@article {31530,
	title = {Spin-coated epoxy resin embedding technique enables facile SEM/FIB thickness determination of porous metal oxide ultra-thin films},
	journal = {Journal of Microscopy},
	volume = {270},
	year = {2018},
	pages = {302-308},
	abstract = {<p>Summary A facile nonsubjective method was designed to measure porous nonconductive iron oxide film thickness using a combination of a focused ion beam (FIB) and scanning electron microscopy. Iron oxide films are inherently nonconductive and porous, therefore the objective of this investigation was to optimize a methodology that would increase the conductivity of the film to facilitate high resolution imaging with a scanning electron microscopy and to preserve the porous nature of the film that could potentially be damaged by the energy of the FIB. Sputter coating the sample with a thin layer of iridium before creating the cross section with the FIB decreased sample charging and drifting, but differentiating the iron layer from the iridium coating with backscattered electron imaging was not definitive, making accurate assumptions of the delineation between the two metals difficult. Moreover, the porous nature of the film was lost due to beam damage following the FIB process. A thin layer plastication technique was therefore used to embed the porous film in epoxy resin that would provide support for the film during the FIB process. However, the thickness of the resin created using conventional thin layer plastication processing varied across the sample, making the measuring process only possible in areas where the resin layer was at its thinnest. Such variation required navigating the area for ideal milling areas, which increased the subjectivity of the process. We present a method to create uniform thin resin layers, of controlled thickness, that are ideal for quantifying the thickness of porous nonconductive films with FIB/scanning electron microscopy.</p>},
	keywords = {Epoxy resin embedding, focused ion beam, metal oxide ultrathin films, QUANTIFICATION, scanning electron microscopy, spin coating},
	doi = {10.1111/jmi.12683},
	url = {https://onlinelibrary.wiley.com/doi/abs/10.1111/jmi.12683},
	author = {PE{\~N}A, B. and OWEN, G.RH. and DETTELBACH, K.E. and BERLINGUETTE, C.P.}
}
@article {2648,
	title = {Implementation of a data repository-driven approach for targeted proteomics experiments by multiple reaction monitoring},
	journal = {Journal of Proteomics},
	volume = {72},
	number = {5},
	year = {2009},
	note = {ISI Document Delivery No.: 478RATimes Cited: 5Cited Reference Count: 30Walsh, Geraldine M. Lin, Shujun Evans, Daniel M. Khosrovi-Eghbal, Arash Beavis, Ronald C. Kast, Juergen},
	month = {Jul},
	pages = {838-852},
	type = {Article},
	abstract = {Multiple reaction monitoring (MRM), commonly employed for the mass spectrometric detection of small molecules, is rapidly gaining ground in proteomics. Its high sensitivity and specificity makes this targeted approach particularly useful when sample throughput or proteome coverage limits global studies. Existing tools to design MRM assays rely exclusively on theoretical predictions, or combine them with previous observations on the same type of sample. The additional mass spectrometric experimentation this requires can pose significant demands on time and material. To overcome these challenges, a new MRM worksheet was introduced into The Global Proteome Machine database (GPMDB) that provided all of the information needed to design MRM transitions based solely on archived observations made by other researchers in previous experiments. This required replacing the precursor ion intensity by the number of peptide observations, which proved to be an adequate substitute if peptides did not occur in multiple forms. While the absence of collision energy information proved largely inconsequential, successful prediction of unique transitions depended on the type of fragment ion involved. The design of MRM assays for iTRAQ-labeled tryptic peptides obtained from human platelet proteins demonstrated the usefulness of the MRM worksheet also for quantitative applications. This workflow, which relies exclusively on experimental observations stored in data repositories, therefore represents an attractive alternative for the prediction of MRM transitions prior to experimental validation and optimization. (C) 2008 Elsevier B.V. All rights reserved.},
	keywords = {ABSOLUTE, Data repository, HIGH-SENSITIVITY, LIBRARIES, Multiple reaction monitoring, PEPTIDES, PHOSPHORYLATION, PLASMA-PROTEINS, PLATELETS, PREDICTION, PROTEIN IDENTIFICATION, PROTEOMICS, QUANTIFICATION, SHOTGUN PROTEOMICS, Tandem mass spectrometry, TANDEM MASS-SPECTROMETRY, Targeted},
	isbn = {1874-3919},
	url = {<Go to ISI>://000268604400013},
	author = {Walsh, G. M. and Lin, S. and Evans, D. M. and Khosrovi-Eghbal, A. and Beavis, R. C. and Kast, J.}
}
@article {2121,
	title = {Making connections for life: an in vivo map of the yeast interactome},
	journal = {Hfsp Journal},
	volume = {2},
	number = {5},
	year = {2008},
	note = {ISI Document Delivery No.: 355VHTimes Cited: 1Cited Reference Count: 28Kast, Juergen},
	month = {Oct},
	pages = {244-250},
	type = {Article},
	abstract = {Proteins are the true workhorses of any cell. To carry out specific tasks, they frequently bind other molecules in their surroundings. Due to their structural complexity and flexibility, the most diverse array of interactions is seen with other proteins. The different geometries and affinities available for such interactions typically bestow specific functions on proteins. Having available a map of protein - protein interactions is therefore of enormous importance for any researcher interested in gaining insight into biological systems at the level of cells and organisms. In a recent report, a novel approach has been employed that relies on the spontaneous folding of complementary enzyme fragments fused to two different proteins to test whether these interact in their actual cellular context [Tarassov et al., Science 320, 1465-1470 (2008)]. Genome- wide application of this protein- fragment complementation assay has resulted in the first map of the in vivo interactome of Saccharomyces cerevisiae. The current data show striking similarities but also significant differences to those obtained using other large- scale approaches for the same task. This warrants a general discussion of the current state of affairs of protein - protein interaction studies and foreseeable future trends, highlighting their significance for a variety of applications and their potential to revolutionize our understanding of the architecture and dynamics of biological systems.},
	keywords = {AMINO-ACIDS, CELL-CULTURE, COMPLEXES, CROSS-LINKING, IDENTIFICATION, MASS-SPECTROMETRY, PROTEIN-PROTEIN INTERACTIONS, QUANTIFICATION, QUANTITATION, SACCHAROMYCES-CEREVISIAE},
	isbn = {1955-2068},
	url = {<Go to ISI>://000259736700002},
	author = {Kast, J.}
}
