Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Brent M Dorr"'
Autor:
Maximiliano Figueroa, Nicolas Oliveira, Annabelle Lejeune, Kristian W Kaufmann, Brent M Dorr, André Matagne, Joseph A Martial, Jens Meiler, Cécile Van de Weerdt
Publikováno v:
PLoS ONE, Vol 8, Iss 8, p e71858 (2013)
The computational protein design protocol Rosetta has been applied successfully to a wide variety of protein engineering problems. Here the aim was to test its ability to design de novo a protein adopting the TIM-barrel fold, whose formation requires
Externí odkaz:
https://doaj.org/article/1bd88007f61846ac98c74b30eb162b97
Autor:
Hyun Ok Ham, Zheng Qu, Carolyn A. Haller, Brent M. Dorr, Erbin Dai, Wookhyun Kim, David R. Liu, Elliot L. Chaikof
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-8 (2016)
Bioactive coatings offer a strategy to modulate host response to implants, but their translation to the clinic is hampered by their fast in vivo degradation. Here, the authors use an engineered bacterial protein to regenerate an anti-thrombogenic fil
Externí odkaz:
https://doaj.org/article/67c96988069c478296613a074a5dbf5b
Autor:
Alexandra DeSousa, Christopher J. Podracky, Brent M. Dorr, David R. Liu, Chihui An, Dominic M. Walsh
Publikováno v:
Nature chemical biology. 17(3)
Epitope-specific enzymes are powerful tools for site-specific protein modification but generally require genetic manipulation of the target protein. Here, we describe the laboratory evolution of the bacterial transpeptidase sortase A to recognize the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::842105d48a39f778bed4b9ca73ebb1f6
https://pubmed.ncbi.nlm.nih.gov/33462498
https://pubmed.ncbi.nlm.nih.gov/33462498
Autor:
Dmitry Ter-Ovanesyan, Ulrich A. K. Betz, Brent M. Dorr, Nicolas Rasche, Björn Hock, Marcel Rieker, Jason Tonillo, Harald Kolmar, Stefan Becker
Publikováno v:
Bioconjugate Chemistry. 27:1341-1347
Human growth hormone (hGH) plays an important role during human development and is also an approved therapeutic for the treatment of several diseases. However, one major drawback of hGH is its short circulating half-life requiring frequent administra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc8c974527d8c2ab2419cd35f3f32b6b
https://doi.org/10.1021/acs.bioconjchem.6b00137
https://doi.org/10.1021/acs.bioconjchem.6b00137
Publikováno v:
Proceedings of the National Academy of Sciences. 111:13343-13348
Staphylococcus aureus sortase A catalyzes the transpeptidation of an LPXTG peptide acceptor and a glycine-linked peptide donor and has proven to be a powerful tool for site-specific protein modification. The substrate specificity of sortase A is stri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5023f576d1149c4318ffe510407d99c0
https://doi.org/10.1073/pnas.1411179111
https://doi.org/10.1073/pnas.1411179111
Autor:
Brent M. Dorr, Steven Combs, Joel M. Harp, Carie Fortenberry, Laura S. Mizoue, Will Proffitt, Elizabeth Anne Bowman, Jens Meiler
Publikováno v:
Journal of the American Chemical Society. 133:18026-18029
It has been demonstrated previously that symmetric, homodimeric proteins are energetically favored, which explains their abundance in nature. It has been proposed that such symmetric homodimers underwent gene duplication and fusion to evolve into pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3fd99a523eca4dabddd9110cd1ac440a
https://doi.org/10.1021/ja2051217
https://doi.org/10.1021/ja2051217
Publikováno v:
Proceedings of the National Academy of Sciences. 108:11399-11404
The ability to routinely generate efficient protein catalysts of bond-forming reactions chosen by researchers, rather than nature, is a long-standing goal of the molecular life sciences. Here, we describe a directed evolution strategy for enzymes tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::597b5bf49beafdce708ce6e7e0cb59e3
https://doi.org/10.1073/pnas.1101046108
https://doi.org/10.1073/pnas.1101046108
Publikováno v:
Journal of Molecular Modeling
The burial of hydrophobic amino acids in the protein core is a driving force in protein folding. The extent to which an amino acid interacts with the solvent and the protein core is naturally proportional to the surface area exposed to these environm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a3fea2e2f0a9b1cf690facabd9ef6da
https://doi.org/10.1007/s00894-009-0454-9
https://doi.org/10.1007/s00894-009-0454-9
Autor:
Annabelle Lejeune, André Matagne, Cécile Van de Weerdt, Nicolas Oliveira, Brent M. Dorr, Kristian Kaufmann, Jens Meiler, Joseph Martial, Maximiliano Figueroa
Publikováno v:
PLoS ONE
PLoS ONE, Vol 8, Iss 8, p e71858 (2013)
PLoS ONE, Vol 8, Iss 8, p e71858 (2013)
The computational protein design protocol Rosetta has been applied successfully to a wide variety of protein engineering problems. Here the aim was to test its ability to design de novo a protein adopting the TIM-barrel fold, whose formation requires
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9ce414545c7017dcbe2cfcb0311435fb
http://europepmc.org/articles/PMC3747059
http://europepmc.org/articles/PMC3747059
Autor:
Elliot L. Chaikof, David R. Liu, Carolyn A. Haller, Brent M. Dorr, Ulla M. Marzec, Venkata R. Krishnamurthy, Monica T. Hinds, Zheng Qu, Stephen R. Hanson, Sawan Hurst
Publikováno v:
Advanced healthcare materials. 3(1)
Rapid one-step modification of thrombomodulin with alkylamine derivatives such as azide, biotin, and PEG is achieved using an evolved sortase (eSrtA) mutant. The feasibility of a point-of-care scheme is demonstrated herein to site-specifically immobi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1edee2901569f42c9395a79ee6c7e01c
https://pubmed.ncbi.nlm.nih.gov/23788402
https://pubmed.ncbi.nlm.nih.gov/23788402