78025-77-1Relevant academic research and scientific papers
A bioorthogonal small-molecule-switch system for controlling protein function in live cells
Liu, Peng,Calderon, Abram,Konstantinidis, Georgios,Hou, Jian,Voss, Stephanie,Chen, Xi,Li, Fu,Banerjee, Soumya,Hoffmann, Jan-Erik,Theiss, Christiane,Dehmelt, Leif,Wu, Yao-Wen
, p. 10049 - 10055 (2015)
Chemically induced dimerization (CID) has proven to be a powerful tool for modulating protein interactions. However, the traditional dimerizer rapamycin has limitations in certain in vivo applications because of its slow reversibility and its affinity for
Small-molecule-targeted protein degradation
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, (2017/09/30)
Certain aspects of the invention relate to compounds, compositions and methods that are useful for treating or preventing a disease in a subject by enhancing the degradation of a protein. In other aspects, said compounds can be useful research tools for i
A rapid and fluorogenic TMP-AcBOPDIPY probe for covalent labeling of proteins in live cells
Liu, Wei,Li, Fu,Chen, Xi,Hou, Jian,Yi, Long,Wu, Yao-Wen
, p. 4468 - 4471 (2014/04/17)
Protein labeling is enormously useful for characterizing protein function in cells and organisms. Chemical tagging methods have emerged as a new generation protein labeling strategy in live cells. Here we have developed a novel and versatile TMP-AcBOPDIPY
Cell compatible trimethoprim-decorated iron oxide nanoparticles bind dihydrofolate reductase for magnetica ly modulating focal adhesion of mammalian cells
Long, Marcus J. C.,Pan, Yue,Lin, Hsin-Chieh,Hedstrom, Lizbeth,Xu, Bing
, p. 10006 - 10009 (2011/08/09)
On the basis of the high affinity binding of trimethoprim (TMP) to Escherichia coli dihydrofolate reductase (eDHFR), TMP-decorated iron oxide nanoparticles bind to eDHFR with high affinity and specificity, which allows magnetic modulation of focal adhesio
Receptor-based design of dihydrofolate reductase inhibitors: Comparison of crystallographically determined enzyme binding with enzyme affinity in a series of carboxy-substituted trimethoprim analogues
Kuyper,Roth,Baccanari,Ferone,Beddell,Champness,Stammers,Dann,Norrington,Baker
, p. 303 - 310 (2007/10/02)
By the use of molecular models of Escherichia coli dihydrofolate reductase (DHFR), analogues of trimethoprim (TMP) were designed which incorporated various 3'-carboxyalkoxy moieties in order to acquire ionic interactions with positively charged active-sit
