DOI: 10.1016/s0076-6879(10)83011-3. Visual Proteomics

Visual Proteomics

10.1016/s0076-6879(10)83011-3

Crossref book-chapter

Elsevier

Methods in Enzymology (78)

Bibliography

FÃ¶rster, F., Han, B.-G., & Beck, M. (2010). Visual Proteomics. Cryo-EM, Part C: Analyses, Interpretation, and Case Studies, 215â243.

Authors 3

Friedrich Förster (first)
Bong-Gyoon Han (additional)
Martin Beck (additional)

References 37 Referenced 74

10.1038/nmeth.1390 / Nat. Methods / Visual proteomics of the human pathogen Leptospira interrogans by Beck (2009)
10.1073/pnas.230282097 / Proc. Natl. Acad. Sci. USA / Toward detecting and identifying macromolecules in a cellular context: Template matching applied to electron tomograms by Bohm (2000)
10.1016/j.cell.2008.11.016 / Cell / The native 3D organization of bacterial polysomes by Brandt (2009)
10.1016/j.jsb.2005.04.006 / J. Struct. Biol. / A resolution criterion for electron tomography based on cross-validation by Cardone (2005)
10.1126/science.1066198 / Science / Crystal structure of the free radical intermediate of pyruvate: Ferredoxin oxidoreductase by Chabrière (2001)
10.1038/226421a0 / Nature / Three dimensional reconstructions of spherical viruses by Fourier synthesis from electron micrographs by Crowther (1970)
10.1021/pr700624e / J. Proteome Res. / A “tagless” strategy for identification of stable protein complexes genome-wide by multidimensional orthogonal chromatographic separation and iTRAQ reagent tracking by Dong (2008)
10.1016/S0076-6879(98)90019-2 / Methods Enzymol. / Purification of yeast mitochondrial chaperonin 60 and co-chaperonin 10 by Dubaquie (1998)
10.1016/j.ultramic.2006.02.004 / Ultramicroscopy / CTF determination and correction in electron cryotomography by Fernandez (2006)
10.1111/j.1365-2958.2004.04077.x / Mol. Microbiol. / Functional consequences of single:double ring transitions in chaperonins: Life in the cold by Ferrer (2004)
{'key': '10.1016/S0076-6879(10)83011-3_bib0080', 'series-title': 'Dissertation', 'article-title': 'Quantitative Analysis of macromolecules in cryoelectron tomograms using correlation methods', 'author': 'Förster', 'year': '2005'} / Dissertation / Quantitative Analysis of macromolecules in cryoelectron tomograms using correlation methods by Förster (2005)
10.1016/j.jsb.2007.07.006 / J. Struct. Biol. / Classification of cryo-electron sub-tomograms using constrained correlation by Förster (2008)
10.1073/pnas.0813068106 / Proc. Natl. Acad. Sci. USA / Survey of large protein complexes in D. vulgaris reveals great structural diversity by Han (2009)
10.1038/nrm1684 / Nat. Rev. / AAA+ proteins: Have engine, will work by Hanson (2005)
10.1017/S0033583504003920 / Q. Rev. Biophys. / Realizing the potential of electron cryo-microscopy by Henderson (2004)
10.1016/S0959-440X(96)80055-8 / Curr. Opin. Struct. Biol. / Scores for sequence searches and alignments by Henikoff (1996)
10.1016/0014-5793(95)00222-U / FEBS Lett. / Equatorial split of holo-chaperonin from Thermus thermophilus by ATP and K+ by Ishii (1995)
10.1021/ac025747h / Anal. Chem. / Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search by Keller (2002)
10.1016/j.jmb.2005.08.017 / J. Mol. Biol. / Crystallographic studies on decameric Brucella spp. Lumazine synthase: A novel quaternary arrangement evolved for a new function? by Klinke (2005)
10.1126/science.1176343 / Science / Proteome organization in a genome-reduced bacterium by Kuhner (2009)
{'key': '10.1016/S0076-6879(10)83011-3_bib0135', 'series-title': 'Electron Tomography', 'first-page': '197', 'article-title': 'Least-squares method of alignment using markers', 'author': 'Lawrence', 'year': '1992'} / Electron Tomography / Least-squares method of alignment using markers by Lawrence (1992)
10.1109/MSP.2006.1628882 / IEEE Signal. Process. Mag. / Cryo-electron tomography of biological specimens by Leis (2006)
10.1038/nature08184 / Nature / Proteome-wide cellular protein concentrations of the human pathogen Leptospira interrogans by Malmstrom (2009)
10.1021/bi047848a / Biochemistry / Crystal structure of lumazine synthase from Mycobacterium tuberculosis as a target for rational drug design: Binding mode of a new class of purinetrione inhibitors by Morgunova (2005)
10.1016/j.jsb.2004.10.006 / J. Struct. Biol. / TOM software toolbox: Acquisition and analysis for electron tomography by Nickell (2005)
10.1038/nrm1861 / Nat. Rev. / A visual approach to proteomics by Nickell (2006)
10.1016/j.jsb.2006.04.014 / J. Struct. Biol. / Mapping 70S ribosomes in intact cells by cryoelectron tomography and pattern recognition by Ortiz (2006)
10.1128/jb.174.21.6928-6937.1992 / J. Bacteriol. / Identification and molecular analysis of a 63-kilodalton stress protein from Neisseria gonorrhoeae by Pannekoek (1992)
10.1093/nar/gkj059 / Nucleic Acids Res. / MODBASE: A database of annotated comparative protein structure models and associated resources by Pieper (2006)
10.1016/j.jsb.2008.05.003 / J. Struct. Biol. / A visualization and segmentation toolbox for electron microscopy by Pruggnaller (2008)
10.1006/jmbi.1995.0542 / J. Mol. Biol. / Studies on the lumazine synthase/riboflavin synthase complex of Bacillus subtilis: Crystal structure analysis of reconstituted, icosahedral beta-subunit capsids with bound substrate analogue inhibitor at 2.4Å resolution by Ritsert (1995)
10.1016/j.jsb.2003.11.007 / J. Struct. Biol. / FindEM—A fast, efficient program for automatic selection of particles from electron micrographs by Roseman (2004)
10.1016/S0022-2836(02)00016-5 / J. Mol. Biol. / Enzyme function less conserved than anticipated by Rost (2002)
10.1083/jcb.150.1.F13 / J. Cell Biol. / AAA proteins. Lords of the ring by Vale (2000)
10.1016/j.jsb.2006.07.014 / J. Struct. Biol. / 3D reconstruction and processing of volumetric data in cryo-electron tomography by Winkler (2007)
10.1016/j.jsb.2009.08.002 / J. Struct. Biol. / Contrast transfer function correction applied to cryo-electron tomography and sub-tomogram averaging by Zanetti (2009)
10.1006/jmbi.2000.4435 / J. Mol. Biol. / X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6A resolution: Determinants of thermostability revealed from structural comparisons by Zhang (2001)

Dates

Type	When
Created	14 years, 10 months ago (Oct. 1, 2010, 4:40 a.m.)
Deposited	6 years, 8 months ago (Dec. 7, 2018, 1:26 p.m.)
Indexed	3 weeks, 6 days ago (July 27, 2025, 3:52 a.m.)
Issued	15 years, 7 months ago (Jan. 1, 2010)
Published	15 years, 7 months ago (Jan. 1, 2010)
Published Print	15 years, 7 months ago (Jan. 1, 2010)

Funders 0

None

BibTeX

@inbook{F_rster_2010, title={Visual Proteomics}, ISSN={0076-6879}, url={http://dx.doi.org/10.1016/s0076-6879(10)83011-3}, DOI={10.1016/s0076-6879(10)83011-3}, booktitle={Cryo-EM, Part C: Analyses, Interpretation, and Case studies}, publisher={Elsevier}, author={Förster, Friedrich and Han, Bong-Gyoon and Beck, Martin}, year={2010}, pages={215–243} }

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