Glenn Foulds - Academia.edu (original) (raw)
Papers by Glenn Foulds
Proteomics, Mar 1, 2004
Multiplexed photoaptamer‐based arrays that allow for the simultaneous measurement of multiple pro... more Multiplexed photoaptamer‐based arrays that allow for the simultaneous measurement of multiple proteins of interest in serum samples are described. Since photoaptamers covalently bind to their target analytes before fluorescent signal detection, the arrays can be vigorously washed to remove background proteins, providing the potential for superior signal‐to‐noise ratios and lower limits of quantification in biological matrices. Data are presented here for a 17‐plex photoaptamer array exhibiting limits of detection below 10 fM for several analytes including interleukin‐16, vascular endothelial growth factor, and endostatin and able to measure proteins in 10% serum samples. The assays are simple, scalable, and reproducible. Affinity of the capture reagent is shown to be directly correlated to the limit of detection for the analyte on the array.
Humana Press eBooks, Nov 15, 2003
ABSTRACT Described in this chapter is a capillary electrophoresis (CE) method for the accurate de... more ABSTRACT Described in this chapter is a capillary electrophoresis (CE) method for the accurate determination of protein-DNA binding constants (1). The advantages of the method include the fast separation and quantitation of protein-DNA complex and free DNA, in uncoated capillaries without sieving matrices, coupled with LIF detection of fluorescently-labeled DNA at nM to πM concentrations.
Journal of the Chemical Society, 1997
Acta Chemica Scandinavica, 1995
Journal of the Chemical Society, 1995
ABSTRACT
Journal of the Chemical Society, 1997
Biologically active peptides and their receptors are involved in many of life's essential process... more Biologically active peptides and their receptors are involved in many of life's essential processes. They are of enormous medical interest as many diseases and illnesses can be treated by agents which block or imitate the function of specific peptides and their receptors. ' 11
Journal of the Chemical Society, Perkin Transactions 1, 1997
Journal of the Chemical Society, Perkin Transactions 1, 1997
Capillary Electrophoresis of Nucleic Acids
ABSTRACT Described in this chapter is a capillary electrophoresis (CE) method for the accurate de... more ABSTRACT Described in this chapter is a capillary electrophoresis (CE) method for the accurate determination of protein-DNA binding constants (1). The advantages of the method include the fast separation and quantitation of protein-DNA complex and free DNA, in uncoated capillaries without sieving matrices, coupled with LIF detection of fluorescently-labeled DNA at nM to πM concentrations.
Acta Chemica Scandinavica, 1995
PROTEOMICS, 2004
Multiplexed photoaptamer‐based arrays that allow for the simultaneous measurement of multiple pro... more Multiplexed photoaptamer‐based arrays that allow for the simultaneous measurement of multiple proteins of interest in serum samples are described. Since photoaptamers covalently bind to their target analytes before fluorescent signal detection, the arrays can be vigorously washed to remove background proteins, providing the potential for superior signal‐to‐noise ratios and lower limits of quantification in biological matrices. Data are presented here for a 17‐plex photoaptamer array exhibiting limits of detection below 10 fM for several analytes including interleukin‐16, vascular endothelial growth factor, and endostatin and able to measure proteins in 10% serum samples. The assays are simple, scalable, and reproducible. Affinity of the capture reagent is shown to be directly correlated to the limit of detection for the analyte on the array.
Journal of Chromatography A, 1999
A simple capillary electrophoresis mobility shift assay (CEMSA), with no gel and uncoated capilla... more A simple capillary electrophoresis mobility shift assay (CEMSA), with no gel and uncoated capillaries, for the accurate determination of protein-DNA affinities free in solution was applied to constructs of the MyoD/ E47 DNA-binding proteins. The determined affinities are compared to those obtained by EMSA. MyoD-E47 covalent heterodimer binds DNA more tightly (K 51.8 nM) than MyoD (K 514.2 nM) or E47 (K 511.5 nM) covalent homodimers. The effect of non-specific d d d DNA on binding affinities was more important than salt concentration in the MyoD/ E47 series. Application of this method to the MyoD/ E47 system demonstrates the generality of our CEMSA.
Nucleic Acids Research, 1998
Quantitative determination of dissociation constants for DNA-protein complexes will help clarify ... more Quantitative determination of dissociation constants for DNA-protein complexes will help clarify the molecular mechanisms of transcription, replication and DNA repair. A practical capillary electrophoresis mobility shift assay (CEMSA) for protein-DNA affinities free in solution is presented. The method is fast and simple, precise and general. The speed (<2 min separations) and simplicity derive from the use of an uncoated capillary with no gel matrix. The dissociation constant for GCNK58, a DNA-binding-region construct of the yeast transcription factor GCN4, binding to the AP1 DNA site was measured (K d = 35 ± 4 nM) to demonstrate the utility of the method.
Proteomics, Mar 1, 2004
Multiplexed photoaptamer‐based arrays that allow for the simultaneous measurement of multiple pro... more Multiplexed photoaptamer‐based arrays that allow for the simultaneous measurement of multiple proteins of interest in serum samples are described. Since photoaptamers covalently bind to their target analytes before fluorescent signal detection, the arrays can be vigorously washed to remove background proteins, providing the potential for superior signal‐to‐noise ratios and lower limits of quantification in biological matrices. Data are presented here for a 17‐plex photoaptamer array exhibiting limits of detection below 10 fM for several analytes including interleukin‐16, vascular endothelial growth factor, and endostatin and able to measure proteins in 10% serum samples. The assays are simple, scalable, and reproducible. Affinity of the capture reagent is shown to be directly correlated to the limit of detection for the analyte on the array.
Humana Press eBooks, Nov 15, 2003
ABSTRACT Described in this chapter is a capillary electrophoresis (CE) method for the accurate de... more ABSTRACT Described in this chapter is a capillary electrophoresis (CE) method for the accurate determination of protein-DNA binding constants (1). The advantages of the method include the fast separation and quantitation of protein-DNA complex and free DNA, in uncoated capillaries without sieving matrices, coupled with LIF detection of fluorescently-labeled DNA at nM to πM concentrations.
Journal of the Chemical Society, 1997
Acta Chemica Scandinavica, 1995
Journal of the Chemical Society, 1995
ABSTRACT
Journal of the Chemical Society, 1997
Biologically active peptides and their receptors are involved in many of life's essential process... more Biologically active peptides and their receptors are involved in many of life's essential processes. They are of enormous medical interest as many diseases and illnesses can be treated by agents which block or imitate the function of specific peptides and their receptors. ' 11
Journal of the Chemical Society, Perkin Transactions 1, 1997
Journal of the Chemical Society, Perkin Transactions 1, 1997
Capillary Electrophoresis of Nucleic Acids
ABSTRACT Described in this chapter is a capillary electrophoresis (CE) method for the accurate de... more ABSTRACT Described in this chapter is a capillary electrophoresis (CE) method for the accurate determination of protein-DNA binding constants (1). The advantages of the method include the fast separation and quantitation of protein-DNA complex and free DNA, in uncoated capillaries without sieving matrices, coupled with LIF detection of fluorescently-labeled DNA at nM to πM concentrations.
Acta Chemica Scandinavica, 1995
PROTEOMICS, 2004
Multiplexed photoaptamer‐based arrays that allow for the simultaneous measurement of multiple pro... more Multiplexed photoaptamer‐based arrays that allow for the simultaneous measurement of multiple proteins of interest in serum samples are described. Since photoaptamers covalently bind to their target analytes before fluorescent signal detection, the arrays can be vigorously washed to remove background proteins, providing the potential for superior signal‐to‐noise ratios and lower limits of quantification in biological matrices. Data are presented here for a 17‐plex photoaptamer array exhibiting limits of detection below 10 fM for several analytes including interleukin‐16, vascular endothelial growth factor, and endostatin and able to measure proteins in 10% serum samples. The assays are simple, scalable, and reproducible. Affinity of the capture reagent is shown to be directly correlated to the limit of detection for the analyte on the array.
Journal of Chromatography A, 1999
A simple capillary electrophoresis mobility shift assay (CEMSA), with no gel and uncoated capilla... more A simple capillary electrophoresis mobility shift assay (CEMSA), with no gel and uncoated capillaries, for the accurate determination of protein-DNA affinities free in solution was applied to constructs of the MyoD/ E47 DNA-binding proteins. The determined affinities are compared to those obtained by EMSA. MyoD-E47 covalent heterodimer binds DNA more tightly (K 51.8 nM) than MyoD (K 514.2 nM) or E47 (K 511.5 nM) covalent homodimers. The effect of non-specific d d d DNA on binding affinities was more important than salt concentration in the MyoD/ E47 series. Application of this method to the MyoD/ E47 system demonstrates the generality of our CEMSA.
Nucleic Acids Research, 1998
Quantitative determination of dissociation constants for DNA-protein complexes will help clarify ... more Quantitative determination of dissociation constants for DNA-protein complexes will help clarify the molecular mechanisms of transcription, replication and DNA repair. A practical capillary electrophoresis mobility shift assay (CEMSA) for protein-DNA affinities free in solution is presented. The method is fast and simple, precise and general. The speed (<2 min separations) and simplicity derive from the use of an uncoated capillary with no gel matrix. The dissociation constant for GCNK58, a DNA-binding-region construct of the yeast transcription factor GCN4, binding to the AP1 DNA site was measured (K d = 35 ± 4 nM) to demonstrate the utility of the method.