| 1. |
- Bergquist, Jonas, et al.
(författare)
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Peptide Mapping of Proteins in Human Body Fluids using Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry
- 2002
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Ingår i: Mass spectrometry reviews (Print). - : Wiley. - 0277-7037 .- 1098-2787. ; 21:1, s. 2-15
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Tidskriftsartikel (refereegranskat)abstract
- Human body fluids have been rediscovered in the postgenomic era as great sources of biological markers and perhaps particularly as sources of potential protein biomarkers of disease. Analytical tools that allow rapid screening, low sample consumption, and accurate protein identification are of great importance in studies of complex biological samples and clinical diagnosis. Mass spectrometry is today one of the most important analytical tools with applications in a wide variety of fields. One of the fastest growing applications is in proteomics, or the study of protein expression in an organism. Mass spectrometry has been used to find post-translational modifications and to identify key functions of proteins in the human body. In this study, we review the use of human body fluids as sources for clinical markers and present new data that show the ability of Fourier transform ion cyclotron resonance (FTICR) mass spectrometry (MS) to identify, and characterize proteins in four human body fluids: plasma, cerebrospinal fluid (CSF), saliva, and urine. The body fluids were tryptically digested without any prior separation, purification, or selection, and the digest was introduced into a 9.4 T FTICR mass spectrometer by direct-infusion electrospray ionization (ESI). Even though these samples represent complex biological mixtures, the described method provides information that is comparable with traditional 2D-PAGE data. The sample consumption is extremely low, a few microliters, and the analysis time is only a few minutes. It is, however evident that the separation of proteins and/or peptides must be included in the methodology in order to detect low-abundance proteins and other proteins of biological relevance.
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| 2. |
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| 3. |
- Hansen, Klavs, 1958
(författare)
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DECAY DYNAMICS IN MOLECULAR BEAMS
- 2021
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Ingår i: Mass Spectrometry Reviews. - : Wiley. - 0277-7037 .- 1098-2787. ; 40:6, s. 725-740
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Tidskriftsartikel (refereegranskat)abstract
- The phenomenon of power law decays in molecular beams is reviewed. The transition from a canonical to a microcanonical description of the decay is analyzed, and the appearance of the power law decay derived. Deviations from a power law often contain information on parallel competing processes. This is illustrated with examples where thermal radiation or dark unimolecular channels are the competing processes. Also corrections to the power law due to finite heat capacities and from nonideal energy distributions are derived. Finally, the consequences for the interpretation of action spectroscopy data are reviewed. (c) 2020 The Authors. Mass Spectrometry Reviews published by Wiley Periodicals, Inc. Mass Spec Rev
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| 4. |
- Hellborg, Ragnar, et al.
(författare)
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Accelerator Mass Spectrometry
- 2008
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Ingår i: Mass Spectrometry Reviews. - : Wiley. - 0277-7037 .- 1098-2787. ; 27:5, s. 398-427
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Forskningsöversikt (refereegranskat)abstract
- In this overview the technique of accelerator mass spectrometry (AMS) and its use are described. AMS is a highly sensitive method of counting atoms. It is used to detect very low concentrations of natural isotopic abundances (typically in the range between 10(-12) and 10(-16)) of both radionuclides and stable nuclides. The main advantages of AMS compared to conventional radiometric methods are the use of smaller samples (mg and even sub-mg size) and shorter measuring times (less than 1 hr). The equipment used for AMS is almost exclusively based on the electrostatic tandem accelerator, although some of the newest systems are based on a slightly different principle. Dedicated accelerators as well as older "nuclear physics machines" can be found in the 80 or so AMS laboratories in existence today. The most widely used isotope studied with AMS is (14)C. Besides radiocarbon dating this isotope is used in climate studies, biomedicine applications and many other fields. More than 100,000 (14)C samples are measured per year. Other isotopes studied include (10)Be, (26)Al, (36)Cl, (41)Ca, (59)Ni, (129)I, U, and Pu. Although these measurements are important, the number of samples of these other isotopes measured each year is estimated to be less than 10% of the number of (14)C samples. (c) 2008 Wiley Periodicals, Inc., Mass Spec Rev.
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| 5. |
- Kushnir, Mark M., et al.
(författare)
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Liquid chromatography-tandem mass spectrometry applications in endocrinology
- 2010
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Ingår i: Mass spectrometry reviews (Print). - : Wiley. - 0277-7037 .- 1098-2787. ; 29:3, s. 480-502
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Forskningsöversikt (refereegranskat)abstract
- Liquid chromatography-tandem mass spectrometry (LC-MS/MS) has been recognized as a primary methodology for the accurate analysis of endogenous steroid hormones in biological samples. This review focuses on the use of LC-MS/MS in clinical laboratories to assist with the diagnosis of diverse groups of endocrine and metabolic diseases. Described analytical methods use on-line and off-line sample preparation and analytical derivatization to enhance analytical sensitivity, specificity, and clinical utility. Advantages of LC-MS/MS as an analytical technique include high specificity, possibility to simultaneously measure multiple analytes, and the ability to assess the specificity of the analysis in every sample. All described analytical methods were extensively validated, utilized in routine diagnostic practice, and were applied in a number of clinical and epidemiological studies, including a study of the steroidogenesis in ovarian follicles.
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| 6. |
- Moruz, Luminita, et al.
(författare)
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Peptide retention time prediction
- 2016
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Ingår i: Mass spectrometry reviews (Print). - : Wiley. - 0277-7037 .- 1098-2787.
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Tidskriftsartikel (refereegranskat)abstract
- Most methods for interpreting data from shotgun proteomics experiments are to large degree dependent on being able to predict properties of peptide-ions. Often such predicted properties are limited to molecular mass and fragment spectra, but here we put focus on a perhaps underutilized property, a peptide's chromatographic retention time. We review a couple of different principles of retention time prediction,and their applications within computational proteomics.
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| 7. |
- Thomas, Richard D.
(författare)
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When electrons meet molecular ions and what happens next : Dissociative recombination from interstellar molecular clouds to internal combustion engines
- 2008
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Ingår i: Mass spectrometry reviews (Print). - : Wiley. - 0277-7037 .- 1098-2787. ; 27:5, s. 485-530
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Forskningsöversikt (refereegranskat)abstract
- The interaction of matter with its environment is the driving force behind the evolution of 99% of the observed matter in the universe. The majority of the visible universe exists in a state of weak ionization, the so called fourth state of matter: plasma. Plasmas are ubiquitous, from those occurring naturally interstellar molecular clouds, cometary comae, circumstellar;shells, to those which are anthropic in origin: flames, combustion engines and fusion reactors. The evolution of these plasmas is driven by the interaction of the plasma constituents, the ions, and the electrons. One of the most important subsets of these reactions is electron-molecular ion recombination. This process is significant for two very important reasons. It is an ionization reducing reaction. removing two ionised species and Producing neutral products. Furthermore, these products may themselves be reactive radical species which can then further drive the evolution of the plasma. The rate at which the electron reacts with the ion depends on many parameters, for examples the collision energy. the internal energy of the ion, and the structure of the ion itself. Measuring these properties together with the manner in which the system breaks up, is therefore critical if the evolution of the environment is to be understood at all. Several techniques have been developed to study just such reactions to obtain the necessary information on the parameters. In this paper the focus will be on one the most recently developed of these, the Ion Storage Ring. together with the detection tools and techniques used to extract the necessary information from the reaction.
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| 8. |
- Fletcher, John, 1978, et al.
(författare)
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DEVELOPMENTS IN MOLECULAR SIMS DEPTH PROFILING AND 3D IMAGING OF BIOLOGICAL SYSTEMS USING POLYATOMIC PRIMARY IONS
- 2011
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Ingår i: Mass Spectrometry Reviews. - : Wiley. - 0277-7037. ; 30:1, s. 142-174
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Forskningsöversikt (refereegranskat)abstract
- In principle mass spectral imaging has enormous potential for discovery applications in biology. The chemical specificity of mass spectrometry combined with spatial analysis capabilities of liquid metal cluster beams and the high yields of polyatomic ion beams should present unprecedented ability to spatially locate molecular chemistry in the 100 nm range. However, although metal cluster ion beams have greatly increased yields in the m/z range up to 1000, they still have to be operated under the static limit and even in most favorable cases maximum yields for molecular species from 1 mm pixels are frequently below 20 counts. However, some very impressive molecular imaging analysis has been accomplished under these conditions. Nevertheless although molecular ions of lipids have been detected and correlation with biology is obtained, signal levels are such that lateral resolution must be sacrificed to provide a sufficient signal to image. To obtain useful spatial resolution detection below 1 mm is almost impossible. Too few ions are generated! The review shows that the application of polyatomic primary ions with their low damage cross-sections offers hope of a new approach to molecular SIMS imaging by accessing voxels rather than pixels to thereby increase the dynamic signal range in 2D imaging and to extend the analysis to depth profiling and 3D imaging. Recent data on cells and tissue analysis suggest that there is, in consequence, the prospect that a wider chemistry might be accessible within a sub-micron area and as a function of depth. However, these advances are compromised by the pulsed nature of current ToF-SIMS instruments. The duty cycle is very low and results in excessive analysis times, and maximum mass resolution is incompatible with maximum spatial resolution. New instrumental directions are described that enable a dc primary beam to be used that promises to be able to take full advantage of all the capabilities of the polyatomic ion beam. Some new data are presented that suggest that the aspirations for these new instruments will be realized. However, although prospects are good, the review highlights the continuing challenges presented by the low ionization efficiency and the complications that arise from matrix effects. (C) 2010 Wiley Periodicals, Inc., Mass Spec Rev 30:142-174, 2011
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