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Showing 1-25 of 25 results for "56451" within Papers
Enhanced in-source fragmentation in MALDI-TOF-MS of oligonucleotides using 1,5-diaminonaphthalene
Hagan, N. A.; Smith, C. A.; Antoine, M. D.; Lin, J. S.; Feldman, A. B.; Demirev, P. A.
Journal of the American Chemical Society, 23, 773-777 (2012)
Robert Jirásko et al.
Analytical and bioanalytical chemistry, 406(19), 4601-4610 (2014-05-21)
The combination of ultrahigh-resolution mass spectrometry imaging (UHRMSI) and ultrahigh-performance liquid chromatography coupled with tandem mass spectrometry (UHPLC/MS/MS) was used for the identification and the spatial localization of atorvastatin (AT) and its metabolites in rat tissues. Ultrahigh-resolution and high mass
Shelley N Jackson et al.
Journal of the American Society for Mass Spectrometry, 29(7), 1463-1472 (2018-03-20)
Matrix-assisted laser/desorption ionization (MALDI) mass spectrometry imaging (MSI) is widely used as a unique tool to record the distribution of a large range of biomolecules in tissues. 2,6-Dihydroxyacetophenone (DHA) matrix has been shown to provide efficient ionization of lipids, especially
Daiki Asakawa et al.
The journal of physical chemistry. B, 117(8), 2321-2327 (2013-01-31)
The early mechanisms of matrix-assisted laser desorption/ionization in-source decay (MALDI-ISD) are described herein. MALDI-ISD is initiated by the hydrogen transfer from excited matrix molecules to the carbonyl oxygen of the peptide backbone, which is followed by a radical-induced cleavage, producing
Mandana Hunter et al.
Journal of neurochemistry, 146(5), 613-630 (2018-05-29)
The human subventricular zone (SVZ) has a defined cytological and neurochemical architecture, with four constituent laminae that act in concert to support its neurogenic activity. Lipidomic specialisation has previously been demonstrated in the neurologically normal human SVZ, with enrichment of
Laura Molin et al.
Rapid communications in mass spectrometry : RCM, 25(20), 3091-3096 (2011-09-29)
1,5-Diaminonaphthalene (DAN) has been described as an interesting and effective matrix for matrix-assisted laser desorption/ionization (MALDI) experiments in positive ion mode, being able to activate in-source decomposition phenomena and, when employed for the analysis of proteins containing disulphide bridge(s), being
Daiki Asakawa et al.
Journal of mass spectrometry : JMS, 47(2), 180-187 (2012-02-24)
Matrix-assisted laser desorption/ionization in-source decay (MALDI-ISD) has been used for characterization of a phosphorylated peptides and proteins because labile phosphate group is not lost during the MALDI-ISD process. The conventional MALDI-ISD is initiated by the hydrogen transfer from reducing matrix
Delphine Debois et al.
Analytical chemistry, 82(10), 4036-4045 (2010-04-20)
Matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS) imaging is a powerful technique giving access to the distribution of a large range of biomolecules directly from a tissue section, allowing, for example, the discovery of new pathological biomarkers. Nevertheless, one main difficulty
Issey Osaka et al.
Rapid communications in mass spectrometry : RCM, 27(1), 103-108 (2012-12-15)
Although matrix-assisted laser desorption/ionization in-source decay (MALDI-ISD) is an important method for post-translational modification (PTM) analysis, the conventional matrices, 2,5-dihydroxybenzoic acid (2,5-DHB) and 1,5-diaminonaphthalene (1,5-DAN), are poor in terms of the fragment ion yields of the phosphorylated peptides. The use
Takuma Degawa et al.
European journal of mass spectrometry (Chichester, England), 18(4), 345-348 (2012-09-14)
A peptide containing a single disulfide bond was sequenced using high-energy collision-induced dissociation (HE-CID) in conjunction with a high mass resolution time-of-flight tandem mass spectrometer equipped with a matrix-assisted laser desorption/ionization source. This mass spectrometer, which has spiral ion trajectory
Daiki Asakawa et al.
Journal of the American Society for Mass Spectrometry, 24(2), 297-300 (2013-01-12)
MALDI in-source decay (ISD) has been used for top-down sequencing of proteins. The use of the matrix 1,5-diaminonapthalene (1,5-DAN) gave abundant w ions, which are formed from the unimolecular dissociation of z• radical fragments via α cleavage reaction and thus
Junhai Yang et al.
Analytical chemistry, 85(5), 2907-2912 (2013-02-20)
We have developed targets precoated with matrix for imaging lipids in tissues using matrix-assisted laser desorption ionization mass spectrometry (MALDI MS). Thin tissue sections (rat kidney and mouse or rat brains) were placed onto 1,5-diaminonaphthalene precoated targets (prepared beforehand by
Aurélien Thomas et al.
Analytical chemistry, 84(4), 2048-2054 (2012-01-17)
Matrix sublimation has demonstrated to be a powerful approach for high-resolution matrix-assisted laser desorption ionization (MALDI) imaging of lipids, providing very homogeneous solvent-free deposition. This work presents a comprehensive study aiming to evaluate current and novel matrix candidates for high
Yuko Fukuyama et al.
Journal of mass spectrometry : JMS, 41(2), 191-201 (2005-12-31)
MS/MS is indispensable for the amino acid sequencing of peptides. However, its use is limited for peptides containing disulfide bonds. We have applied the reducing properties of 1,5-diaminonaphthalene (1,5-DAN) as a MALDI matrix to amino acid sequencing and disulfide bond
Pascale Lemaire et al.
Rapid communications in mass spectrometry : RCM, 27(16), 1837-1846 (2013-07-17)
In-Source Decay (ISD) in Matrix-Assisted Laser Desorption/Ionization (MALDI) mass spectrometry is a fast and easy top-down activation method. Our objective is to find a suitable matrix to locate the deuterons following in-solution hydrogen/deuterium exchange (HDX). This matrix must circumvent the
Daiki Asakawa et al.
Analytical chemistry, 86(5), 2451-2457 (2014-02-12)
Matrix-assisted laser desorption ionization in-source decay (MALDI-ISD) is a useful method for top-down sequencing of proteins and preferentially produces the c'/z(•) fragment pair. Subsequently, radical z(•) fragments undergo a variety of radical reactions. This work is focused on the chemical
New Method for Characterizing Highly Disulfide-Bridged Peptides in Complex Mixtures: Application to Toxin Identification from Crude Venoms
Quinton, Loiec; Demeure, Kevin; Dobson, Rowan; Gilles, Nicolas; Gabelica, Valerie; De Pauw, Edwin
Journal of Proteome Research, 6, 2316-3223 (2007)
Kevin Demeure et al.
Analytical chemistry, 79(22), 8678-8685 (2007-10-18)
In-source decay (ISD) in MALDI leads to c- and z-fragment ion series enhanced by hydrogen radical donors and is a useful method for sequencing purified peptides and proteins. Until now, most efforts to improve methods using ISD concerned instrumental optimization.
Tyler A Zimmerman et al.
Analytical chemistry, 83(15), 6090-6097 (2011-06-23)
In-source decay (ISD) fragmentation as combined with matrix-assisted laser desorption/ionization (MALDI) mass spectrometry allows protein sequencing directly from mass spectra. Acquisition of MALDI-ISD mass spectra from tissue samples is achieved using an appropriate MALDI matrix, such as 1,5-diaminonaphthalene (DAN). Recent
Kevin Demeure et al.
Journal of the American Society for Mass Spectrometry, 21(11), 1906-1917 (2010-09-14)
In-source decay (ISD) is a rapid fragmentation occurring in the matrix-assisted laser desorption/ionization (MALDI) source before the ion extraction. Despite the increasing interest for peptides de novo sequencing by ISD, the influence of the matrix and of the peptide itself
Motoshi Sakakura et al.
Journal of the American Society for Mass Spectrometry, 21(6), 979-988 (2010-03-30)
The use of 5-aminosalicylic acid (5-ASA) as a new matrix for in-source decay (ISD) of peptides including mono- and di-phosphorylated peptides in matrix-assisted laser desorption/ionization (MALDI) mass spectrometry (MS) is described. The use of 5-ASA in MALDI-ISD has been evaluated
Glycosylation characterization of therapeutic mAbs by top-and middle-down mass spectrometry
Tran QB, et al.
Data in Brief, 6, 68-76 (2016)
1,5-Naphthalenediamine.
IARC monographs on the evaluation of the carcinogenic risk of chemicals to humans, 27, 127-132 (1982-04-01)
David Calligaris et al.
Analytical chemistry, 85(4), 2117-2126 (2013-01-18)
Matrix-assisted laser desorption/ionization mass spectrometry imaging (MALDI MSI) is a rapidly growing method in biomedical research allowing molecular mapping of proteins on histological sections. The images can be analyzed in terms of spectral pattern to define regions of interest. However
Patty's Toxicology (2012)
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