2003
DOI: 10.1002/chin.200320293
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Structural Proteomics: Toward High‐Throughput Structural Biology as a Tool in Functional Genomics

Abstract: Biochemistry Biochemistry Z 0250 Structural Proteomics: Toward High-Throughput Structural Biology as a Tool in Functional Genomics -[33 refs.]. -(YEE, A.; PARDEE, K.; CHRISTENDAT, D.; SAVCHENKO, A.; EDWARDS, A. M.; ARROWSMITH*, C. H.; Acc. Chem. Res. 36 (2003) 3, 183-189; Ontario Cancer Inst., Dep. Med. Biophys., Univ. Toronto, Toronto, Ont. M5G 2C4, Can.; Eng.) -Lindner 20-293

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Cited by 22 publications
(29 citation statements)
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“…However, biochemical studies to characterize these new proteins, such as quantitative binding assays and highresolution structural studies 1; 2; 27; 28 , are often hampered by low protein solubility. Up to 80% of nonmembrane proteins that have been identified so far are unsuitable for structural studies due to low solubility [29][30][31] . Similar problems related to poor protein solubility occur in the pharmaceutical industry where it has been estimated that more than 90% of all potential protein pharmaceuticals are unsuitable for preclinical or clinical development due to low solubility 32 .…”
Section: Introductionmentioning
confidence: 99%
“…However, biochemical studies to characterize these new proteins, such as quantitative binding assays and highresolution structural studies 1; 2; 27; 28 , are often hampered by low protein solubility. Up to 80% of nonmembrane proteins that have been identified so far are unsuitable for structural studies due to low solubility [29][30][31] . Similar problems related to poor protein solubility occur in the pharmaceutical industry where it has been estimated that more than 90% of all potential protein pharmaceuticals are unsuitable for preclinical or clinical development due to low solubility 32 .…”
Section: Introductionmentioning
confidence: 99%
“…It is essential to categorize the determined structures into several groups together with annotated proteins for a structure-based functional prediction. Recently, Yee et al (2003) demonstrated a total of 27 hypothetical proteins from MTH that could be categorized to deduce their functional annotation from a structure that was determined by NMR spectroscopy or X-ray crystallography.…”
Section: Function Discovery From Protein Structurementioning
confidence: 99%
“…Since there is no doubt that the three-dimensional structure of a protein could provide an essential clue for the fundamental questions about its biological functions, structural proteomics projects could fill up the universe of protein folding space provided an accurate prediction of the structure-function relationship. For structural proteomics research, two major experimental techniques (X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy) with newly developed high throughput techniques (Staunton et al, 2003;Terwilliger, 2003;Yee et al, 2003) have played a central role in determining the protein structures on a genomic scale. Other approaches, homology modeling (Sanchez et al, 2000) and electron microscopy (Henderson, 1995) will also become important tools in the near future since these methods could be complementary to NMR and X-ray crystallography in structural proteomics research.…”
Section: Introductionmentioning
confidence: 99%
“…The burgeoning genomic information now available makes vast numbers of proteins accessible for structural and functional studies, and many large-scale projects have developed automated protocols for amplifying, cloning, and expressing genes, and for screening proteins for desirable properties [1][2][3][4][5]. Similar strides have been made in streamlining protein purification, but production of sufficient material for detailed structural and functional characterization remains labor-intensive and time-consuming [3,4,6,7].…”
Section: Introductionmentioning
confidence: 99%