Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Grant E Frahm"'
Autor:
Christian C Luebbert, Tessa M Clarke, Roberta Pointet, Grant E Frahm, Sharon Tam, Barry Lorbetskie, Simon Sauvé, Michael J W Johnston
Publikováno v:
PLoS ONE, Vol 12, Iss 12, p e0189814 (2017)
We have previously identified extensive glycation, bound fatty acids and increased quantities of protein aggregates in commercially available recombinant HSA (rHSA) expressed in Oryza sativa (Asian rice) (OsrHSA) when compared to rHSA from other expr
Externí odkaz:
https://doaj.org/article/1596bad85fcf497b959640f480c17d61
Publikováno v:
PLoS ONE, Vol 11, Iss 2, p e0150229 (2016)
Microflow digital imaging (MDI) has become a widely accepted method for assessing sub-visible particles in pharmaceutical formulations however, to date; no data have been presented on the utility of this methodology when formulations include opaque v
Externí odkaz:
https://doaj.org/article/45bdf6880cf24597b69144df91ec2088
Autor:
Grant E Frahm, Daryl G S Smith, Anita Kane, Barry Lorbetskie, Terry D Cyr, Michel Girard, Michael J W Johnston
Publikováno v:
PLoS ONE, Vol 9, Iss 10, p e109893 (2014)
The use of different expression systems to produce the same recombinant human protein can result in expression-dependent chemical modifications (CMs) leading to variability of structure, stability and immunogenicity. Of particular interest are recomb
Externí odkaz:
https://doaj.org/article/a8433f41fbf446fdb4d542f13b7782e7
Autor:
Shan Zou, Zygmunt J. Jakubek, Raisa Rahman, Michael V. Johnston, Rola Mansa, Christian C. Luebbert, Grant E. Frahm
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-11 (2021)
Scientific Reports
Scientific Reports
The development of reference standards for nanoparticle sizing allows for cross laboratory studies and effective transfer of particle sizing methodology. To facilitate this, these reference standards must be stable upon long-term storage. Here, we ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da577afc1484c9cafd04b6f35a67f983
https://doaj.org/article/a70c2e3ff8ec46fc836e709e22829d94
https://doaj.org/article/a70c2e3ff8ec46fc836e709e22829d94
Publikováno v:
ACS Omega
ACS Omega, Vol 5, Iss 49, Pp 31845-31857 (2020)
ACS Omega, Vol 5, Iss 49, Pp 31845-31857 (2020)
Product excipients are used to confer a number of desirable properties on the drug substance to maintain or improve stability and facilitate drug delivery. This is especially important for products where the active pharmaceutical ingredient (API) is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::19f1eee74514b995201a4cfff6505dff
https://doi.org/10.1021/acsomega.0c04692
https://doi.org/10.1021/acsomega.0c04692
Autor:
Simon Sauvé, Christian C. Luebbert, Grant E. Frahm, Michael V. Johnston, Roberta Pointet, Tessa M. Clarke, Barry Lorbetskie, Sharon Tam
Publikováno v:
PLoS ONE
PLoS ONE, Vol 12, Iss 12, p e0189814 (2017)
PLoS ONE, Vol 12, Iss 12, p e0189814 (2017)
We have previously identified extensive glycation, bound fatty acids and increased quantities of protein aggregates in commercially available recombinant HSA (rHSA) expressed in Oryza sativa (Asian rice) (OsrHSA) when compared to rHSA from other expr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f64e611605ce6385a35d74d9e1c3d414
http://europepmc.org/articles/PMC5744977
http://europepmc.org/articles/PMC5744977
Publikováno v:
Journal of Liposome Research. 23:101-109
At elevated temperatures, studies have shown that serum albumin undergoes irreversible changes to its secondary structure. Anionic fatty acids and/or anionic surfactants have been shown to stabilize human serum albumin (HSA) against thermal denaturat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::091d91411d664cfa4e51280e3cf703e1
https://doi.org/10.3109/08982104.2012.747535
https://doi.org/10.3109/08982104.2012.747535
Publikováno v:
Bioconjugate chemistry. 27(6)
A pH-driven DNA nanomachine based on the human α-thrombin binding aptamer was designed for the specific catch-and-release of human α-thrombin at neutral and acidic pH, respectively. In neutral conditions, the thrombin aptamer component of the nanom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d64f8af23b83d5bd2efa64e1d7ad0d53
https://pubmed.ncbi.nlm.nih.gov/27115292
https://pubmed.ncbi.nlm.nih.gov/27115292
Publikováno v:
The Journal of Physical Chemistry B. 116:4661-4670
Previous studies have demonstrated that liposome-protein interactions can result in changes to the thermal stability of the protein. We utilized far-UV circular dichroism spectropolarimetry and fluorescence spectroscopy to investigate the interaction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab4eb095901addcb2d395cae28aaa0f3
https://doi.org/10.1021/jp2125729
https://doi.org/10.1021/jp2125729
Autor:
Anita Kane, Grant E. Frahm, Daryl G.S. Smith, Michel Girard, Terry D. Cyr, Michael V. Johnston, Barry Lorbetskie
Publikováno v:
PLoS ONE
PLoS ONE, Vol 9, Iss 10, p e109893 (2014)
PLoS ONE, Vol 9, Iss 10, p e109893 (2014)
The use of different expression systems to produce the same recombinant human protein can result in expression-dependent chemical modifications (CMs) leading to variability of structure, stability and immunogenicity. Of particular interest are recomb
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::150d83fc740dc054b1eaff0891a8f6e1
http://europepmc.org/articles/PMC4192584
http://europepmc.org/articles/PMC4192584