Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Nicholas C Schumann"'
Autor:
Jordan L. Pederick, Birgit I Gaiser, Nicholas C Schumann, Kate L. Wegener, Kwangjun Lee, James Hodgkinson-Bean, Steven W. Polyak, Thomas D. Avery, Grant W. Booker, John B. Bruning, Andrew D. Abell, Wanisa Salaemae, Andrew P. Thompson
Publikováno v:
ACS Chemical Biology. 16:2339-2347
Mycobacterium tuberculosis dethiobiotin synthase (MtDTBS) is a crucial enzyme involved in the biosynthesis of biotin in the causative agent of tuberculosis, M. tuberculosis. Here, we report a binder of MtDTBS, cyclopentylacetic acid 2 (KD = 3.4 ± 0.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5ac2bc6435643604f3c068bed34da81f
https://doi.org/10.1021/acschembio.1c00491
https://doi.org/10.1021/acschembio.1c00491
Autor:
Cory L. Brooks, David A. Ostrov, Nicholas C. Schumann, Schuchi Kakkad, Danmeng Li, Karla Peña, Brady Paul Williams, Nathan E. Goldfarb
Publikováno v:
Biochemical and biophysical research communications. 630
The 2.6 Å crystal structure of the apo form of Hip1 (hydrolase important for pathogenesis) has been previously reported. However, very little is known about the active site architecture of this M. tuberculosis (Mtb), serine hydrolase drug target. To
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1eee51851345f2600b286ce85e2b3250
https://pubmed.ncbi.nlm.nih.gov/36148729
https://pubmed.ncbi.nlm.nih.gov/36148729
Autor:
Nicholas C, Schumann, Kwang Jun, Lee, Andrew P, Thompson, Wanisa, Salaemae, Jordan L, Pederick, Thomas, Avery, Birgit I, Gaiser, James, Hodgkinson-Bean, Grant W, Booker, Steven W, Polyak, John B, Bruning, Kate L, Wegener, Andrew D, Abell
Publikováno v:
ACS chemical biology. 16(11)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8a67d54aea5164bd70befc0f5c2bc214
https://pubmed.ncbi.nlm.nih.gov/34533923
https://pubmed.ncbi.nlm.nih.gov/34533923
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 29:396-399
A series of dipeptide aldehydes containing different N-terminal heterocycles was prepared and assayed in vitro against α-chymotrypsin to ascertain the importance of the heterocycle in maintaining a β-strand geometry while also providing a hydrogen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29aedcc22dc39c9e8535e702f4198401
https://doi.org/10.1016/j.bmcl.2018.12.032
https://doi.org/10.1016/j.bmcl.2018.12.032