19 research outputs found
Polyglutamine expansion of ataxin-3 alters its degree of ubiquitination and phosphorylation at specific sites
Combination of Chemical Genetics and Phosphoproteomics for Kinase Signaling Analysis Enables Confident Identification of Cellular Downstream Targets
Invandrare med diabetes - att stötta och bemöta ur ett transkulturellt perspektiv
Immigration is today happening in Sweden to a great extent and this requires a higher level of demands within the transcultural nursing. With this fact as a base to our literature review the aim of the study was developed. This was to investigate how immigrants with diabetes mellitus type 2 experience health and to find out the importance of knowledge related to the patients compliance of given advise and prescriptions. On the basis of the aim the following questions of issue was formulated: How do immigrants with diabetes mellitus type 2 experience their health and what knowledge do they possess concerning their illness? and Within which areas of the immigrants life is it important for the nurse to gain knowledge in order to affect and oblige him or her? A critical review of nine scientific articles emerged in three themes that answer the questions of issue. These themes are: Experience of health and illness, Factors that influence the immigrants acting and Religion, culture and communication. The themes of the study support and relates to Leiningers sunrise model.Invandring sker i Sverige idag i allt större utstrÀckning och högre krav stÀlls pÄ den transkulturella omvÄrdnaden. Med detta som grund utformades studiens syfte som var att genom litteraturstudie undersöka hur invandrare med diabetes mellitus typ 2 upplever hÀlsa samt kunskapens betydelse för patientens följsamhet till givna rÄd och ordination. UtifrÄn syftet formulerades följande frÄgestÀllningar Hur upplever invandrare med diabetes mellitus typ 2 sin hÀlsa och vad har de för kunskap kring sin sjukdom? samt Kring vilka omrÄden i den invandrades liv behöver sjuksköterskan ha kunskap för att pÄ bÀsta sÀtt kunna pÄverka och tillmötesgÄ denna? Efter att kritiskt granskat 9 vetenskapliga artiklar mynnade resultaten ut i tre teman som svarar pÄ frÄgestÀllningarna. Dessa teman Àr HÀlso- och sjukdomsuppfattning, Faktorer som pÄverkar den invandrades agerande och Religion, kultur och kommunikation. Studiens teman stöttar och anknytes till Leiningers sunrise-modell
Mass spectrometry analyses of normal and polyglutamine expanded ataxin-3 reveal novel interaction partners involved in mitochondrial function
Comparison of SILAC and mTRAQ Quantification for Phosphoproteomics on a Quadrupole Orbitrap Mass Spectrometer
Advances in mass spectrometric methodology
and instrumentation
have promoted a continuous increase in analytical performance in the
field of phosphoproteomics. Here, we employed the recently introduced
quadrupole Orbitrap (Q Exactive) mass spectrometer for quantitative
signaling analysis to a depth of more than 15â000 phosphorylation
sites. In parallel to the commonly used SILAC approach, we evaluated
the nonisobaric chemical labeling reagent mTRAQ as an alternative
quantification technique. Both enabled high phosphoproteome coverage
in H3122 lung cancer cells. Replicate quantifications by mTRAQ identified
almost as many significant phosphorylation changes upon treatment
with ALK kinase inhibitor crizotinib as found by SILAC quantification.
Overall, mTRAQ was slightly less precise than SILAC as evident from
a somewhat higher variance of replicate phosphosite ratios. Direct
comparison of SILAC- and mTRAQ-quantified phosphosites revealed that
the majority of changes were detected by either quantification techniques,
but also highlighted the aspect of false negative identifications
in quantitative proteomics applications. Further inspection of crizotinib-regulated
phosphorylation changes unveiled interference with multiple antioncogenic
mechanisms downstream of ALK fusion kinase in H3122 cells. In conclusion,
our results demonstrate a strong analytical performance of the Q Exactive
in global phosphoproteomics, and establish mTRAQ quantification as
a useful alternative to metabolic isotope labeling
Comparison of SILAC and mTRAQ Quantification for Phosphoproteomics on a Quadrupole Orbitrap Mass Spectrometer
Advances in mass spectrometric methodology
and instrumentation
have promoted a continuous increase in analytical performance in the
field of phosphoproteomics. Here, we employed the recently introduced
quadrupole Orbitrap (Q Exactive) mass spectrometer for quantitative
signaling analysis to a depth of more than 15â000 phosphorylation
sites. In parallel to the commonly used SILAC approach, we evaluated
the nonisobaric chemical labeling reagent mTRAQ as an alternative
quantification technique. Both enabled high phosphoproteome coverage
in H3122 lung cancer cells. Replicate quantifications by mTRAQ identified
almost as many significant phosphorylation changes upon treatment
with ALK kinase inhibitor crizotinib as found by SILAC quantification.
Overall, mTRAQ was slightly less precise than SILAC as evident from
a somewhat higher variance of replicate phosphosite ratios. Direct
comparison of SILAC- and mTRAQ-quantified phosphosites revealed that
the majority of changes were detected by either quantification techniques,
but also highlighted the aspect of false negative identifications
in quantitative proteomics applications. Further inspection of crizotinib-regulated
phosphorylation changes unveiled interference with multiple antioncogenic
mechanisms downstream of ALK fusion kinase in H3122 cells. In conclusion,
our results demonstrate a strong analytical performance of the Q Exactive
in global phosphoproteomics, and establish mTRAQ quantification as
a useful alternative to metabolic isotope labeling
Comparison of SILAC and mTRAQ Quantification for Phosphoproteomics on a Quadrupole Orbitrap Mass Spectrometer
Advances in mass spectrometric methodology
and instrumentation
have promoted a continuous increase in analytical performance in the
field of phosphoproteomics. Here, we employed the recently introduced
quadrupole Orbitrap (Q Exactive) mass spectrometer for quantitative
signaling analysis to a depth of more than 15â000 phosphorylation
sites. In parallel to the commonly used SILAC approach, we evaluated
the nonisobaric chemical labeling reagent mTRAQ as an alternative
quantification technique. Both enabled high phosphoproteome coverage
in H3122 lung cancer cells. Replicate quantifications by mTRAQ identified
almost as many significant phosphorylation changes upon treatment
with ALK kinase inhibitor crizotinib as found by SILAC quantification.
Overall, mTRAQ was slightly less precise than SILAC as evident from
a somewhat higher variance of replicate phosphosite ratios. Direct
comparison of SILAC- and mTRAQ-quantified phosphosites revealed that
the majority of changes were detected by either quantification techniques,
but also highlighted the aspect of false negative identifications
in quantitative proteomics applications. Further inspection of crizotinib-regulated
phosphorylation changes unveiled interference with multiple antioncogenic
mechanisms downstream of ALK fusion kinase in H3122 cells. In conclusion,
our results demonstrate a strong analytical performance of the Q Exactive
in global phosphoproteomics, and establish mTRAQ quantification as
a useful alternative to metabolic isotope labeling
Comparison of SILAC and mTRAQ Quantification for Phosphoproteomics on a Quadrupole Orbitrap Mass Spectrometer
Advances in mass spectrometric methodology
and instrumentation
have promoted a continuous increase in analytical performance in the
field of phosphoproteomics. Here, we employed the recently introduced
quadrupole Orbitrap (Q Exactive) mass spectrometer for quantitative
signaling analysis to a depth of more than 15â000 phosphorylation
sites. In parallel to the commonly used SILAC approach, we evaluated
the nonisobaric chemical labeling reagent mTRAQ as an alternative
quantification technique. Both enabled high phosphoproteome coverage
in H3122 lung cancer cells. Replicate quantifications by mTRAQ identified
almost as many significant phosphorylation changes upon treatment
with ALK kinase inhibitor crizotinib as found by SILAC quantification.
Overall, mTRAQ was slightly less precise than SILAC as evident from
a somewhat higher variance of replicate phosphosite ratios. Direct
comparison of SILAC- and mTRAQ-quantified phosphosites revealed that
the majority of changes were detected by either quantification techniques,
but also highlighted the aspect of false negative identifications
in quantitative proteomics applications. Further inspection of crizotinib-regulated
phosphorylation changes unveiled interference with multiple antioncogenic
mechanisms downstream of ALK fusion kinase in H3122 cells. In conclusion,
our results demonstrate a strong analytical performance of the Q Exactive
in global phosphoproteomics, and establish mTRAQ quantification as
a useful alternative to metabolic isotope labeling
Comparison of SILAC and mTRAQ Quantification for Phosphoproteomics on a Quadrupole Orbitrap Mass Spectrometer
Advances in mass spectrometric methodology
and instrumentation
have promoted a continuous increase in analytical performance in the
field of phosphoproteomics. Here, we employed the recently introduced
quadrupole Orbitrap (Q Exactive) mass spectrometer for quantitative
signaling analysis to a depth of more than 15â000 phosphorylation
sites. In parallel to the commonly used SILAC approach, we evaluated
the nonisobaric chemical labeling reagent mTRAQ as an alternative
quantification technique. Both enabled high phosphoproteome coverage
in H3122 lung cancer cells. Replicate quantifications by mTRAQ identified
almost as many significant phosphorylation changes upon treatment
with ALK kinase inhibitor crizotinib as found by SILAC quantification.
Overall, mTRAQ was slightly less precise than SILAC as evident from
a somewhat higher variance of replicate phosphosite ratios. Direct
comparison of SILAC- and mTRAQ-quantified phosphosites revealed that
the majority of changes were detected by either quantification techniques,
but also highlighted the aspect of false negative identifications
in quantitative proteomics applications. Further inspection of crizotinib-regulated
phosphorylation changes unveiled interference with multiple antioncogenic
mechanisms downstream of ALK fusion kinase in H3122 cells. In conclusion,
our results demonstrate a strong analytical performance of the Q Exactive
in global phosphoproteomics, and establish mTRAQ quantification as
a useful alternative to metabolic isotope labeling