Search

Your search keyword '"Speicher, Kaye D."' showing total 21 results
Start Over Author "Speicher, Kaye D."
21 results on '"Speicher, Kaye D."'

3. Deciphering the human platelet sheddome

Author

Fong, Karen P., Barry, Colin, Tran, Anh N., Traxler, Elizabeth A., Wannemacher, Kenneth M., Tang, Hsin-Yao, Speicher, Kaye D., Blair, Ian A., Speicher, David W., Grosser, Tilo, and Brass, Lawrence F.

Published
2011
Full Text
View/download PDF

8. 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
Full Text
View/download PDF

10. Analysis of human red cell spectrin tetramer (head-to-head) assembly using complementary univalent peptides

Author

DeSilva, Tara M., Kou-Cheng Peng, Speicher, Kaye D., and Speicher, David W.

Subjects
Erythrocytes -- Research, Cytoskeletal proteins -- Research, Biological sciences, Chemistry
Abstract

The properties of human red cell spectrin tetramer head-to-head formation were studied using two complementary univalent peptides, the alphaI domain and beta monomers. Tetramers from alphaI and beta monomers bind more easily as temperature decreased from 37 to zero degree centigrade. The interconversion between dimer and tetramer is influenced by the first alpha-beta head-to-head association and dissociation. Removal of the first site on a tetramer increases the rate of association and frees the dimer-tetramer interconversion from temperature constraints.

Published
1992

11. Correction: Corrigendum: Landscape of the mitochondrial Hsp90 metabolome in tumours

Author

Chae, Young Chan, primary, Angelin, Alessia, additional, Lisanti, Sofia, additional, Kossenkov, Andrew V., additional, Speicher, Kaye D., additional, Wang, Huan, additional, Powers, James F., additional, Tischler, Arthur S., additional, Pacak, Karel, additional, Fliedner, Stephanie, additional, Michalek, Ryan D., additional, Karoly, Edward D., additional, Wallace, Douglas C., additional, Languino, Lucia R., additional, Speicher, David W., additional, and Altieri, Dario C., additional

Published
2015
Full Text
View/download PDF

12. ABRF-PRG03: Phosphorylation Site Determination

Author

Arnott, David, Gawinowicz, Mary Ann, Grant, Raymond A., Neubert, Thomas A., Packman, Len C., Speicher, Kaye D., Stone, Kathryn, and Turck, Christoph W.

Subjects
Phosphopeptides, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Articles, Phosphorylation, Chemistry Techniques, Analytical, Chromatography, Liquid
Abstract

A fundamental aspect of proteomics is the analysis of post-translational modifications, of which phosphorylation is an important class. Numerous nonradioactivity-based methods have been described for high-sensitivity phosphorylation site mapping. The ABRF Proteomics Research Group has conducted a study to help determine how many laboratories are equipped to take on such projects, which methods they choose to apply, and how successful the laboratories are in implementing particular methodologies. The ABRF-PRG03 sample was distributed as a tryptic digest of a mixture of two proteins with two synthetic phosphopeptides added. Each sample contained 5 pmol of unphosphorylated protein digest, 1 pmol of each phosphopeptide from the same protein, and 200 fmol of a minor protein component. Study participants were challenged to identify the two proteins and the two phosphorylated peptides, and determine the site of phosphorylation in each peptide. Almost all respondents successfully identified the major protein component, whereas only 10% identified the minor protein component. Phosphorylation site analysis proved surprisingly difficult, with only 3 of the 54 laboratories correctly determining both sites of phosphorylation. Various strategies and instruments were applied to this task with mixed success; chromatographic separation of the peptides was clearly helpful, whereas enrichment by metal affinity chromatography met with surprisingly little success. We conclude that locating sites of phosphorylation remains a significant challenge at this level of sample abundance.

Published
2003

14. Landscape of the mitochondrial Hsp90 metabolome in tumours

Author

Chae, Young Chan, primary, Angelin, Alessia, additional, Lisanti, Sofia, additional, Kossenkov, Andrew V., additional, Speicher, Kaye D., additional, Wang, Huan, additional, Powers, James F., additional, Tischler, Arthur S., additional, Pacak, Karel, additional, Fliedner, Stephanie, additional, Michalek, Ryan D., additional, Karoly, Edward D., additional, Wallace, Douglas C., additional, Languino, Lucia R., additional, Speicher, David W., additional, and Altieri, Dario C., additional

Published
2013
Full Text
View/download PDF

18. Identification of the Amino Acid Mutations Associated With Human Erythrocyte Spectrin αII Domain Polymorphisms

Author

DiPaolo, Byron R., Speicher, Kaye D., and Speicher, David W.

Abstract

Four distinct spectrin all domain polymorphisms are known to occur in several nonwhite populations. Type 1 is essentially the only form found in whites and is also the most common form in nonwhites. In contrast to most other spectrin mutations that are single-base substitutions, two of the all domain polymorphisms, types 2 and 3, are particularly unusual because they appear to involve 4-Kd insertions relative to type 1. We have identified the mutations responsible for these polymorphisms using biochemical approaches and a computer database of spectrin-domain peptides separated by two-dimensional gels. The type 3 mutation is characterized by an apparent 4-Kd increase in all domain peptides with no change in pi. This apparent molecular weight increase is a sodium dodecyl sulfate (SDS) gel artifact resulting from an Arg → His mutation at residue 22 of the domain. The type 4 polymorphism shows a basic charge shift with no apparent change in molecular weight on gels. This charge shift results from a mutation of Thr → Arg at position 174 of the domain. This mutation appears to be linked to a “silent” mutation at position 130 from an lie → Val. Support for possible linkage was obtained from analysis of three unrelated donors with the type 2 polymorphism. The type 2 polymorphism shows both the charge shift characteristic of the type 4 mutation and the apparent size shift that defines the type 3 polymorphism. Analysis of type 2 peptides confirmed that the two mutations described above for type 4 as well as the mutation at residue 22 observed in type 3 occur simultaneously in type 2. The observation that the type 2 polymorphism is a composite of the type 3 and 4 mutations is especially surprising because the type 2 polymorphism occurs far more frequently than either the type 3 or 4 forms. The basis for apparent linkage between the mutations at residues 130 and 174, which are encoded by different exons, is also not clear. Identification of the mutations described here permits design of genetic screening analyses that can be applied to larger populations to evaluate this potential linkage.

Published
1993
Full Text
View/download PDF

20. ABRF-PRG04: differentiation of protein isoforms.

Author

Arnott D, Gawinowicz MA, Kowalak JA, Lane WS, Speicher KD, Turck CW, West KA, and Neubert TA

Subjects
Amino Acid Sequence, Carbonic Anhydrases genetics, Isoenzymes classification, Isoenzymes genetics, Isoenzymes isolation & purification, Mass Spectrometry, Molecular Sequence Data, Surveys and Questionnaires, Carbonic Anhydrases classification, Carbonic Anhydrases isolation & purification, Proteomics
Abstract

Accurate protein identification sometimes requires careful discrimination between closely related protein isoforms that may differ by as little as a single amino acid substitution or post-translational modification. The ABRF Proteomics Research Group sent a mixture of three picomoles each of three closely related proteins to laboratories who requested it in the form of intact proteins, and participating laboratories were asked to identify the proteins and report their results. The primary goal of the ABRF-PRG04 Study was to give participating laboratories a chance to evaluate their capabilities and practices with regards to sample fractionation (1D- or 2D-PAGE, HPLC, or none), protein digestion methods (in-solution, in-gel, enzyme choice), and approaches to protein identification (instrumentation, use of software, and/or manual techniques to facilitate interpretation), as well as determination of amino acid or post-translational modifications. Of the 42 laboratories that responded, 8 (19%) correctly identified all three isoforms and N-terminal acetylation of each, 16 (38%) labs correctly identified two isoforms, 9 (21%) correctly identified two isoforms but also made at least one incorrect identification, and 9 (21%) made no correct protein identifications. All but one lab used mass spectrometry, and data submitted enabled a comparison of strategies and methods used.

Published
2007

21. ABRF-PRG03: phosphorylation site determination.

Author

Arnott D, Gawinowicz MA, Grant RA, Neubert TA, Packman LC, Speicher KD, Stone K, and Turck CW

Subjects
Chromatography, Liquid, Phosphorylation, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Chemistry Techniques, Analytical, Phosphopeptides chemistry
Abstract

A fundamental aspect of proteomics is the analysis of post-translational modifications, of which phosphorylation is an important class. Numerous nonradioactivity-based methods have been described for high-sensitivity phosphorylation site mapping. The ABRF Proteomics Research Group has conducted a study to help determine how many laboratories are equipped to take on such projects, which methods they choose to apply, and how successful the laboratories are in implementing particular methodologies. The ABRF-PRG03 sample was distributed as a tryptic digest of a mixture of two proteins with two synthetic phosphopeptides added. Each sample contained 5 pmol of unphosphorylated protein digest, 1 pmol of each phosphopeptide from the same protein, and 200 fmol of a minor protein component. Study participants were challenged to identify the two proteins and the two phosphorylated peptides, and determine the site of phosphorylation in each peptide. Almost all respondents successfully identified the major protein component, whereas only 10% identified the minor protein component. Phosphorylation site analysis proved surprisingly difficult, with only 3 of the 54 laboratories correctly determining both sites of phosphorylation. Various strategies and instruments were applied to this task with mixed success; chromatographic separation of the peptides was clearly helpful, whereas enrichment by metal affinity chromatography met with surprisingly little success. We conclude that locating sites of phosphorylation remains a significant challenge at this level of sample abundance.

Published
2003

Catalog

Books, media, physical & digital resources
See catalog results