Cargando…
Reply to Comment on “Binding Affinity Determines Substrate Specificity and Enables Discovery of substrates for N-Myristoyltransferases”
In our previously published article, an intriguing enzymology observation with the N-myristoyltransferases (NMT1 and NMT2) led us to conclude that binding affinity is important for determining in vivo substrate specificity and this can explain the vast literature that reports the coimmunoprecipitati...
Autores principales: | Su, Dan, Kosciuk, Tatsiana, Lin, Hening |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2022
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9361279/ https://www.ncbi.nlm.nih.gov/pubmed/35966602 http://dx.doi.org/10.1021/acscatal.2c01818 |
Ejemplares similares
-
Binding Affinity Determines Substrate Specificity
and Enables Discovery of Substrates for N-Myristoyltransferases
por: Su, Dan, et al.
Publicado: (2021) -
Discovery of high affinity inhibitors of Leishmania donovani N-myristoyltransferase
por: Rackham, Mark D., et al.
Publicado: (2015) -
NMT1 and NMT2 are lysine myristoyltransferases regulating the ARF6 GTPase cycle
por: Kosciuk, Tatsiana, et al.
Publicado: (2020) -
Discovery of pyridyl-based inhibitors of Plasmodium falciparum N-myristoyltransferase
por: Yu, Zhiyong, et al.
Publicado: (2015) -
Discovery of a Novel Class
of Orally Active Trypanocidal N-Myristoyltransferase
Inhibitors
por: Brand, Stephen, et al.
Publicado: (2011)