Zobrazeno 1 - 10
of 89
pro vyhledávání: '"Erik J. Fernandez"'
Autor:
Anne S. Robinson, Christopher J. O'Brien, Christopher J. Roberts, Joseph A. Costanzo, Kathryn E. Tiller, Erin C. Tamargo, Erik J. Fernandez
Publikováno v:
Protein Engineering, Design and Selection. 27:157-167
Non-native protein aggregation is a prevalent problem occurring in many biotechnological manufacturing processes and can compromise the biological activity of the target molecule or induce an undesired immune response. Additionally, some non-native a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bec52e1b938d7ae39f6677a82019ca66
https://doi.org/10.1093/protein/gzu008
https://doi.org/10.1093/protein/gzu008
Autor:
Shaojie Zhang, Simpson Gregoire, Erik J. Fernandez, Inchan Kwon, Kelly Wilson, Joseph A. Costanzo
Publikováno v:
Biotechnology and Bioengineering. 111:462-474
Protein misfolding and aggregation are implicated in numerous human diseases and significantly lower production yield of proteins expressed in mammalian cells. Despite the importance of understanding and suppressing protein aggregation in mammalian c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4f2ba1ea52b963ffc712fc34b5e1d643
https://doi.org/10.1002/bit.25119
https://doi.org/10.1002/bit.25119
Autor:
Richard L. Remmele, Erik J. Fernandez, Dingjiang Liu, Vladimir I. Razinkov, Nayoung Kim, Christopher J. Roberts
Publikováno v:
Biophysical Chemistry. 172:26-36
Changes in non-native aggregation mechanisms of an anti-streptavidin (anti-SA) IgG1 antibody were determined over a wide range of pH and [NaCl] under accelerated (high temperature) conditions, using a combination of calorimetry, chromatography, stati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e6be15fbcf4e1bc22eef1ed0ffce083
https://doi.org/10.1016/j.bpc.2012.12.004
https://doi.org/10.1016/j.bpc.2012.12.004
Autor:
Jacob L. Jordan, Christopher J. Roberts, Jennifer M. Andrews, Rebecca K. Brummitt, Erik J. Fernandez
Publikováno v:
Biophysical Chemistry. :10-18
Amyloid aggregates have been hypothesized as a global low free energy state for proteins at finite concentrations. Near its midpoint unfolding temperature, α-chymotrypsinogen A (aCgn) spontaneously forms amyloid polymers, indicating the free energy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b43b61a0e9d555074522bc999e36a5c1
https://doi.org/10.1016/j.bpc.2012.06.001
https://doi.org/10.1016/j.bpc.2012.06.001
Publikováno v:
ACS Chemical Neuroscience. 2:645-657
Growing evidence suggests that on-pathway amyloid-β (Aβ) oligomers are primary neurotoxic species and have a direct correlation with the onset of Alzheimer's disease (AD). One promising therapeutic strategy to block AD progression is to reduce the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4476808a50bb9fc15d9c97d3df4f9589
https://doi.org/10.1021/cn200056g
https://doi.org/10.1021/cn200056g
Publikováno v:
Langmuir. 27:286-295
Hydrogen exchange mass spectrometry (HXMS) coupled to proteolytic digestion has been used to probe the conformation of bovine β-lactoglobulin (BLG), bovine α-lactalbumin (BLA), and human serum albumin (HSA) in solution and while adsorbed to the hyd
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13145e354a1536993f6efb14804492c6
https://doi.org/10.1021/la103793r
https://doi.org/10.1021/la103793r
Autor:
Jacob L. Jordan, Erik J. Fernandez, Aming Zhang, William F. Weiss, Magdalena I. Ivanova, Christopher J. Roberts
Publikováno v:
Biochemistry. 49:10553-10564
Understanding nonnative protein aggregation is critical not only to a number of amyloidosis disorders but also for the development of effective and safe biopharmaceuticals. In a series of previous studies [Weiss et al. (2007) Biophys. J. 93, 4392-440
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff62e41359435897130b76a468c45b1e
https://doi.org/10.1021/bi1014216
https://doi.org/10.1021/bi1014216
Publikováno v:
Journal of Chromatography A. 1217:5571-5583
Hydrogen exchange has been a useful technique for studying the conformational state of proteins, both in bulk solution and at interfaces, for several decades. Here, we propose a physically based model of simultaneous protein adsorption, unfolding and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::425df86b3fba064806a0ba48464d859a
https://doi.org/10.1016/j.chroma.2010.06.051
https://doi.org/10.1016/j.chroma.2010.06.051
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1788:1714-1721
Beta-amyloid peptide (Abeta) is a primary protein component of senile plaques in Alzheimer's disease (AD) and plays an important, but not fully understood role in neurotoxicity. Model peptides with the demonstrated ability to mimic the structural and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::726dd352adb4f1e4c4f692e09e1dd229
https://doi.org/10.1016/j.bbamem.2009.04.010
https://doi.org/10.1016/j.bbamem.2009.04.010
Publikováno v:
Biotechnology and Bioengineering. 104:181-192
Beta-amyloid peptide (Abeta) is the major protein constituent found in senile plaques in Alzheimer's disease (AD). It is believed that Abeta plays a role in neurodegeneration associated with AD and that its toxicity is related to its structure or agg
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbf61ce046c27686049fe5c95427ddd3
https://doi.org/10.1002/bit.22367
https://doi.org/10.1002/bit.22367