Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Revansiddha H. Katte"'
Autor:
Revansiddha H. Katte, Yuanyun Ao, Wang Xu, Yang Han, Guohua Zhong, Dibya Ghimire, Jon Florence, Torry A. Tucker, Maolin Lu
Publikováno v:
Viruses, Vol 16, Iss 3, p 391 (2024)
The surface spike (S) glycoprotein mediates cell entry of SARS-CoV-2 into the host through fusion at the plasma membrane or endocytosis. Omicron lineages/sublineages have acquired extensive mutations in S to gain transmissibility advantages and alter
Externí odkaz:
https://doaj.org/article/6c133e0c09264f378e3710df8ec91a44
Publikováno v:
Biomolecules, Vol 11, Iss 5, p 634 (2021)
S100P, a small calcium-binding protein, associates with the p53 protein with micromolar affinity. It has been hypothesized that the oncogenic function of S100P may involve binding-induced inactivation of p53. We used 1H-15N HSQC experiments and molec
Externí odkaz:
https://doaj.org/article/4e0b342771f641d9937f4c96f3e8b05f
Publikováno v:
Biomolecules
Volume 11
Issue 5
Biomolecules, Vol 11, Iss 634, p 634 (2021)
Volume 11
Issue 5
Biomolecules, Vol 11, Iss 634, p 634 (2021)
S100P, a small calcium-binding protein, associates with the p53 protein with micromolar affinity. It has been hypothesized that the oncogenic function of S100P may involve binding-induced inactivation of p53. We used 1H-15N HSQC experiments and molec
Publikováno v:
Archives of biochemistry and biophysics. 691
Metastasis-associated S100A4 protein is a small calcium-binding protein typically overexpressed in several tumor forms, and it is widely accepted that S100A4 plays a significant role in the metastasis of cancer. Tumor suppressor p53 is one of the S10
Publikováno v:
PLoS ONE, Vol 14, Iss 5, p e0216427 (2019)
PLoS ONE
PLoS ONE
In this report, using NMR and molecular modeling, we have studied the structure of lysozyme-S100A6 complex and the influence of tranilast [N-(3, 4-dimethoxycinnamoyl) anthranilic acid], an antiallergic drug which binds to lysozyme, on lysozyme-S100A6
Autor:
Revansiddha H. Katte, Chin Yu
Publikováno v:
PLoS ONE, Vol 13, Iss 6, p e0198767 (2018)
The proteins S100A9 and S100A12 are associated with the human S100 calcium-binding protein family. These proteins promote interaction with target proteins and alter their conformation when they bind to calcium ions in EF-hand motifs. The V domain of