Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Yazhuang Dai"'
Publikováno v:
Molecules, Vol 26, Iss 4, p 1151 (2021)
Suramin was initially used to treat African sleeping sickness and has been clinically tested to treat human cancers and HIV infection in the recent years. However, the therapeutic index is low with numerous clinical side-effects, attributed to its di
Externí odkaz:
https://doaj.org/article/2dbddee52bcb41a3b87badcea5646373
Publikováno v:
Acta Biochimica et Biophysica Sinica. 50:1062-1067
Human Raf1 kinase inhibitory protein (hRKIP) is an important modulator of the Ras/Raf1/MEK/ERK signaling pathway. Here, we demonstrated that anti-leprosy drug Clofazimine can bind to hRKIP with a significantly stronger affinity than the endogenous su
Autor:
Huilin Wang, Yazhuang Dai, Xinli Liao, Meijing Hou, Hongwei Yao, Yi Fan, Donghai Lin, Chenyun Guo
Publikováno v:
Biochemical and Biophysical Research Communications. 487:268-273
Ribosomal protein S1 (RpsA), the largest 30S protein in ribosome, plays a significant role in translation and trans-translation. In Mycobacterium tuberculosis, the C-terminus of RpsA is known as tuberculosis drug target of pyrazinoic acid, which inhi
Publikováno v:
European journal of medicinal chemistry. 196
The emergence of antibiotic-resistant Mycobacterium Tuberculosis (Mtb) infections compels new treatment strategies, of which targeting trans-translation is promising. During the trans-translation process, the ribosomal protein S1 (RpsA) plays a key r
Publikováno v:
Molecules
Volume 26
Issue 4
Molecules, Vol 26, Iss 1151, p 1151 (2021)
Volume 26
Issue 4
Molecules, Vol 26, Iss 1151, p 1151 (2021)
Suramin was initially used to treat African sleeping sickness and has been clinically tested to treat human cancers and HIV infection in the recent years. However, the therapeutic index is low with numerous clinical side-effects, attributed to its di
Lead compounds and key residues of ribosomal protein S1 in drug-resistant Mycobacterium tuberculosis
Publikováno v:
Bioorganic chemistry. 82
Ribosomal protein S1 (RpsA) has been identified as a novel target of pyrazinoic acid (POA), which is the active form of pyrazinamide (PZA), in vivo. RpsA plays a crucial role in trans-translation, which is widespread in microbes. In our investigation