Erik J Fernandez
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Explore the profile of Erik J Fernandez including associated specialties, affiliations and a list of published articles.
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41
Citations
392
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Recent Articles
1.
Gospodarek A, Sun W, OConnell J, Fernandez E
J Chromatogr A
. 2014 Dec;
1371:204-19.
PMID: 25456599
In hydrophobic interaction chromatography (HIC), interactions between buried hydrophobic residues and HIC surfaces can cause conformational changes that interfere with separations and cause yield losses. This paper extends our previous...
2.
Gospodarek A, Hiser D, OConnell J, Fernandez E
J Chromatogr A
. 2014 Jul;
1355:238-52.
PMID: 24997510
Recent studies with proteins indicate that conformational changes and aggregation can occur during ion exchange chromatography (IEC). Such behavior is not usually expected, but could lead to decreased yield and...
3.
Costanzo J, OBrien C, Tiller K, Tamargo E, Robinson A, Roberts C, et al.
Protein Eng Des Sel
. 2014 Apr;
27(5):157-67.
PMID: 24722670
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,...
4.
Weiss 4th W, Zhang A, Ivanova M, Sahin E, Jordan J, Fernandez E, et al.
Biophys Chem
. 2013 Dec;
185:79-87.
PMID: 24374388
Proper disulfide formation can be essential for the conformational stability of natively folded proteins. For proteins that must unfold in order to aggregate, disruption of native disulfides may therefore promote...
5.
Gregoire S, Zhang S, Costanzo J, Wilson K, Fernandez E, Kwon I
Biotechnol Bioeng
. 2013 Oct;
111(3):462-74.
PMID: 24114411
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...
6.
Kim N, Remmele Jr R, Liu D, Razinkov V, Fernandez E, Roberts C
Biophys Chem
. 2013 Jan;
172:26-36.
PMID: 23334430
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...
7.
Wong H, Qi W, Choi H, Fernandez E, Kwon I
ACS Chem Neurosci
. 2012 Aug;
2(11):645-57.
PMID: 22860159
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...
8.
Brummitt R, Andrews J, Jordan J, Fernandez E, Roberts C
Biophys Chem
. 2012 Jul;
168-169:10-8.
PMID: 22750559
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...
9.
Zhang A, Singh S, Shirts M, Kumar S, Fernandez E
Pharm Res
. 2011 Aug;
29(1):236-50.
PMID: 21805212
Purpose: Aggregation of monoclonal antibodies (mAbs) is a common yet poorly understood issue in therapeutic development. There remains a need for high-resolution structural information about conformational changes and intermolecular contacts...
10.
Zhang A, Qi W, Singh S, Fernandez E
Pharm Res
. 2011 Feb;
28(5):1179-93.
PMID: 21301933
Purpose: The impact of freeze-thaw (F/T) on structure integrity of protein therapeutics is poorly understood, partially due to lack of methods to detect protein structural perturbations during F/T processing in...