Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Doron C. Greenbaum"'
Publikováno v:
PLoS Pathogens, Vol 7, Iss 9, p e1002139 (2011)
Trypanosoma cruzi is the causative agent of Chagas' disease. Novel chemotherapy with the drug K11777 targets the major cysteine protease cruzain and disrupts amastigote intracellular development. Nevertheless, the biological role of the protease in i
Externí odkaz:
https://doaj.org/article/eca616ca39be4e849c0472b525006d02
Publikováno v:
Journal of the American Chemical Society
Thioamide quenchers can be paired with compact fluorophores to design “turn-on” fluorescent protease substrates. We have used this method to study a variety of serine-, cysteine-, carboxyl-, and metallo-proteases, including trypsin, chymotrypsin,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d8836ed0302c17f304771d5046e1c9a
https://doi.org/10.1021/ja412297x
https://doi.org/10.1021/ja412297x
Autor:
Doron C. Greenbaum, Todd E. Golde, Jaime Ballard, Bhumit A. Patel, Thierry T. Diagana, A. Taylor Bright, Frantisek Supek, Elizabeth A. Winzeler, Michael B. Harbut, Case W. McNamara, Bryan K. S. Yeung
Publikováno v:
Proceedings of the National Academy of Sciences. 109:21486-21491
Early secretory and endoplasmic reticulum (ER)-localized proteins that are terminally misfolded or misassembled are degraded by a ubiquitin- and proteasome-mediated process known as ER-associated degradation (ERAD). Protozoan pathogens, including the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::951e600982fe2f6387f5d06dc653920d
https://doi.org/10.1073/pnas.1216016110
https://doi.org/10.1073/pnas.1216016110
Autor:
Hyunil Jo, Swapnil J. Kulkarni, Kristin E. Low, William F. DeGrado, Xiaozhen Hu, Doron C. Greenbaum, Peter L. Davies, Nataline Meinhardt, Yibing Wu
Publikováno v:
Journal of the American Chemical Society. 134:17704-17713
We have designed a highly specific inhibitor of calpain by mimicking a natural protein-protein interaction between calpain and its endogenous inhibitor calpastatin. To enable this goal we established a new method of stabilizing an α-helix in a small
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::671f4f9b15fc2ed6bf727819bc946348
https://doi.org/10.1021/ja307599z
https://doi.org/10.1021/ja307599z
Autor:
Nicholas Francella, Farida Korobova, Doron C. Greenbaum, Parris T. Humphrey, Brian McOmber, Dustin Brisson, Özlem Önder
Publikováno v:
Journal of Biological Chemistry. 287:16860-16868
Host-derived proteases are crucial for the successful infection of vertebrates by several pathogens, including the Lyme disease spirochete bacterium, Borrelia burgdorferi. B. burgdorferi must traverse tissue barriers in the tick vector during transmi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5d4016a6887d904dc56bcdd942da0da
https://doi.org/10.1074/jbc.m111.290775
https://doi.org/10.1074/jbc.m111.290775
Autor:
Michael Klemba, Geetha Velmourougane, Seema Dalal, Doron C. Greenbaum, Nataline Meinhardt, Michael B. Harbut, Sheena McGowan, James C. Whisstock, Christine A Oellig
Publikováno v:
Journal of Medicinal Chemistry. 54:1655-1666
The malarial PfA-M1 metallo-aminopeptidase is considered a putative drug target. The natural product dipeptide mimetic, bestatin, is a potent inhibitor of PfA-M1. Herein we present a new, efficient, and high-yielding protocol for the synthesis of bes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de4cd1f54ccf6faec17095997b56f2e9
https://doi.org/10.1021/jm101227t
https://doi.org/10.1021/jm101227t
Autor:
Michael C. Myers, Tianhua Wang, Paul Bates, Huiyan Jing, Rachel Kaletsky, Donna M. Huryn, Scott L. Diamond, Amos B. Smith, Doron C. Greenbaum, Parag P. Shah, Jeremy E. Purvis
Publikováno v:
Molecular Pharmacology
A tetrahydroquinoline oxocarbazate (PubChem CID 23631927) was tested as an inhibitor of human cathepsin L (EC 3.4.22.15) and as an entry blocker of severe acute respiratory syndrome (SARS) coronavirus and Ebola pseudotype virus. In the cathepsin L in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae795f7c933ab565c5702e017d4e3716
Autor:
Rajesh Chandramohanadas, Peter A. Greer, Paul H. Davis, Michael B. Harbut, Geetha Velmourougane, Doron C. Greenbaum, David S. Roos, Claire Darling, Daniel P. Beiting, Ming Yeh Lee
Publikováno v:
Science. 324:794-797
Let Me Out Apicomplexan parasites like Plasmodium falciparum , which causes malaria, and Toxoplasma gondii , which cause toxoplasmosis, replicate inside animal host cells. In order for infections to spread successfully within the host from cell to ce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::434e0829be907072ddbcc281f1c39d33
https://doi.org/10.1126/science.1171085
https://doi.org/10.1126/science.1171085
Autor:
Geetha Velmourougane, Gilana Reiss, Doron C. Greenbaum, Rajesh Chandramohanadas, Michael B. Harbut
Publikováno v:
Bioorganic & Medicinal Chemistry Letters. 18:5932-5936
A novel set of activity-based probes (ABPs) for functionally profiling metallo-aminopeptidases was synthesized based on the bestatin inhibitor scaffold, the first synthesis of bestatin analogues using solid-phase techniques. These ABPs were shown to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7d16b0a28e00e6f04a5c8687043f608
https://doi.org/10.1016/j.bmcl.2008.09.021
https://doi.org/10.1016/j.bmcl.2008.09.021
Autor:
Francesco Leonetti, Matthew Bogyo, Jonathan A. Ellman, Fabien Lecaille, Youngchool Choe, Charles S. Craik, Dieter Brömme, Doron C. Greenbaum
Publikováno v:
Journal of Biological Chemistry. 281:12824-12832
The substrate specificities of papain-like cysteine proteases (clan CA, family C1) papain, bromelain, and human cathepsins L, V, K, S, F, B, and five proteases of parasitic origin were studied using a completely diversified positional scanning synthe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76ffc1dd7c4f94bc9e39eaff7c74bd7c
https://doi.org/10.1074/jbc.m513331200
https://doi.org/10.1074/jbc.m513331200