Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Douglas S MacPherson"'
Autor:
Douglas S. MacPherson, Dobeen Hwang, Samantha M. Sarrett, Outi Keinänen, Cindy Rodriguez, Christoph Rader, Brian M. Zeglis
Publikováno v:
Mol Pharm
Site-specifically modified radioimmunoconjugates exhibit superior in vitro and in vivo behavior compared to analogues synthesized via traditional stochastic methods. However, the development of approaches to site-specific bioconjugation that combine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44eaaf5f34f272baab167425e39bbe17
https://doi.org/10.1021/acs.molpharmaceut.2c00700
https://doi.org/10.1021/acs.molpharmaceut.2c00700
Publikováno v:
ACS Biomater Sci Eng
Matrix metalloproteinase (MMP) enzymes are over-expressed by some metastatic cancers, in which they are responsible for the degradation and remodeling of the extracellular matrix. In recent years, MMPs have emerged as promising targets for enzyme-res
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b55658a0b6c6bd32570d5da3fd5fc2e3
https://doi.org/10.1021/acsbiomaterials.1c01488
https://doi.org/10.1021/acsbiomaterials.1c01488
Publikováno v:
Dalton Trans
Metallic radionuclides have been instrumental in the field of nuclear imaging for over half a century. While recent years have played witness to a dramatic rise in the use of radiometals as labels for chelator-bearing biomolecules, imaging agents bas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77dde511067ea6df2df4b33b8f5be424
https://pubmed.ncbi.nlm.nih.gov/31556418
https://pubmed.ncbi.nlm.nih.gov/31556418
Autor:
Charles Maldarelli, Charalampos G. Pappas, V. Narang, Chunqiu Zhang, Ayala Lampel, Douglas S MacPherson, Rein V. Ulijn, Tong Wang, Ramim Shafi
Publikováno v:
Angewandte Chemie (International ed. in English). 56(46)
The reversible regulation of catalytic activity is a feature found in natural enzymes which is not commonly observed in artificial catalytic systems. Here, we fabricate an artificial hydrolase with pH-switchable activity, achieved by introducing a ca
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1109666107ca8a8ad1908d3636cbe879
https://pubmed.ncbi.nlm.nih.gov/28941038
https://pubmed.ncbi.nlm.nih.gov/28941038