Specific Inhibition of Anti-Rh Serum by ‘Unnatural’ Sugars

Nature ◽  
1959 ◽  
Vol 184 (4691) ◽  
pp. 989-990 ◽  
Author(s):  
WILLIAM C. BOYD ◽  
MARJORIE H. McMASTER ◽  
EUGENIA WASZCZENKO-ZACHARCZENKO
Keyword(s):  
Specific Inhibition ◽  
Unnatural Sugars

Selective Destruction of Tumor Cells through Specific Inhibition of Products Resulting from Chromosomal Translocations

2001 ◽  
Vol 1 (2) ◽  
pp. 109-119 ◽  
Author(s):  
A. Rodriguez-Garcia ◽  
M. Sanchez-Martin ◽  
J. Perez-Losada ◽  
P. Perez-Mancera ◽  
A. Sagrera-Aparisi ◽  
...  
Keyword(s):  
Tumor Cells ◽  
Chromosomal Translocations ◽  
Specific Inhibition ◽  
Selective Destruction

The synthesis of novel 6-substituted acyclouridine derivatives which show specific inhibition of HIV-1

1990 ◽  
Vol 55 (s1) ◽  
pp. 89-92 ◽  
Author(s):  
Hiromichi Tanaka ◽  
Masanori Baba ◽  
Masaru Ubasawa ◽  
Hideaki Takashima ◽  
Kouichi Sekiya ◽  
...  
Keyword(s):  
Specific Inhibition ◽  
Hiv 1

scholarly journals trans-Translation inhibitors bind to a novel site on the ribosome and clear Neisseria gonorrhoeae in vivo

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Zachary D. Aron ◽  
Atousa Mehrani ◽  
Eric D. Hoffer ◽  
Kristie L. Connolly ◽  
Pooja Srinivas ◽  
...  
Keyword(s):  
Oral Dose ◽  
Neisseria Gonorrhoeae ◽  
Multiple Drug ◽  
Specific Inhibition ◽  
Drug Resistant ◽  
Peptidyl Transfer ◽  
Bacterial Ribosome ◽  
Multiple Drug Resistant ◽  
Unique Site

AbstractBacterial ribosome rescue pathways that remove ribosomes stalled on mRNAs during translation have been proposed as novel antibiotic targets because they are essential in bacteria and are not conserved in humans. We previously reported the discovery of a family of acylaminooxadiazoles that selectively inhibit trans-translation, the main ribosome rescue pathway in bacteria. Here, we report optimization of the pharmacokinetic and antibiotic properties of the acylaminooxadiazoles, producing MBX-4132, which clears multiple-drug resistant Neisseria gonorrhoeae infection in mice after a single oral dose. Single particle cryogenic-EM studies of non-stop ribosomes show that acylaminooxadiazoles bind to a unique site near the peptidyl-transfer center and significantly alter the conformation of ribosomal protein bL27, suggesting a novel mechanism for specific inhibition of trans-translation by these molecules. These results show that trans-translation is a viable therapeutic target and reveal a new conformation within the bacterial ribosome that may be critical for ribosome rescue pathways.

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