40 research outputs found
Low-Temperature Photochemically Activated Amorphous Indium-Gallium-Zinc Oxide for Highly Stable Room-Temperature Gas Sensors
We
report on highly stable amorphous indium-gallium-zinc oxide
(IGZO) gas sensors for ultraviolet (UV)-activated room-temperature
detection of volatile organic compounds (VOCs). The IGZO sensors fabricated
by a low-temperature photochemical activation process and exhibiting
two orders higher photocurrent compared to conventional zinc oxide
sensors, allowed high gas sensitivity against various VOCs even at
room temperature. From a systematic analysis, it was found that by
increasing the UV intensity, the gas sensitivity, response time, and
recovery behavior of an IGZO sensor were strongly enhanced. In particular,
under an UV intensity of 30 mW cm<sup>–2</sup>, the IGZO sensor
exhibited gas sensitivity, response time and recovery time of 37%,
37 and 53 s, respectively, against 750 ppm concentration of acetone
gas. Moreover, the IGZO gas sensor had an excellent long-term stability
showing around 6% variation in gas sensitivity over 70 days. These
results strongly support a conclusion that a low-temperature solution-processed
amorphous IGZO film can serve as a good candidate for room-temperature
VOCs sensors for emerging wearable electronics
Modified MuDPIT Separation Identified 4488 Proteins in a System-wide Analysis of Quiescence in Yeast
A modified multidimensional protein
identification technology (MudPIT)
separation was coupled to an LTQ Orbitrap Velos mass spectrometer
and used to rapidly identify the near-complete yeast proteome from
a whole cell tryptic digest. This modified online two-dimensional
liquid chromatography separation consists of 39 strong cation exchange
steps followed by a short 18.5 min reversed-phase (RP) gradient. A
total of 4269 protein identifications were made from 4189 distinguishable
protein families from yeast during log phase growth. The “Micro”
MudPIT separation performed as well as a standard MudPIT separation
in 40% less gradient time. The majority of the yeast proteome can
now be routinely covered in less than a days’ time with high
reproducibility and sensitivity. The newly devised separation method
was used to detect changes in protein expression during cellular quiescence
in yeast. An enrichment in the GO annotations “oxidation reduction”,
“catabolic processing” and “cellular response
to oxidative stress” was seen in the quiescent cellular fraction,
consistent with their long-lived stress resistant phenotypes. Heterogeneity
was observed in the stationary phase fraction with a less dense cell
population showing reductions in KEGG pathway categories of “Ribosome”
and “Proteasome”, further defining the complex nature
of yeast populations present during stationary phase growth. In total,
4488 distinguishable protein families were identified in all cellular
conditions tested
Modified MuDPIT Separation Identified 4488 Proteins in a System-wide Analysis of Quiescence in Yeast
A modified multidimensional protein
identification technology (MudPIT)
separation was coupled to an LTQ Orbitrap Velos mass spectrometer
and used to rapidly identify the near-complete yeast proteome from
a whole cell tryptic digest. This modified online two-dimensional
liquid chromatography separation consists of 39 strong cation exchange
steps followed by a short 18.5 min reversed-phase (RP) gradient. A
total of 4269 protein identifications were made from 4189 distinguishable
protein families from yeast during log phase growth. The “Micro”
MudPIT separation performed as well as a standard MudPIT separation
in 40% less gradient time. The majority of the yeast proteome can
now be routinely covered in less than a days’ time with high
reproducibility and sensitivity. The newly devised separation method
was used to detect changes in protein expression during cellular quiescence
in yeast. An enrichment in the GO annotations “oxidation reduction”,
“catabolic processing” and “cellular response
to oxidative stress” was seen in the quiescent cellular fraction,
consistent with their long-lived stress resistant phenotypes. Heterogeneity
was observed in the stationary phase fraction with a less dense cell
population showing reductions in KEGG pathway categories of “Ribosome”
and “Proteasome”, further defining the complex nature
of yeast populations present during stationary phase growth. In total,
4488 distinguishable protein families were identified in all cellular
conditions tested
Modified MuDPIT Separation Identified 4488 Proteins in a System-wide Analysis of Quiescence in Yeast
A modified multidimensional protein
identification technology (MudPIT)
separation was coupled to an LTQ Orbitrap Velos mass spectrometer
and used to rapidly identify the near-complete yeast proteome from
a whole cell tryptic digest. This modified online two-dimensional
liquid chromatography separation consists of 39 strong cation exchange
steps followed by a short 18.5 min reversed-phase (RP) gradient. A
total of 4269 protein identifications were made from 4189 distinguishable
protein families from yeast during log phase growth. The “Micro”
MudPIT separation performed as well as a standard MudPIT separation
in 40% less gradient time. The majority of the yeast proteome can
now be routinely covered in less than a days’ time with high
reproducibility and sensitivity. The newly devised separation method
was used to detect changes in protein expression during cellular quiescence
in yeast. An enrichment in the GO annotations “oxidation reduction”,
“catabolic processing” and “cellular response
to oxidative stress” was seen in the quiescent cellular fraction,
consistent with their long-lived stress resistant phenotypes. Heterogeneity
was observed in the stationary phase fraction with a less dense cell
population showing reductions in KEGG pathway categories of “Ribosome”
and “Proteasome”, further defining the complex nature
of yeast populations present during stationary phase growth. In total,
4488 distinguishable protein families were identified in all cellular
conditions tested
Modified MuDPIT Separation Identified 4488 Proteins in a System-wide Analysis of Quiescence in Yeast
A modified multidimensional protein
identification technology (MudPIT)
separation was coupled to an LTQ Orbitrap Velos mass spectrometer
and used to rapidly identify the near-complete yeast proteome from
a whole cell tryptic digest. This modified online two-dimensional
liquid chromatography separation consists of 39 strong cation exchange
steps followed by a short 18.5 min reversed-phase (RP) gradient. A
total of 4269 protein identifications were made from 4189 distinguishable
protein families from yeast during log phase growth. The “Micro”
MudPIT separation performed as well as a standard MudPIT separation
in 40% less gradient time. The majority of the yeast proteome can
now be routinely covered in less than a days’ time with high
reproducibility and sensitivity. The newly devised separation method
was used to detect changes in protein expression during cellular quiescence
in yeast. An enrichment in the GO annotations “oxidation reduction”,
“catabolic processing” and “cellular response
to oxidative stress” was seen in the quiescent cellular fraction,
consistent with their long-lived stress resistant phenotypes. Heterogeneity
was observed in the stationary phase fraction with a less dense cell
population showing reductions in KEGG pathway categories of “Ribosome”
and “Proteasome”, further defining the complex nature
of yeast populations present during stationary phase growth. In total,
4488 distinguishable protein families were identified in all cellular
conditions tested
Dynamics of Subcellular Proteomes During Brain Development
Many neurological disorders are caused by perturbations
during
brain development, but these perturbations cannot be readily identified
until there is comprehensive description of the development process.
In this study, we performed mass spectrometry analysis of the synaptosomal
and mitochondrial fractions from three rat brain regions at four postnatal
time points. To quantitate our analysis, we employed <sup>15</sup>N labeled rat brains using a technique called SILAM (stable isotope
labeling in mammals). We quantified 167429 peptides and identified
over 5000 statistically significant changes during development including
known disease-associated proteins. Global analysis revealed distinct
trends between the synaptic and nonsynaptic mitochondrial proteomes
and common protein networks between regions each consisting of a unique
array of expression patterns. Finally, we identified novel regulators
of neurodevelopment that possess the identical temporal pattern of
known regulators of neurodevelopment. Overall, this study is the most
comprehensive quantitative analysis of the developing brain proteome
to date, providing an important resource for neurobiologists
Dynamics of Subcellular Proteomes During Brain Development
Many neurological disorders are caused by perturbations
during
brain development, but these perturbations cannot be readily identified
until there is comprehensive description of the development process.
In this study, we performed mass spectrometry analysis of the synaptosomal
and mitochondrial fractions from three rat brain regions at four postnatal
time points. To quantitate our analysis, we employed <sup>15</sup>N labeled rat brains using a technique called SILAM (stable isotope
labeling in mammals). We quantified 167429 peptides and identified
over 5000 statistically significant changes during development including
known disease-associated proteins. Global analysis revealed distinct
trends between the synaptic and nonsynaptic mitochondrial proteomes
and common protein networks between regions each consisting of a unique
array of expression patterns. Finally, we identified novel regulators
of neurodevelopment that possess the identical temporal pattern of
known regulators of neurodevelopment. Overall, this study is the most
comprehensive quantitative analysis of the developing brain proteome
to date, providing an important resource for neurobiologists
Dynamics of Subcellular Proteomes During Brain Development
Many neurological disorders are caused by perturbations
during
brain development, but these perturbations cannot be readily identified
until there is comprehensive description of the development process.
In this study, we performed mass spectrometry analysis of the synaptosomal
and mitochondrial fractions from three rat brain regions at four postnatal
time points. To quantitate our analysis, we employed <sup>15</sup>N labeled rat brains using a technique called SILAM (stable isotope
labeling in mammals). We quantified 167429 peptides and identified
over 5000 statistically significant changes during development including
known disease-associated proteins. Global analysis revealed distinct
trends between the synaptic and nonsynaptic mitochondrial proteomes
and common protein networks between regions each consisting of a unique
array of expression patterns. Finally, we identified novel regulators
of neurodevelopment that possess the identical temporal pattern of
known regulators of neurodevelopment. Overall, this study is the most
comprehensive quantitative analysis of the developing brain proteome
to date, providing an important resource for neurobiologists
Dynamics of Subcellular Proteomes During Brain Development
Many neurological disorders are caused by perturbations
during
brain development, but these perturbations cannot be readily identified
until there is comprehensive description of the development process.
In this study, we performed mass spectrometry analysis of the synaptosomal
and mitochondrial fractions from three rat brain regions at four postnatal
time points. To quantitate our analysis, we employed <sup>15</sup>N labeled rat brains using a technique called SILAM (stable isotope
labeling in mammals). We quantified 167429 peptides and identified
over 5000 statistically significant changes during development including
known disease-associated proteins. Global analysis revealed distinct
trends between the synaptic and nonsynaptic mitochondrial proteomes
and common protein networks between regions each consisting of a unique
array of expression patterns. Finally, we identified novel regulators
of neurodevelopment that possess the identical temporal pattern of
known regulators of neurodevelopment. Overall, this study is the most
comprehensive quantitative analysis of the developing brain proteome
to date, providing an important resource for neurobiologists
Dynamics of Subcellular Proteomes During Brain Development
Many neurological disorders are caused by perturbations
during
brain development, but these perturbations cannot be readily identified
until there is comprehensive description of the development process.
In this study, we performed mass spectrometry analysis of the synaptosomal
and mitochondrial fractions from three rat brain regions at four postnatal
time points. To quantitate our analysis, we employed <sup>15</sup>N labeled rat brains using a technique called SILAM (stable isotope
labeling in mammals). We quantified 167429 peptides and identified
over 5000 statistically significant changes during development including
known disease-associated proteins. Global analysis revealed distinct
trends between the synaptic and nonsynaptic mitochondrial proteomes
and common protein networks between regions each consisting of a unique
array of expression patterns. Finally, we identified novel regulators
of neurodevelopment that possess the identical temporal pattern of
known regulators of neurodevelopment. Overall, this study is the most
comprehensive quantitative analysis of the developing brain proteome
to date, providing an important resource for neurobiologists