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138 results on '"Horn, David M."'

1. Quantitative Analysis of Human Pluripotency and Neural Specification by In-Depth (Phospho)Proteomic Profiling

Author

Singec, Ilyas, Crain, Andrew M, Hou, Junjie, Tobe, Brian TD, Talantova, Maria, Winquist, Alicia A, Doctor, Kutbuddin S, Choy, Jennifer, Huang, Xiayu, La Monaca, Esther, Horn, David M, Wolf, Dieter A, Lipton, Stuart A, Gutierrez, Gustavo J, Brill, Laurence M, and Snyder, Evan Y

Subjects
Biochemistry and Cell Biology, Biological Sciences, Neurosciences, Stem Cell Research, Transplantation, Stem Cell Research - Embryonic - Non-Human, Stem Cell Research - Embryonic - Human, Regenerative Medicine, Underpinning research, 1.1 Normal biological development and functioning, Generic health relevance, Animals, Cell Differentiation, Cell Lineage, Cells, Cultured, Computational Biology, Gene Expression Profiling, Gene Knockdown Techniques, Humans, Neurons, Phosphoproteins, Pluripotent Stem Cells, Proteome, Proteomics, Signal Transduction, Transcriptome, Clinical Sciences, Biochemistry and cell biology
Abstract

Controlled differentiation of human embryonic stem cells (hESCs) can be utilized for precise analysis of cell type identities during early development. We established a highly efficient neural induction strategy and an improved analytical platform, and determined proteomic and phosphoproteomic profiles of hESCs and their specified multipotent neural stem cell derivatives (hNSCs). This quantitative dataset (nearly 13,000 proteins and 60,000 phosphorylation sites) provides unique molecular insights into pluripotency and neural lineage entry. Systems-level comparative analysis of proteins (e.g., transcription factors, epigenetic regulators, kinase families), phosphorylation sites, and numerous biological pathways allowed the identification of distinct signatures in pluripotent and multipotent cells. Furthermore, as predicted by the dataset, we functionally validated an autocrine/paracrine mechanism by demonstrating that the secreted protein midkine is a regulator of neural specification. This resource is freely available to the scientific community, including a searchable website, PluriProt.

Published
2016

2. Orbitrap Mass Spectrometry and High-Field Asymmetric Waveform Ion Mobility Spectrometry (FAIMS) Enable the in-Depth Analysis of Human Serum Proteoforms

Author

Kline, Jake T., primary, Belford, Michael W., additional, Boeser, Cornelia L., additional, Huguet, Romain, additional, Fellers, Ryan T., additional, Greer, Joseph B., additional, Greer, Sylvester M., additional, Horn, David M., additional, Durbin, Kenneth R., additional, Dunyach, Jean-Jacques, additional, Ahsan, Nagib, additional, and Fornelli, Luca, additional

Published
2023
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6. Improved label-free quantification of intact proteoforms using field asymmetric ion mobility spectrometry

Author

Kline, Jake T., primary, Belford, Michael W., additional, Huang, Jingjing, additional, Greer, Joseph B., additional, Bergen, David, additional, Fellers, Ryan T., additional, Greer, Sylvester M., additional, Horn, David M., additional, Zabrouskov, Vlad, additional, Huguet, Romain, additional, Boeser, Cornelia L., additional, Durbin, Kenneth R., additional, and Fornelli, Luca, additional

Published
2023
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11. Intact Antibody Characterization Using Orbitrap Mass Spectrometry

Author

Hao, Zhiqi, primary, Zhang, Terry, additional, Xuan, Yue, additional, Wang, Hongxia, additional, Qian, Jie, additional, Lin, Shanhua, additional, Chen, Jenny, additional, Horn, David M., additional, Argoti, Dayana, additional, Beck, Alain, additional, Cianférani, Sarah, additional, Bennett, Patrick, additional, Miller, Ken, additional, and Makarov, Alexander, additional

Published
2015
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15. An automated matrix-assisted laser desorption/ ionization quadrupole Fourier transform ion cyclotron resonance mass spectrometer for 'bottom-up' proteomics

Author

Brock, Ansgar, Horn, David M., Peters, Eric C., Shaw, Christopher M., Ericson, Christer, Phung, Qui T., and Salomon, Arthur R.

Subjects
Mass spectrometry -- Research, Chemistry
Abstract

Here we describe a new quadrupole Fourier transform ion cyclotron resonance hybrid mass spectrometer equipped with an intermediate-pressure MALDI ion source and demonstrate its suitability for 'bottom-up' proteomics. The integration of a high-speed MALDI sample stage, a quadrupole analyzer, and a FT-ICR mass spectrometer together with a novel software user interface allows this instrument to perform high-throughput proteomics experiments. A set of linearly encoded stages allows sub-second positioning of any location on a mircotiter-sized target with up to 1536 samples with micrometer precision in the source focus of the ion optics. Such precise control enables internal calibration for high mass accuracy MS and MS/MS spectra using separate calibrant and analyte regions on the target plate, avoiding ion suppression effects that would result from the spiking of calibrants into the sample. An elongated open cylindrical analyzer cell with trap plates allows trapping of ions from 1000 to 5000 m/z without notable mass discrimination. The instrument is highly sensitive, detecting less than 50 amol of angiotensin II and neurotensin in [micro]LC MALDI MS run under standard experimental conditions. The automated tandem MS of a reversed-phase separated bovine serum albumin digest demonstrated a successful identification for 27 peptides covering 45% of the sequence. An automated tandem MS experiment of a reversed-phase separated yeast cytosolic protein digest resulted in 226 identified peptides corresponding to 111 different proteins from 799 MS/MS attempts. The benefits of accurate mass measurements for data validation for such experiments are discussed.

Published
2003

16. An automated noncontact deposition interface for liquid chromatography matrix-assisted laser desorption/ionization mass spectrometry

Author

Ericson, Christer, Phung, Qui T., Horn, David M., Peters, Eric C., Fitchett, Jonathan R., Ficarro, Scott B., Salomon, Arthur R., Brill, Laurence M., and Brock, Ansgar

Subjects
Chemistry, Analytic -- Research, Mass spectrometry -- Usage, Chemistry
Abstract

A new multichannel deposition system was developed for off-line liquid chromatography/matrix-assisted laser desorption/ionization mass spectrometry (LC/MALDI-MS). This system employs a pulsed electric field to transfer the eluents from multiple parallel columns directly onto MALDI targets without the column outlets touching the target surface. The deposition device performs well with a wide variety of solvents that have different viscosities, vapor pressures, polarities, and ionic strengths. Surface-modified targets were used to facilitate concentration and precise positioning of samples, allowing for efficient automation of high-throughput MALDI analysis. The operational properties of this system allow the user to prepare samples using MALDI matrixes whose properties range from hydrophilic to hydrophobic. The latter, exemplified by [alpha]-cyano-4-hydroxycinnamic acid, were typically processed with a multistep deposition method consisting of precoating of individual spots on the target plate, sample deposition, and sample recrystallization steps. Using this method, 50 amol of angiotensin II was detected reproducibly with high signal-to-noise ratio after LC separation. Experimental results show that there is no significant decrease in chromatographic resolution using this device. To assess the behavior of the apparatus for complex mixtures, 5 [micro]g of a tryptic digest of the cytosolic proteins of yeast was analyzed by LC/MALDI-MS and more than 13 500 unique analytes were detected in a single LC/MS analysis.

Published
2003

17. Generation of a bacterium with a 21 amino acid genetic code

Author

Mehl, Ryan A., Anderson, Christopher, Santoro, Stephen W., Lei Wang, Martin, Andrew B., King, David S., Horn David M., and Schultz, Peter G.

Subjects
Amino acids -- Chemical properties, Proteins -- Chemical properties, Carbon -- Chemical properties, Chemistry
Abstract

A totally new and independent bacterium is created with a 21 amino acid genetic code is created, which can biosynthesize an abnormal amino acid from fundamental carbon supplies and includes the amino acid in the proteins in relation with the yellowish-brown nonsense codon. Thus, the addition of any such organisms gives a chance to evaluate the result of adding new amino acids to the genetic code, and create proteins with new or increased biological tasks.

Published
2003

22. Detailed unfolding and folding of gaseous ubiquitin ions characterized by electron capture dissociation

Author

Breuker, Kathrin, Oh, HanBin, Horn, David M., Cerda, Blas A., and McLafferty, Fred W.

Subjects
Protein folding -- Research, Ubiquitin -- Chemical properties, Mass spectrometry -- Usage, Dissociation -- Analysis, Chemistry
Abstract

Unfolding and folding of gaseous ubiquitin ions is investigated by electron capture dissociation (ECD) mass spectrometry. ECD confirms that the 13+ ions represent separate conformers, probably with side-chain solvated alpha-helical structures.

Published
2002

25. Electron capture dissociation of gaseous multiply-charged proteins is favored at disulfide bonds and other sites of high hydrogen atom affinity

Author

Zubarev, Roman A., Kruger, Nathan A., Fridriksson, Einar K., Lewis, Mark A., Horn, David M., Carpenter, Barry K., and McLafferty, Fred W.

Subjects
Proteins -- Research, Sulfides -- Research, Chemistry
Abstract

Disulfide bonds in gaseous multiply-protonated proteins are preferably severed in the mass spectrometer by low-energy electrons, in contrast with the excitation of the ions by photons or low-energy collisions. For S-S cyclized proteins, capture of one electron can cleave both an S-S bond and a backbone bond in the same ring, or even both disulfide bonds linking two peptide chains, improving the sequence data obtainable by tandem mass spectrometry on proteins in trace quantities.

Published
1999

33. Phosphopeptide/Phosphoprotein Mapping by Electron Capture Dissociation Mass Spectrometry

Author

Shi, Stone D.-H., Hemling, Mark E., Carr, Steven A., Horn, David M., Lindh, Ingemar, and McLafferty, Fred W.

Subjects
Electrons -- Capture, Dissociation -- Research, Mass spectrometry -- Research, Phosphoproteins -- Research, Glycosylation -- Research, Phosphorylation -- Research, Casein -- Research, Chemistry
Abstract

Of methods for dissociation of multiply charged peptide and protein ions, electron capture dissociation (ECD) has the advantages of cleaving between a high proportion of amino acids, without loss of such posttranslational modifications as glycosylation and carboxylation. Here this capability is successfully extended to phosphorylation, for which collisionally activated dissociation (CAD) can cause extensive loss of [H.sup.3][PO.sup.4] and [HPO.sup.3]. As shown here, these losses are minimal in ECD spectra, an advantage for measuring the degree of phosphorylation. For phosphorylated peptides, ECD and CAD spectra give complementary backbone cleavages for identifying modification sites. For a 24-kDa heterogeneous phosphoprotein, bovine [Beta]-casein, activated ion ECD cleaved 87 of 208 backbone bonds that identified a phosphorylation site at Ser-15, and localized three more among Ser-17,-18, -19, and -22 and Thr-24, and the last among four other sites. This is the first direct site-specific characterization of this key post-translational modification on a protein without its prior degradation, such as proteolysis.

Published
2001

34. Activated Ion Electron Capture Dissociation for Mass Spectral Sequencing of Larger (42 kDa) Proteins

Author

Horn, David M., Ge, Ying, and McLafferty, Fred W.

Subjects
Electrons -- Capture, Dissociation -- Research, Mass spectrometry -- Research, Amino acid sequence -- Research, Chemical bonds -- Research, Proteins -- Analysis, Chemistry
Abstract

In previous studies, electron capture dissociation (ECD) has been successful only with ionized smaller proteins, cleaving between 33 of the 153 amino acid pairs of a 17 kDa protein. This has been increased to 99 cleavages by colliding the ions with a background gas while subjecting them to electron capture. Presumably this ion activation breaks intramolecular noncovalent bonds of the ion's secondary and tertiary structure that otherwise prevent separation of the products from the nonergodic ECD cleavage of a backbone covalent bond. In comparison to collisionally activated dissociation, this 'activated ion' (AI) ECD provides more extensive, and complementary, sequence information. AI ECD effected cleavage of 116, 60, and 47, respectively, backbone bonds in 29, 30, and 42 kDa proteins to provide extensive contiguous sequence information on both termini; AI conditions are being sought to denature the center portion of these large ions. This accurate 'sequence tag' information could potentially identify individual proteins in mixtures at far lower sample levels than methods requiring prior proteolysis.

Published
2000

35. Biomolecule Mass Spectrometry

Author

McLafferty, Fred W., Fridriksson, Einar K., Horn, David M., Lewis, Mark A., and Zubarev, Roman A.

Subjects
Mass spectrometry -- Usage -- Methods, Molecular biology -- Methods -- Usage, Science and technology, Usage, Methods
Abstract

Mass spectrometry (MS) has joined the powerful arsenal of techniques used for structural characterization of biological molecules (1-4). MS can determine the mass of the molecule and the masses of [...]

Published
1999

37. A boys & girls club for Richardson, Texas

Author

Horn, David M. and Faulk, Stephen L.

Subjects
Transparency in architecture, Boys -- Societies and clubs, Girls -- Societies and clubs, Boys & Girls Clubs of America, Richardson (Tex.), Community centers -- Design
Abstract

Thesis Statement: Architecture can be used to promote social interaction through the use of transparency. Social interaction provides today's youth an opportunity to realize their full potential as productive, responsible, and caring citizens. Facility Statement: A Boys and Girls Club for children between the ages 6-18 in Richardson, Texas. Context Statement: The facility will be located at the intersection of N. Floyd Rd. and Renner Rd. The site is adjacent to a middle class neighborhood and the University of Texas at Dallas.

Published
1999

38. Interlaboratory Study on Differential Analysis of Protein Glycosylation by Mass Spectrometry: The ABRF Glycoprotein Research Multi-Institutional Study 2012

Author

Leymarie, Nancy, primary, Griffin, Paula J., additional, Jonscher, Karen, additional, Kolarich, Daniel, additional, Orlando, Ron, additional, McComb, Mark, additional, Zaia, Joseph, additional, Aguilan, Jennifer, additional, Alley, William R., additional, Altmann, Friederich, additional, Ball, Lauren E., additional, Basumallick, Lipika, additional, Bazemore-Walker, Carthene R., additional, Behnken, Henning, additional, Blank, Michael A., additional, Brown, Kristy J., additional, Bunz, Svenja-Catharina, additional, Cairo, Christopher W., additional, Cipollo, John F., additional, Daneshfar, Rambod, additional, Desaire, Heather, additional, Drake, Richard R., additional, Go, Eden P., additional, Goldman, Radoslav, additional, Gruber, Clemens, additional, Halim, Adnan, additional, Hathout, Yetrib, additional, Hensbergen, Paul J., additional, Horn, David M., additional, Hurum, Deanna, additional, Jabs, Wolfgang, additional, Larson, Göran, additional, Ly, Mellisa, additional, Mann, Benjamin F., additional, Marx, Kristina, additional, Mechref, Yehia, additional, Meyer, Bernd, additional, Möginger, Uwe, additional, Neusüβ, Christian, additional, Nilsson, Jonas, additional, Novotny, Milos V., additional, Nyalwidhe, Julius O., additional, Packer, Nicolle H., additional, Pompach, Petr, additional, Reiz, Bela, additional, Resemann, Anja, additional, Rohrer, Jeffrey S., additional, Ruthenbeck, Alexandra, additional, Sanda, Miloslav, additional, Schulz, Jan Mirco, additional, Schweiger-Hufnagel, Ulrike, additional, Sihlbom, Carina, additional, Song, Ehwang, additional, Staples, Gregory O., additional, Suckau, Detlev, additional, Tang, Haixu, additional, Thaysen-Andersen, Morten, additional, Viner, Rosa I., additional, An, Yanming, additional, Valmu, Leena, additional, Wada, Yoshinao, additional, Watson, Megan, additional, Windwarder, Markus, additional, Whittal, Randy, additional, Wuhrer, Manfred, additional, Zhu, Yiying, additional, and Zou, Chunxia, additional

Published
2013
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40. Guidelines for reporting the use of mass spectrometry in proteomics

Author

Taylor, Chris F, primary, Binz, Pierre-Alain, additional, Aebersold, Ruedi, additional, Affolter, Michel, additional, Barkovich, Robert, additional, Deutsch, Eric W, additional, Horn, David M, additional, Hühmer, Andreas, additional, Kussmann, Martin, additional, Lilley, Kathryn, additional, Macht, Marcus, additional, Mann, Matthias, additional, Müller, Dieter, additional, Neubert, Thomas A, additional, Nickson, Janice, additional, Patterson, Scott D, additional, Raso, Roberto, additional, Resing, Kathryn, additional, Seymour, Sean L, additional, Tsugita, Akira, additional, Xenarios, Ioannis, additional, Zeng, Rong, additional, and Julian, Randall K, additional

Published
2008
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42. Human Proteinpedia enables sharing of human protein data

Author

Mathivanan, Suresh, primary, Ahmed, Mukhtar, additional, Ahn, Natalie G, additional, Alexandre, Hainard, additional, Amanchy, Ramars, additional, Andrews, Philip C, additional, Bader, Joel S, additional, Balgley, Brian M, additional, Bantscheff, Marcus, additional, Bennett, Keiryn L, additional, Björling, Erik, additional, Blagoev, Blagoy, additional, Bose, Ron, additional, Brahmachari, Samir K, additional, Burlingame, Alma S, additional, Bustelo, Xosé R, additional, Cagney, Gerard, additional, Cantin, Greg T, additional, Cardasis, Helene L, additional, Celis, Julio E, additional, Chaerkady, Raghothama, additional, Chu, Feixia, additional, Cole, Philip A, additional, Costello, Catherine E, additional, Cotter, Robert J, additional, Crockett, David, additional, DeLany, James P, additional, De Marzo, Angelo M, additional, DeSouza, Leroi V, additional, Deutsch, Eric W, additional, Dransfield, Eric, additional, Drewes, Gerard, additional, Droit, Arnaud, additional, Dunn, Michael J, additional, Elenitoba-Johnson, Kojo, additional, Ewing, Rob M, additional, Eyk, Jennifer Van, additional, Faca, Vitor, additional, Falkner, Jayson, additional, Fang, Xiangming, additional, Fenselau, Catherine, additional, Figeys, Daniel, additional, Gagné, Pierre, additional, Gelfi, Cecilia, additional, Gevaert, Kris, additional, Gimble, Jeffrey M, additional, Gnad, Florian, additional, Goel, Renu, additional, Gromov, Pavel, additional, Hanash, Samir M, additional, Hancock, William S, additional, Harsha, HC, additional, Hart, Gerald, additional, Hays, Faith, additional, He, Fuchu, additional, Hebbar, Prashantha, additional, Helsens, Kenny, additional, Hermeking, Heiko, additional, Hide, Winston, additional, Hjernø, Karin, additional, Hochstrasser, Denis F, additional, Hofmann, Oliver, additional, Horn, David M, additional, Hruban, Ralph H, additional, Ibarrola, Nieves, additional, James, Peter, additional, Jensen, Ole N, additional, Jensen, Pia Hønnerup, additional, Jung, Peter, additional, Kandasamy, Kumaran, additional, Kheterpal, Indu, additional, Kikuno, Reiko F, additional, Korf, Ulrike, additional, Körner, Roman, additional, Kuster, Bernhard, additional, Kwon, Min-Seok, additional, Lee, Hyoung-Joo, additional, Lee, Young-Jin, additional, Lefevre, Michael, additional, Lehvaslaiho, Minna, additional, Lescuyer, Pierre, additional, Levander, Fredrik, additional, Lim, Megan S, additional, Löbke, Christian, additional, Loo, Joseph A, additional, Mann, Matthias, additional, Martens, Lennart, additional, Martinez-Heredia, Juan, additional, McComb, Mark, additional, McRedmond, James, additional, Mehrle, Alexander, additional, Menon, Rajasree, additional, Miller, Christine A, additional, Mischak, Harald, additional, Mohan, S Sujatha, additional, Mohmood, Riaz, additional, Molina, Henrik, additional, Moran, Michael F, additional, Morgan, James D, additional, Moritz, Robert, additional, Morzel, Martine, additional, Muddiman, David C, additional, Nalli, Anuradha, additional, Navarro, J Daniel, additional, Neubert, Thomas A, additional, Ohara, Osamu, additional, Oliva, Rafael, additional, Omenn, Gilbert S, additional, Oyama, Masaaki, additional, Paik, Young-Ki, additional, Pennington, Kyla, additional, Pepperkok, Rainer, additional, Periaswamy, Balamurugan, additional, Petricoin, Emanuel F, additional, Poirier, Guy G, additional, Prasad, T S Keshava, additional, Purvine, Samuel O, additional, Rahiman, B Abdul, additional, Ramachandran, Prasanna, additional, Ramachandra, Y L, additional, Rice, Robert H, additional, Rick, Jens, additional, Ronnholm, Ragna H, additional, Salonen, Johanna, additional, Sanchez, Jean-Charles, additional, Sayd, Thierry, additional, Seshi, Beerelli, additional, Shankari, Kripa, additional, Sheng, Shi Jun, additional, Shetty, Vivekananda, additional, Shivakumar, K, additional, Simpson, Richard J, additional, Sirdeshmukh, Ravi, additional, Michael Siu, K W, additional, Smith, Jeffrey C, additional, Smith, Richard D, additional, States, David J, additional, Sugano, Sumio, additional, Sullivan, Matthew, additional, Superti-Furga, Giulio, additional, Takatalo, Maarit, additional, Thongboonkerd, Visith, additional, Trinidad, Jonathan C, additional, Uhlen, Mathias, additional, Vandekerckhove, Joël, additional, Vasilescu, Julian, additional, Veenstra, Timothy D, additional, Vidal-Taboada, José-Manuel, additional, Vihinen, Mauno, additional, Wait, Robin, additional, Wang, Xiaoyue, additional, Wiemann, Stefan, additional, Wu, Billy, additional, Xu, Tao, additional, Yates, John R, additional, Zhong, Jun, additional, Zhou, Ming, additional, Zhu, Yunping, additional, Zurbig, Petra, additional, and Pandey, Akhilesh, additional

Published
2008
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48. An Automated LC-MALDI FT-ICR MS Platform.

Author

Peters, Eric C., Brock, Ansgar, Horn, David M., Phung, Qui T., Ericson, Christer, Salomon, Arthur R., Ficarro, Scott B., and Brill, Laurence M.

Subjects
LIQUID chromatography, MATRIX-assisted laser desorption-ionization, FOURIER transform spectroscopy, ION cyclotron resonance spectrometry
Abstract

Describes an automated liquid chromatography-matrix-assisted laser desorption ionization Fourier-transform ion cyclotron resonance mass spectrometry platform for high-throughput proteomics. Flow chart for the protein profiling of biological samples; Automated deposition of a reversed-phase chromatography; Reaction of a lysine residue.

Published
2002

49. Electron Capture Dissociation of Multiply-Charged Oxygenated Cations. A Nonergodic Process

Author

Cerda, Blas A., Horn, David M., Breuker, Kathrin, Carpenter, Barry K., and McLafferty, Fred W.

Abstract

Several mechanistic aspects have been proposed as important in causing the unusual ion chemistry induced in multiply-charged protein cations by electron capture. The 5–7 eV energy released by neutralization appears to induce cleavage before energy randomization (nonergodic), and the electron forms radical species whose activation energies for dissociation should be much lower. In contrast, electron capture by [HO(C2H4O)24H + 2H]2+ions from polyethylene glycol yields no radical ions, losing H•consistent with the lower H•affinity of the hydroxyl and ether groups vs the amide and S–S functionalities of proteins. However, the dominant product ions, [HO(C2H4O)24–nH + H]+(n= 2 to 8), do appear to be formed by nonergodic dissociation of the hypervalent (M + 2H)1+•intermediate. The expected complementary alkoxy radical ion product is not found, possibly due to an energetic Franck–Condon relaxation. Precursors ionized with (NH4)22+and Na22+yield ECD products that are analogous but of different size (nvalues). Those for Na22+can be rationalized with structures proposed by Bowers and coworkers. ECD spectra of polyethers should be useful for sequencing.

Published
1999
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50. Human Proteinpedia enables sharing of human protein data

Author

Mathivanan, Suresh, Ahmed, Mukhtar, Ahn, Natalie G, Alexandre, Hainard, Amanchy, Ramars, Andrews, Philip C, Bader, Joel S, Balgley, Brian M, Bantscheff, Marcus, Bennett, Keiryn L, Björling, Erik, Blagoev, Blagoy, Bose, Ron, Brahmachari, Samir K, Burlingame, Alma S, Bustelo, Xosé R, Cagney, Gerard, Cantin, Greg T, Cardasis, Helene L, Celis, Julio E, Chaerkady, Raghothama, Chu, Feixia, Cole, Philip A, Costello, Catherine E, Cotter, Robert J, Crockett, David, DeLany, James P, De Marzo, Angelo M, DeSouza, Leroi V, Deutsch, Eric W, Dransfield, Eric, Drewes, Gerard, Droit, Arnaud, Dunn, Michael J, Elenitoba-Johnson, Kojo, Ewing, Rob M, Eyk, Jennifer Van, Faca, Vitor, Falkner, Jayson, Fang, Xiangming, Fenselau, Catherine, Figeys, Daniel, Gagné, Pierre, Gelfi, Cecilia, Gevaert, Kris, Gimble, Jeffrey M, Gnad, Florian, Goel, Renu, Gromov, Pavel, Hanash, Samir M, Hancock, William S, Harsha, HC, Hart, Gerald, Hays, Faith, He, Fuchu, Hebbar, Prashantha, Helsens, Kenny, Hermeking, Heiko, Hide, Winston, Hjernø, Karin, Hochstrasser, Denis F, Hofmann, Oliver, Horn, David M, Hruban, Ralph H, Ibarrola, Nieves, James, Peter, Jensen, Ole N, Jensen, Pia Hønnerup, Jung, Peter, Kandasamy, Kumaran, Kheterpal, Indu, Kikuno, Reiko F, Korf, Ulrike, Körner, Roman, Kuster, Bernhard, Kwon, Min-Seok, Lee, Hyoung-Joo, Lee, Young-Jin, Lefevre, Michael, Lehvaslaiho, Minna, Lescuyer, Pierre, Levander, Fredrik, Lim, Megan S, Löbke, Christian, Loo, Joseph A, Mann, Matthias, Martens, Lennart, Martinez-Heredia, Juan, McComb, Mark, McRedmond, James, Mehrle, Alexander, Menon, Rajasree, Miller, Christine A, Mischak, Harald, Mohan, S Sujatha, Mohmood, Riaz, Molina, Henrik, Moran, Michael F, Morgan, James D, Moritz, Robert, Morzel, Martine, Muddiman, David C, Nalli, Anuradha, Navarro, J Daniel, Neubert, Thomas A, Ohara, Osamu, Oliva, Rafael, Omenn, Gilbert S, Oyama, Masaaki, Paik, Young-Ki, Pennington, Kyla, Pepperkok, Rainer, Periaswamy, Balamurugan, Petricoin, Emanuel F, Poirier, Guy G, Prasad, T S Keshava, Purvine, Samuel O, Rahiman, B Abdul, Ramachandran, Prasanna, Ramachandra, Y L, Rice, Robert H, Rick, Jens, Ronnholm, Ragna H, Salonen, Johanna, Sanchez, Jean-Charles, Sayd, Thierry, Seshi, Beerelli, Shankari, Kripa, Sheng, Shi Jun, Shetty, Vivekananda, Shivakumar, K, Simpson, Richard J, Sirdeshmukh, Ravi, Michael Siu, K W, Smith, Jeffrey C, Smith, Richard D, States, David J, Sugano, Sumio, Sullivan, Matthew, Superti-Furga, Giulio, Takatalo, Maarit, Thongboonkerd, Visith, Trinidad, Jonathan C, Uhlen, Mathias, Vandekerckhove, Joël, Vasilescu, Julian, Veenstra, Timothy D, Vidal-Taboada, José-Manuel, Vihinen, Mauno, Wait, Robin, Wang, Xiaoyue, Wiemann, Stefan, Wu, Billy, Xu, Tao, Yates, John R, Zhong, Jun, Zhou, Ming, Zhu, Yunping, Zurbig, Petra, Pandey, Akhilesh, Mathivanan, Suresh, Ahmed, Mukhtar, Ahn, Natalie G, Alexandre, Hainard, Amanchy, Ramars, Andrews, Philip C, Bader, Joel S, Balgley, Brian M, Bantscheff, Marcus, Bennett, Keiryn L, Björling, Erik, Blagoev, Blagoy, Bose, Ron, Brahmachari, Samir K, Burlingame, Alma S, Bustelo, Xosé R, Cagney, Gerard, Cantin, Greg T, Cardasis, Helene L, Celis, Julio E, Chaerkady, Raghothama, Chu, Feixia, Cole, Philip A, Costello, Catherine E, Cotter, Robert J, Crockett, David, DeLany, James P, De Marzo, Angelo M, DeSouza, Leroi V, Deutsch, Eric W, Dransfield, Eric, Drewes, Gerard, Droit, Arnaud, Dunn, Michael J, Elenitoba-Johnson, Kojo, Ewing, Rob M, Eyk, Jennifer Van, Faca, Vitor, Falkner, Jayson, Fang, Xiangming, Fenselau, Catherine, Figeys, Daniel, Gagné, Pierre, Gelfi, Cecilia, Gevaert, Kris, Gimble, Jeffrey M, Gnad, Florian, Goel, Renu, Gromov, Pavel, Hanash, Samir M, Hancock, William S, Harsha, HC, Hart, Gerald, Hays, Faith, He, Fuchu, Hebbar, Prashantha, Helsens, Kenny, Hermeking, Heiko, Hide, Winston, Hjernø, Karin, Hochstrasser, Denis F, Hofmann, Oliver, Horn, David M, Hruban, Ralph H, Ibarrola, Nieves, James, Peter, Jensen, Ole N, Jensen, Pia Hønnerup, Jung, Peter, Kandasamy, Kumaran, Kheterpal, Indu, Kikuno, Reiko F, Korf, Ulrike, Körner, Roman, Kuster, Bernhard, Kwon, Min-Seok, Lee, Hyoung-Joo, Lee, Young-Jin, Lefevre, Michael, Lehvaslaiho, Minna, Lescuyer, Pierre, Levander, Fredrik, Lim, Megan S, Löbke, Christian, Loo, Joseph A, Mann, Matthias, Martens, Lennart, Martinez-Heredia, Juan, McComb, Mark, McRedmond, James, Mehrle, Alexander, Menon, Rajasree, Miller, Christine A, Mischak, Harald, Mohan, S Sujatha, Mohmood, Riaz, Molina, Henrik, Moran, Michael F, Morgan, James D, Moritz, Robert, Morzel, Martine, Muddiman, David C, Nalli, Anuradha, Navarro, J Daniel, Neubert, Thomas A, Ohara, Osamu, Oliva, Rafael, Omenn, Gilbert S, Oyama, Masaaki, Paik, Young-Ki, Pennington, Kyla, Pepperkok, Rainer, Periaswamy, Balamurugan, Petricoin, Emanuel F, Poirier, Guy G, Prasad, T S Keshava, Purvine, Samuel O, Rahiman, B Abdul, Ramachandran, Prasanna, Ramachandra, Y L, Rice, Robert H, Rick, Jens, Ronnholm, Ragna H, Salonen, Johanna, Sanchez, Jean-Charles, Sayd, Thierry, Seshi, Beerelli, Shankari, Kripa, Sheng, Shi Jun, Shetty, Vivekananda, Shivakumar, K, Simpson, Richard J, Sirdeshmukh, Ravi, Michael Siu, K W, Smith, Jeffrey C, Smith, Richard D, States, David J, Sugano, Sumio, Sullivan, Matthew, Superti-Furga, Giulio, Takatalo, Maarit, Thongboonkerd, Visith, Trinidad, Jonathan C, Uhlen, Mathias, Vandekerckhove, Joël, Vasilescu, Julian, Veenstra, Timothy D, Vidal-Taboada, José-Manuel, Vihinen, Mauno, Wait, Robin, Wang, Xiaoyue, Wiemann, Stefan, Wu, Billy, Xu, Tao, Yates, John R, Zhong, Jun, Zhou, Ming, Zhu, Yunping, Zurbig, Petra, and Pandey, Akhilesh

Abstract

Proteomic technologies, such as yeast two-hybrid, mass spectrometry (MS), protein/peptide arrays and fluorescence microscopy, yield multi-dimensional data sets, which are often quite large and either not published or published as supplementary information that is not easily searchable. Without a system in place for standardizing and sharing data, it is not fruitful for the biomedical community to contribute these types of data to centralized repositories.

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