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33 results on '"Weinberger, Scot R."'

7. MPSA abstracts

Author

Aminlari, Mahmoud, Asquith, Thomas, Sarlo, Katherine, Bailey, Jerome M., Tu, Oanh, Issai, Gilbert, Ha, Alice, Shively, John E., Bell, Alexander W., Baur, Nicole C., Bergeron, John J. M., Ou, Wei -Jia, Thomas, David Y., Cianflone, Katherine, Baldo, Allain, Hincke, Maxwell T., Momparler, Richard L., Laliberté, Josée, Thomson, David M. P., Sutherland, M., Besada, Vladimir, Gonzalez, Javier, Padron, Gabriel, Garay, Hilda, Reyes, Osvaldo, Takao, Toshifumi, Shimonishi, Yasutsugu, Bischoff, Rainer, Roecklin, Dominique, Bouchon, Bernadette, Klarskov, Klaus, Van Dorsselaer, Alain, Brake, Patricia G., Pacitti, Anne, Higgins, Terry, Stevis, Panos, Malinowski, John, McElhiney, Sue, Huang, Janes, Vestal, Christine, Buckel, Scott D., Stevenson, Tracy, Loo, Joseph A., Caffrey, Martin, Wang, Jin, Wallace, Carmichael J. A., Clark-Lewis, Ian, Carraway, C. A. Carothers, Huang, J., Li, Y., Juang, S. -H., Gallo, A., Mayer, B. J., Carraway, K. L., Coleman, Patrick L., Sarpong, Daniel, Deerfield, II, David W., Holland-Minkley, Amanda, Hempel, John D., Nicholas, Jr., Hugh B., Denslow, Nancy D., Folmar, Leroy C., Sullivan, Craig V., Dixon, James D., Mark, Jonathan P., Elicone, Christopher P., Maleknia, Simin D., McGuinness, Brian F., Regnier, Fred E., Afeyan, Noubar B., Dolence, Julia M., Poulter, C. Dale, Egorov, Tsezi, Musolyamov, Alexander, Popineau, Yves, Andersen, Jens, Roepstorff, Peter, Falkenstein, Roberto J., Biscoglio de Jiménez Bonino, Mirtha J., Peña, Clara, Gauggel, D. L., Asquith, T. N., Isfort, R. J., Miller, N. S., Cody, D. B., Giblin, Michael F., Wong, Tuck C., Quinn, Thomas P., Grant, Gregory A., Crankshaw, Mark W., Griffith, Scott, Schroeder, Steve, Quinn, Thomas, Guinet, F., Petillot, Y., Chapsal, J. M., Dubayle, J., Greco, F., Barge, O., Forest, E., Valentin, C., Hahn, Frederick M, Baker, Jonathan A., Poulter, C. Dale, Haniu, Mitsuru, Kenney, William C., Rohde, Michael F., Harman, James G., Lee, Eun Ju, Glasgow, Joel, Lew, Sew Fen, Belduz, Ali O., Harris, Reed J., Molony, Michael S., Keyt, Lene H., Wu, Shiaw -Lin, Hawke, David H., Tso, Jaqueline, Early, Sherrell, Miller, Chad G., Hayman, G. Thomas, Miernyk, Jan A., Hellman, Ulf, Wernstedt, Christer, Góñez, Jorge, Hess, Daniel, Studer, Ralph, Hunziker, Peter E., Hirano, Hisashi, Watanabe, Yoshihiro, Barbashov, Sergei F., Komatsu, Setsuko, Hemmings, Andrew M., Miyagi, Masaru, Tsunasawa, Susumu, Huber, Reuben E., Roth, Nathan J., Gaunt, Michael T., Jenö, Paul, Mini, Thierry, Moes, Suzette, Horst, Martin, Jinnai, Kenji, Ashizawa, Tetsuo, Atassi, M. Zouhair, Johnsen, Anders H., Jensen, Hanne, Rehfeld, Jens F., Kamo, Masaharu, Kawakami, Takao, Miyatake, Norifumi, Tsugita, Akira, Keen, JN, Zagalsky, PF, Findlay, JBC, Kraft, Regine, Kostka, Susanne, Hartmann, Enno, Krutzsch, Henry C., Inman, John K., Machalinski, Claudia, Bonino, Mirtha Biscoglio de Jiménez, McRorie, Donald K., Dieckmann, Gregg R., Heilman, Susan, DeGrado, William F., Pecoraro, Vincent L., Kenny, James, Sahakian, Julie, Tso, Jacqueline, Moyer, Mary B., Burkhart, William A., Muranova, Tatyana, Makova, Lubov, Nicholas, Hugh, Hempel, John, Hinich, Amy, Deerfield, David, Behrmann, Joseph, Ropelewski, Alex, Nixon, Lori, Maneri, Leonard, Nugent, Kerry, Stoney, Ken, Wieser, John, Ohguro, Hiroshi, Palczewski, Krzysztof, Walsh, Kenneth A., Johnson, Richard S., Packman, Leonard C, Webster, Carl, Gray, John, Padrón, G., Morera, V., González, L. J., Támbara, Y., Besada, V., Villalonga, R., Chinea, G., Reyes, O., Bringas, H. Garay R., Nazábal, C., Parkinson, Bruce P., Yamada, Kent A., Randolph, Anne, Pisano, Anthony, Packer, Nicole H., Redmond, John W., Williams, Keith L., Gooley, Andrew A., Rasmussen, Hanne H., Mørtz, Ejvind, Mann, Matthias, Celis, Julio E., Rasmussen, Lone K., Sørensen, Esben S., Petersen, Torben E., Gliemann, Jørgen, Jensen, Poul Henning, Renlund, Staffan, Wadensten, Henrik, Persson, Annika, Persson, Per, Johansson, Agneta, Edlund, Per -Olof, Rose, Donald J., Sack, Ragna, Apffel, Alex, Miller, Chad, Levine, Rodney L., Sakaguchi, Kazuyasu, Zambrano, Nicola, Lewis, Marc S., Baldwin, Eric T., Shapiro, Bruce A., Erickson, John W, Omichinski, James G., Clore, G. Marius, Gronenborn, Angela M., Appella, Ettore, Schröder, Werner, Moser, Irmgard, Pansegrau, Werner, Lanka, Erich, Simpson, Richard J., Eddes, James, Ji, Hong, Reid, Gavin E., Moritz, Robert L., Højrup, Peter, Speicher, David W., Reim, David F., Speicher, Kaye D., Srinivasa, B. R., Barde, S. P., Stirtan, William G., Sukhanova, Alyona, Vorob'ev, Sergey, Gabibov, Alexander, Bronstein, Igor, Tanaka, Kenji, Einaga, Kuniko, Tsukada, Minoru, Tait, Jonathan F., Fujikawa, Kazuo, Takamoto, Keiji, Satake, Kazuo, Vakser, Ilya A., Velikodvorskaia, V. V., Gabibov, A. G., Rabinkov, A. G., Videler, Tennie, Osborne, Michael, Moore, Geoffrey, James, Richard, Kleanthous, Colin, Walent, Jane H., Bessen, Richard, Marsh, Dick, Clore, G. Marius, Niece, Ronald L., Tsao, Francis H. C., Wang, Hong, Weinberger, Scot R., Chakel, Lynn M., Wondrak, Ewald M., Kimmel, Alan R., and Louis, John M.

Published
1994
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8. Functional wave time-lag focusing matrix-assisted laser desorption/ionization in a linear time-of-flight mass spectrometer: improved mass accuracy

Author

Whittal, Randy M., Russon, Larry M., Weinberger, Scot R., and Li, Liang

Subjects
Ionization -- Research, Mass spectrometry -- Research, Ions -- Research, Chemistry
Abstract

A strength of matrix-assisted laser desorption/ionization (MALDI) mass spectrometry is its ability to analyze mixtures without separation. MALDI mass spectrometers capable of providing a linear mass calibration over a broad mass range should find wide use in these applications. This work addresses issues pertinent to mass measurement accuracy of a time-lag focusing MALDI time-of-flight instrument and presents a new approach to improving mass accuracy by using a functional wave extraction pulse, instead of a square wave, for time-lag focusing. A model is described of an ideal extraction pulse shape that provides constant total kinetic energy for all ions. If total kinetic energy is constant, then there is an exact linear correlation between ion mass and flight time raised to the second power. Using a descending wave extraction pulse, it is demonstrated that mass accuracy of better than 30 ppm using two internal calibrants and better than 70 ppm using external calibrants can be obtained over a 25 ku mass range. The practical aspects of an instrument needed to obtain consistent mass accuracy is discussed. It is found that ion flight time shows a small dependence upon laser flux; flight times increase slightly as the flux increases. But this dependence is much smaller than is observed in continuous-extraction MALDI.

Published
1997

14. Detection of the photosystem I:ferredoxin complex by backscattering interferometry

Author

Setif, Pierre, Harris, Nathan, Lagoutte, Bernard, Dotson, Stephen, and Weinberger, Scot R.

Subjects
Backscattering -- Analysis, Ferredoxins -- Chemical properties, Ferredoxins -- Optical properties, Interferometry -- Usage, Photosystem I -- Chemical properties, Protein binding -- Analysis, Chemistry
Abstract

The dissociation constant [K.sub.d] of the photosystem I (PSI):ferredoxin compelx is measured by backscattering interferometry (BSI) with cyanobacterial PSI and ferredoxin. The results have provided evidence that the main contribution for the high affinity binding of ferredoxin to PSI is because of a single region of PsaE comprising arginine 39.

Published
2010

15. Detection of the Photosystem I:Ferredoxin Complex by Backscattering Interferometry

Author

Sétif, Pierre, Harris, Nathan, Lagoutte, Bernard, Dotson, Stephen, and Weinberger, Scot. R

Abstract

The dissociation constant Kdof the photosystem I (PSI):ferredoxin complex has been measured by backscattering interferometry (BSI) with cyanobacterial PSI (350 kDa) and ferredoxin (10.5 kDa). The BSI signal, consisting of shifts for interference fringes resulting from a change in refractive index due to complex formation, was monitored as ferredoxin concentration was titrated. Kdvalues of 0.14−0.38 μM were obtained with wild-type PSI whereas no complex was detectable with a PSI mutant containing a single mutation (R39Q) in the PsaE extrinsic subunit. These results are in quantitative agreement with previous functional determinations consisting in the detection of fast electron transfer within the complex. They provide evidence that the main contribution for the high affinity binding of ferredoxin to PSI is due to a single region of PsaE comprising arginine 39. They do not support the existence of a secondary binding site that could have escaped functional detection.

Published
2024
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19. Time-of-Flight Mass Spectrometry

Author

Weinberger, Scot R., primary, Davis, Stephen, additional, Makarov, Alexander, additional, Thompson, Steve, additional, Purves, Randy, additional, and Whittal, Randy M., additional

Published
2006
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23. The Use of SELDI ProteinChip® Array Technology in Renal Disease Research.

Author

Walker, John M., Goligorsky, Michael S., Fung, Eric, Diamond, Deb, Simonsesn, Anja Hviid, and Weinberger, Scot R.

Abstract

Proteomics approaches can be useful in identifying biomarkers of renal disease as well as in understanding biological processes specific to renal function. When combined with laser-capture microdissection (LCM), proteomics techniques can identify biomarkers that are specific to structures of the renal parenchyma such sas glomeruli, proximal tubules, or distal tubules, thus increasing the specificity of markers. In addition, since proteomics can be applied to urine as well as cells of the renal parenchyma, proteomics has the potential to identify biomarkers that could be useful in non invasive clinical tests. [ABSTRACT FROM AUTHOR]

Published
2003
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29. Limited Acid Hydrolysis as a Means of Fragmenting Proteins Isolated upon Proteinchip® Array Surfaces

Author

Lin, Shanhua, Tornatore, Pete, Weinberger, Scot R., King, Daniel, and Orlando, Ron

Abstract

ProteinChip Array technology enables protein purification, protein profiling and biomarker discovery on a convenient biochip platform. Traditional proteomic approaches towards protein identification rely upon the generation of peptides through the use of specific proteases. However, for a variety of reasons, the digestion of proteins bound to planar arrays using specific proteases, such as trypsin, has proven to be difficult, at times providing little or no protein digestion at all. Additionally, should more than one protein be present on the array surface, the digestion product consists of peptides from different proteins, adding another dimension of complexity to database mining approaches. These factors have driven our group to explore alternative means of on-chip protein digestion. In this article, we describe an approach to generating peptide maps by limited acid hydrolysis. Depending upon the adsorbed protein, this method requires between 500 femtomol to 5 picomol of protein for on-chip hydrolysis. Besides generating several internal peptide fragments, limited acid hydrolysis also has the advantage of generating peptide ladders from the N- or C-terminus of the protein. From these ladders, a partial primary sequence of the protein can be directly derived using analysis by a simple laser desorption/ionization mass spectrometer. Furthermore, tandem mass spectrometry (MS/MS) can be performed on several internal peptide fragments, thus facilitating the identification of several proteins within a mixture. Based upon the preliminary results of this work, we continue to explore the possibility of using limited acid hydrolysis to identify unknown proteins captured on ProteinChip Array surfaces.

Published
2001
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31. Intrinsic Buffer Hydroxyl Radical Dosimetry Using Tris(hydroxymethyl)aminomethane.

Author

Roush AE, Riaz M, Misra SK, Weinberger SR, and Sharp JS

Subjects
Oxidation-Reduction, Photolysis, Proteins analysis, Proteins chemistry, Proteomics methods, Hydroxyl Radical analysis, Hydroxyl Radical chemistry, Mass Spectrometry methods, Tromethamine chemistry
Abstract

Fast photochemical oxidation of proteins (FPOP) is a powerful covalent labeling tool that uses hydroxyl radicals generated by laser flash photolysis of hydrogen peroxide to footprint protein surfaces. Because radical production varies with many experimental parameters, hydroxyl radical dosimeters have been introduced to track the effective radical dosage experienced by the protein analyte. FPOP experiments performed using adenine optical radical dosimetry containing protein in Tris buffer demonstrated unusual dosimetry behavior. We have investigated the behavior of Tris under oxidative conditions in detail. We find that Tris can act as a novel gain-of-signal optical hydroxyl radical dosimeter in FPOP experiments. This new dosimeter is also amenable to inline real-time monitoring, thereby allowing real-time adjustments to compensate for differences in samples for their quenching ability.

Published
2020
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32. Current developments in SELDI affinity technology.

Author

Tang N, Tornatore P, and Weinberger SR

Subjects
Molecular Probe Techniques trends, Molecular Probes chemical synthesis, Molecular Probes chemistry, Protein Array Analysis methods, Protein Array Analysis trends, Proteins analysis, Proteins chemistry, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization methods, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization trends
Abstract

The overall history and recent advancements in Surface-Enhanced Laser Desorption/Ionization (SELDI) affinity technology is reviewed. A detailed account of SELDI technology, utilizing Immobilized-Metal Affinity surfaces, pseudo-specific chromatographic surfaces, and biospecific interactive surfaces, is presented with particular emphasis placed upon examination of fundamental characteristics as well as specific applications for each. Finally, a detailed review of the specific use of such affinity surfaces in fundamental aspects of clinical, process, and research proteomics activity is presented., (Copyright 2003 Wiley Periodicals, Inc., Mass Spec Rev 23:34-44, 2004)

Published
2004
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