon, Bo Huang, Zhi Zhang, Jianing Li, Sabareesh Subramaniam, David W. Andrews, Franklin A. Hays, Jialing Lin, Hetal Brahmbhatt, Chenyi Liao
Publikováno v:
The EMBO Journal. 35:208-236
Pro‐apoptotic Bax induces mitochondrial outer membrane permeabilization (MOMP) by forming oligomers through a largely undefined process. Using site‐specific disulfide crosslinking, compartment‐specific chemical labeling, and mutational analysis