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pro vyhledávání: '"Matthew C. Cummins"'
Publikováno v:
bioRxiv
Many protein therapeutics are competitive inhibitors that function by binding to endogenous proteins and preventing them from interacting with native partners. One effective strategy for engineering competitive inhibitors is to graft structural motif
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67771cb90f1728d764674cc125df34ce
https://doi.org/10.1101/2023.03.28.534629
https://doi.org/10.1101/2023.03.28.534629
Autor:
Matthew C. Cummins, Tim M. Jacobs, Frank D. Teets, Frank DiMaio, Ashutosh Tripathy, Brian Kuhlman
Publikováno v:
Protein Sci
Using the molecular modeling program Rosetta, we designed a de novo protein, called SEWN0.1, which binds the heterotrimeric G protein Gα(q.) The design is helical, well‐folded, and primarily monomeric in solution at a concentration of 10 μM. Howe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f8889155264a25ca924fdf9a4d9f85ed
https://doi.org/10.1002/pro.4368
https://doi.org/10.1002/pro.4368
Autor:
Matthew C. Cummins, Tim M. Jacobs, Frank D. Teets, Frank DiMaio, Ashutosh Tripathy, Brian Kuhlman
Using the molecular modeling program Rosetta, we designed a de novo protein, called SEWN0.1, that binds the heterotrimeric G protein Gαq. The design is helical, well-folded, and primarily monomeric in solution at a concentration of 10 uM. However, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d6305df91a845f9fbaf9be7dfe4f6719
https://doi.org/10.1101/2022.02.02.478886
https://doi.org/10.1101/2022.02.02.478886
Publikováno v:
The Journal of Biological Chemistry
During signal transduction, the G protein, Gαq, binds and activates phospholipase C-β isozymes. Several diseases have been shown to manifest upon constitutively activating mutation of Gαq, such as uveal melanoma. Therefore, methods are needed to d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b312183ea3757d6df7e63b851043a207
https://pubmed.ncbi.nlm.nih.gov/34715131
https://pubmed.ncbi.nlm.nih.gov/34715131
Publikováno v:
Scientific Reports
Scientific reports, vol 6, iss 1
Scientific reports, vol 6, iss 1
Extreme acidophiles are capable of growth at pH values near zero. Sustaining life in acidic environments requires extensive adaptations of membranes, proton pumps, and DNA repair mechanisms. Here we describe an adaptation of a core biochemical pathwa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::742b7dac444f8c2267e8459e2fd96d10