@article {2307,
	title = {Cyanobacterial copper-binding ligands isolated from artificial seawater cultures},
	journal = {Marine Chemistry},
	volume = {110},
	number = {1-2},
	year = {2008},
	note = {ISI Document Delivery No.: 313BETimes Cited: 4Cited Reference Count: 34Wiramanaden, Cheryl I. E. Cullen, Jay T. Ross, Andrew R. S. Orians, Kristin J.},
	month = {May},
	pages = {28-41},
	type = {Article},
	abstract = {This paper demonstrates a method to isolate and characterise strong biogenic copper-binding ligands from an artificial seawater matrix. Pseudo-polarography is used to detect the ligands, determine their ionic strength-corrected binding constants, and track them through each step of the extraction process. Two ligand types are found, one strong and one relatively weak, with log K{\textquoteright} values of 49.4 +/- 1.1 and 19.8 +/- 5.5 respectively, assuming that the metal is bound as copper(II). If a copper(I) complex, the log K{\textquoteright} of the strong copper-binding ligand would be 25. Pseudo-polarography is then used to assess different resins for ligand extraction and to determine the eluent fraction in which the strong ligand is recovered. XAD-16 is found to be a suitable resin for extracting the strong binding ligand from salt water into methanol, suggesting that the ligand is weakly hydrophobic. As ligands are identified by their complexation of copper, no assumptions are made regarding the functional groups of these natural ligands. The copper-binding ligands are successfully extracted into solvents suitable for mass spectrometric analysis using soft ionisation methods such as electrospray and MALDI. (C) 2008 Elsevier B.V. All rights reserved.},
	keywords = {AFFINITY-CHROMATOGRAPHY, chemical speciation, COMPETITION TECHNIQUE, COMPLEXING LIGANDS, copper, CU STRESS, EMILIANIA-HUXLEYI, IONIZATION MASS-SPECTROMETRY, LIGANDS, mass, NORTH PACIFIC, ORGANIC-COMPLEXES, polarography, SARGASSO SEA, sea water, SPECTROMETRY, TRACE-METALS},
	isbn = {0304-4203},
	url = {<Go to ISI>://000256715300004},
	author = {Wiramanaden, C. I. E. and Cullen, J. T. and Ross, A. R. S. and Orians, K. J.}
}
@article {2290,
	title = {Mass spectrometric identification of formaldehyde-induced peptide modifications under in vivo protein cross-linking conditions},
	journal = {Analytica Chimica Acta},
	volume = {618},
	number = {2},
	year = {2008},
	note = {ISI Document Delivery No.: 317FDTimes Cited: 10Cited Reference Count: 19Toews, Judy Rogalski, Jason C. Clark, Thomas J. Kast, Juergen},
	month = {Jun},
	pages = {168-183},
	type = {Article},
	abstract = {Formaldehyde cross-linking of proteins is emerging as a novel approach to study protein-protein interactions in living cells. It has been shown to be compatible with standard techniques used in functional proteomics such as affinity-based protein enrichment, enzymatic digestion, and mass spectrometric protein identification. So far, the lack of knowledge on formaldehyde-induced protein modifications and suitable mass spectrometric methods for their targeted detection has impeded the identification of the different types of crosslinked peptides in these samples. In particular, it has remained unclear whether in vitro studies that identified a multitude of amino acid residues reacting with formaldehyde over the course of several days are suitable substitutes for the much shorter reaction times of 10-20 min used in cross-linking experiments in living cells. The current study on model peptides identifies amino-termini as well as lysine, tryptophan, and cysteine side chains, i.e. a small subset of those modified after several days, as the major reactive sites under such conditions, and suggests relative position in the peptide sequence as well as sequence microenvironment to be important factors that govern reactivity. Using MALDI-MS, mass increases of 12 Da on amino groups and 30 Da on cysteines were detected as the major reaction products, while peptide fragment ion analysis by tandem mass spectrometry was used to localize the actual modification sites on a peptide. Non-specific cross-linking was absent, and could only be detected with low yield at elevated peptide concentrations. The detailed knowledge on the constraints and products of the formaldehyde reaction with peptides after short incubation times presented in this study is expected to facilitate the targeted mass spectrometric analysis of proteins after in vivo formaldehyde cross-linking. (c) 2008 Elsevier B.V. All rights reserved.},
	keywords = {Chemical modification, COMPLEXES, FORMALDEHYDE, MAP, mass, NETWORK, peptide fragmentation, protein cross-linking, PROTEOMICS, PURIFICATION, REACTIVITY, SPECTROMETRY},
	isbn = {0003-2670},
	url = {<Go to ISI>://000257004400006},
	author = {Toews, J. and Rogalski, J. C. and Clark, T. J. and Kast, J.}
}
@article {1480,
	title = {Electrospray ionization source geometry for mass spectrometry: past, present, and future},
	journal = {Trac-Trends in Analytical Chemistry},
	volume = {25},
	number = {3},
	year = {2006},
	note = {ISI Document Delivery No.: 026CJTimes Cited: 34Cited Reference Count: 130},
	month = {Mar},
	pages = {243-256},
	type = {Review},
	abstract = {The geometry of an electrospray ion source plays important roles in the processes of analyte desolvation, ionization, transportation, and detection in a mass spectrometer. We provide a brief account of the scientific principles involved in developing an electrospray ion source, and in the various geometries used to improve the sensitivity of mass spectrometry. We also present some popular configurations currently available and outline future trends in this research area. (C) 2005 Elsevier Ltd. All rights reserved.},
	keywords = {ANALYSIS SYSTEMS, atmospheric pressure ionization, ATMOSPHERIC-PRESSURE, CAPILLARY-ZONE-ELECTROPHORESIS, CHARGED DROPLETS, commercial ion source design, electrospray ionization, ion source, ion source geometry, mass, MICRO-ELECTROSPRAY, MICROFLUIDIC DEVICES, NANOSCALE LIQUID-CHROMATOGRAPHY, PRESSURE ION LENS, PROTEIN IDENTIFICATION, SOLUTION FLOW-RATES, SPECTROMETRY},
	isbn = {0165-9936},
	url = {<Go to ISI>://000236314000013},
	author = {Manisali, I. and Chen, D. D. Y. and Schneider, B. B.}
}
@article {1097,
	title = {Linear ion traps in mass spectrometry},
	journal = {Mass Spectrometry Reviews},
	volume = {24},
	number = {1},
	year = {2005},
	note = {ISI Document Delivery No.: 888OJTimes Cited: 73Cited Reference Count: 145},
	month = {Jan-Feb},
	pages = {1-29},
	type = {Review},
	abstract = {Linear ion traps are finding new applications in many areas of mass spectrometry. In a linear ion trap, ions are confined radially by a two-dimensional (2D) radio frequency (RF) field, and axially by stopping potentials applied to end electrodes. This review focuses on linear ion trap instrumentation. Potentials and ion motion in linear multipole fields and methods of ion trapping, cooling, excitation, and isolation are described. This is followed by a description of various mass discrimination effects that have been reported with linear ion traps. Linear ion traps combined in various ways with three-dimensional (3D) traps, time-of-flight (TOF) mass analyzers, and Fourier transform ion cyclotron resonance mass spectrometers are then given. Linear ion traps can be used as stand alone mass analyzers, and their use for mass analysis by Fourier transforming image currents, by mass selective radial ejection, and by mass selective axial ejection are reviewed. (C) 2004 Wiley Periodicals, Inc.},
	keywords = {analysis, CYCLOTRON-RESONANCE, ELECTROSPRAY-IONIZATION, EXCITATION, EXTERNAL ACCUMULATION, FRINGING FIELDS, INVERSE FOURIER-TRANSFORM, ion traps, linear multipoles, mass, MOLECULE REACTION, OCTOPOLE FIELDS, OF-FLIGHT, QUADRUPOLE, RADIOFREQUENCY, RESONANCE, space charge, STORAGE ASSISTED DISSOCIATION, SYSTEM},
	isbn = {0277-7037},
	url = {<Go to ISI>://000226383800001},
	author = {Douglas, D. J. and Frank, A. J. and Mao, D. M.}
}
@article {3810,
	title = {Nonthermal escape of the atmospheres of Venus, Earth, and Mars},
	journal = {Reviews of Geophysics},
	volume = {34},
	number = {4},
	year = {1996},
	note = {ISI Document Delivery No.: VU919Times Cited: 37Cited Reference Count: 188},
	month = {Nov},
	pages = {483-505},
	type = {Review},
	abstract = {Atmospheric loss from planetary atmospheres is an important geophysical problem with implications for planetary evolution. This is a multidisciplinary research field that requires an expertise in a wide range of subjects including statistical mechanics, fluid mechanics, plasma physics, collision theory, and surface science. This paper is a review of the current state of our understanding of atmospheric loss from the terrestrial planets. A detailed discussion is provided of the basic concepts required to understand the processes occurring in the high-altitude portion of a planetary atmosphere referred to as the exosphere. Light atomic species with sufficient translational energy can escape from an atmosphere. The translational energy required for escape could be thermal energy and proportional to the ambient temperature or the result of some collisional processes energizing the species above thermal energies. These collisional processes, which include charge exchange and dissociative recombination between energetic ions, neutrals, and electrons, are referred to as nonthermal escape processes. We highlight the similarities and differences in the important escape mechanisms on the terrestrial planets and comment on application of these mechanisms to evolutionary theories of the terrestrial atmospheres. The emphasis in this paper is directed toward the need to consider the exosphere as collisional.},
	keywords = {CHARGE-EXCHANGE, dissociative recombination, FRACTIONATION, HOT OXYGEN GEOCORONA, MAGNETIC-FIELD, MAGNETOHYDRODYNAMIC MODEL, MARTIAN ATMOSPHERE, mass, MULTISPECIES, NITROGEN-ATOMS, SOLAR-WIND INTERACTION, ULTRAVIOLET SPECTROMETER EXPERIMENT},
	isbn = {8755-1209},
	url = {<Go to ISI>://A1996VU91900004},
	author = {Shizgal, B. D. and Arkos, G. G.}
}
