Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Eddie L. Angleton"'
Publikováno v:
European Journal of Biochemistry. 269:3969-3977
We have previously demonstrated that Streptococcus pneumoniae signal peptidase (SPase) I catalyzes a self-cleavage to result in a truncated product, SPase37-204 [Peng, S.B., Wang, L., Moomaw, J., Peery, R.B., Sun, P.M., Johnson, R.B., Lu, J., Treadwa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d8c83d40aee537f3b74326d242098c74
https://doi.org/10.1046/j.1432-1033.2002.03083.x
https://doi.org/10.1046/j.1432-1033.2002.03083.x
Autor:
Alexander Wlodawer, Alla Gustchina, Ludmila Reshetnikova, Jacek Lubkowski, Alexander Zdanov, Kwan Y. Hui, Eddie L. Angleton, William G. Farmerie, Maureen M. Goodenow, Deepa Bhatt, Li Zhang, Ben M. Dunn
Publikováno v:
Nature Structural & Molecular Biology. 2:480-488
The crystal structure of a recombinant form of the proteinase encoded by the feline immunodeficiency virus (FIV PR) has been solved at 2 A resolution and refined to an R-factor of 0.148. The refined structure includes a peptidomimetic, statine-based
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3c0c03a568c465e9a3091d8c9d7882e
https://doi.org/10.1038/nsb0695-480
https://doi.org/10.1038/nsb0695-480
Publikováno v:
FEBS Letters. 327:355-360
Through a series of synthetic model peptides, we have examined the structural requirements of the P2 and P3 residues in statine-based HIV protease (PR) inhibitors. Results agree with the general observations that, the more bulky the P3 aromatic hydro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf80a0d6e5180365db2426c3c3652901
https://doi.org/10.1016/0014-5793(93)81020-z
https://doi.org/10.1016/0014-5793(93)81020-z
Publikováno v:
Biochemical and Biophysical Research Communications. 184:790-796
A site-specific proteolytically generated neoamino terminus of the thrombin receptor having a sequence SFLLRNPNDKYEPF- has been reported to be a functional ligand of the receptor. This discovery raises question on the precise structural requirements
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efa7c084705484a84ec9d3d8df2d9d65
https://doi.org/10.1016/0006-291x(92)90659-9
https://doi.org/10.1016/0006-291x(92)90659-9
Autor:
Deborah L. Mullen, Matthew Clemens, Thalia I. Nicas, Sheng-Bin Peng, Richard Craig Thompson, Eddie L. Angleton, Feng Zheng, Palaniappan Kulanthaivel, Matthew D. Belvo, Adam Joseph Kreuzman, James R. Swartling, Louis Nickolaus Jungheim, Tim A. Smitka, Kristina L. Minton, Valentine J. Klimkowski, Mark A. Strege
Publikováno v:
The Journal of biological chemistry. 279(35)
Signal peptidase (SPase) I is responsible for the cleavage of signal peptides of many secreted proteins in bacteria. Because of its unique physiological and biochemical properties, it serves as a potential target for development of novel antibacteria
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cab7394b77c89219d23b84885dc4d03
https://pubmed.ncbi.nlm.nih.gov/15173160
https://pubmed.ncbi.nlm.nih.gov/15173160
Publikováno v:
European journal of biochemistry. 269(16)
We have previously demonstrated that Streptococcus pneumoniae signal peptidase (SPase) I catalyzes a self-cleavage to result in a truncated product, SPase37-204 [Peng, S.B., Wang, L., Moomaw, J., Peery, R.B., Sun, P.M., Johnson, R.B., Lu, J., Treadwa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::3f7db1b050b371f4ce01aaf6113b4aec
https://pubmed.ncbi.nlm.nih.gov/12180973
https://pubmed.ncbi.nlm.nih.gov/12180973
Autor:
Sheng-Bin Peng, Feng Zheng, Eddie L. Angleton, John E. Scott, John R. Carpenter, David L. Smiley
Publikováno v:
Analytical biochemistry. 293(1)
Signal peptidase (SPase) I is responsible for the cleavage of signal peptides of many secreted proteins in bacteria and serves as a potential target for the development of novel antibacterial agents due to its unique physiological and biochemical pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fb12e0b3b4273701d4ed504b7184138
https://pubmed.ncbi.nlm.nih.gov/11373083
https://pubmed.ncbi.nlm.nih.gov/11373083
Autor:
Eddie L. Angleton, William H. Flurkey
Publikováno v:
Phytochemistry. 23:2723-2725
Electrophoretic analysis of polyphenoloxidase isoenzymes from a variety of angiosperms and from mushroom revealed that the enzymes remain active in the presence of 0.1 % sodium dodecylsulfate. Electrophoresis in the presence of sodium dodecylsulfate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::89d211ca5f19843945de74af5bf0f095
https://doi.org/10.1016/0031-9422(84)83003-4
https://doi.org/10.1016/0031-9422(84)83003-4