@article {2276,
	title = {Utility of formaldehyde cross-linking and mass spectrometry in the study of protein-protein interactions},
	journal = {Journal of Mass Spectrometry},
	volume = {43},
	number = {6},
	year = {2008},
	note = {ISI Document Delivery No.: 319PPTimes Cited: 22Cited Reference Count: 54Sutherland, Brent W. Toews, Judy Kast, Juergen},
	month = {Jun},
	pages = {699-715},
	type = {Article},
	abstract = {For decades, formaldehyde has been routinely used to cross-link proteins in cells, tissue, and in some instances, even entire organisms. Due to its small size, formaldehyde can readily permeate cell walls and membranes, resulting in efficient cross-linking, i.e. the formation of covalent bonds between proteins, DNA, and other reactive molecules. Indeed, formaldehyde cross-linking is an instrumental component of many mainstream analytical/cell biology techniques including chromatin immunoprecipitation (ChIP) of protein-DNA complexes found in nuclei; immunohistological analysis of protein expression and localization within cells, tissues, and organs; and mass spectrometry (MS)-compatible silver-staining methodologies used to visualize low abundance proteins in polyacrylamide gels. However, despite its exquisite suitability for use in the analysis of protein environments within cells, formaldehyde has yet to be commonly employed in the directed analysis of protein-protein interactions and cellular networks. The general purpose of this article is to discuss recent advancements in the use of formaldehyde cross-linking in combination with MS-based methodologies. Key advantages and limitations to the use of formaldehyde over other cross-linkers and technologies currently used to study protein-protein interactions are highlighted, and formaldehyde-based experimental approaches that are proving very promising in their ability to accurately and efficiently identify novel protein-protein and multiprotein interaction complexes are presented. Copyright (c) 2008 John Wiley \& Sons, Ltd.},
	keywords = {ANTIGEN-RETRIEVAL, CHROMATIN IMMUNOPRECIPITATION, COMPLEXES, CROSS-LINKING, FORMALDEHYDE, IDENTIFICATION, IMMUNOHISTOCHEMISTRY, INTERACTION NETWORKS, MASS SPECTROMETRY, PARAFFIN-EMBEDDED TISSUE, protein interactions, PROTEOMICS, review, SURFACE-TOPOLOGY, THROUGHPUT},
	isbn = {1076-5174},
	url = {<Go to ISI>://000257176400001},
	author = {Sutherland, B. W. and Toews, J. and Kast, J.}
}
@article {934,
	title = {Diversity in structure and function of the Ets family PNT domains},
	journal = {Journal of Molecular Biology},
	volume = {342},
	number = {4},
	year = {2004},
	note = {ISI Document Delivery No.: 855WLTimes Cited: 17Cited Reference Count: 86},
	month = {Sep},
	pages = {1249-1264},
	type = {Article},
	abstract = {The PNT (or Pointed) domain, present within a subset of the Ets family of transcription factors, is structurally related to the larger group of SAM domains through a common tertiary arrangement of four alpha-helices. Previous studies have shown that, in contrast to the PNT. domain from Tel, this domain from Ets-1 contains an additional N-terminal helix integral to its folded structure. To further investigate the structural plasticity of the PNT domain, we have used NMR spectroscopy to characterize this domain from two additional Ets proteins, Erg and GABPalpha. These studies both define the conserved and variable features of the PNT domain, and demonstrate that the additional N-terminal helix is also present in GABPa, but not Erg. In contrast to Tel and Yan, which self-associate to form insoluble polymers, we also show that the isolated PNT domains from Ets-1, Ets-2, Erg, Fli-1, GABPalpha, and Pnt-P2 are monomeric in solution. Furthermore, these soluble PNT domains do not associate in any pair-wise combination. Thus these latter Ets family PNT domains likely mediate interactions with additional components of the cellular signaling or transcriptional machinery. (C) 2004 Elsevier Ltd. All rights reserved.},
	keywords = {ALPHA-MOTIF SAM, ASSIGNMENT, AUTOMATED, CHEMICAL-SHIFT, DIPOLAR COUPLINGS, ENDOTHELIAL-CELL DIFFERENTIATION, Erg, GABP, GENE, NMR-SPECTRA, POINTED DOMAIN, protein interactions, PROTEIN-KINASE, SAM domain, TRANSCRIPTION FACTOR},
	isbn = {0022-2836},
	url = {<Go to ISI>://000224005500015},
	author = {Mackereth, C. D. and Scharpf, M. and Gentile, L. N. and Macintosh, S. E. and Slupsky, C. M. and McIntosh, L. P.}
}
