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2,003 results on '"Shapiro, H."'

158. Regional Metabolism of the Brain

Author

Reivich, M., Sokoloff, L., Ginsberg, D. M., Kennedy, C., Shapiro, H., Greenberg, J., Zülch, K. J., editor, Kaufmann, W., editor, Hossmann, K.-A., editor, and Hossmann, V., editor

Published
1977
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171. Jackson’s Theorem in Higher Dimensions

Author

Newman, D. J., Shapiro, H. S., Blanc, Ch., editor, Ghizzetti, A., editor, Ostrowski, A., editor, Todd, J., editor, Unger, H., editor, van Wijngaarden, A., editor, Butzer, P. L., editor, and Korevaar, J., editor

Published
1964
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172. Commercial organolead compounds

Author

Frey, F. W., Shapiro, H., Davison, A., editor, Dewar, M. J. S., editor, Hafner, K., editor, Heilbronner, E., editor, Hofmann, U., editor, Niedenzu, K., editor, Schäfer, Kl., editor, Wittig, G., editor, and Boschke, F., editor

Published
1971
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173. The ecoresponsive genome of Daphnia pulex

Author

Colbourne, J. K., Pfrender, M. E., Gilbert, D., Thomas, W. K., Tucker, A., Oakley, T. H., Tokishita, S., Aerts, A., Arnold, G. J., Basu, M. K., Bauer, D. J., C當eres, C. E., Carmel, L., Casola, C., Choi, J. H., Detter, J. C., Dong, Q., Dusheyko, S., Eads, B. D., Frlich, T., Geiler-Samerotte, K. A., Gerlach, D., Hatcher, P., Jogdeo, S., Krijgsveld, J., Kriventseva, E. V., K�ltz, D., Laforsch, C., Lindquist, E., Lopez, J., Manak, J. R., Muller, J., Pangilinan, J., Patwardhan, R. P., Pitluck, S., Pritham, E. J., Rechtsteiner, A., Rho, M., Rogozin, I. B., Sakarya, O., Salamov, A., Schaack, S., Shapiro, H., Shiga, Y., Skalitzky, C., Smith, Z., Souvorov, A., Sung, W., Tang, Z., Tsuchiya, D., Tu, H., Vos, H., Wang, M., Wolf, Y. I., Yamagata, H., Yamada, Takuji, Ye, Y., Shaw, J. R., Andrews, J., Crease, T. J., Tang, H., Lucas, S. M., Robertson, H. M., Bork, P., Koonin, E. V., Zdobnov, E. M., Grigoriev, I. V., Lynch, M., Boore, J. L., Gerlach, Daniel, Kriventseva, Evgenia, and Zdobnov, Evgeny

Subjects
0106 biological sciences, Molecular Sequence Data, Gene Conversion, Gene Expression, Biology, Environment, 010603 evolutionary biology, 01 natural sciences, Genome, Daphnia pulex, Evolution, Molecular, 03 medical and health sciences, Genes, Duplicate, Gene Duplication, Gene duplication, Gene family, Animals, ddc:576.5, Gene conversion, Amino Acid Sequence, Gene, Ecosystem, Phylogeny, 030304 developmental biology, Regulation of gene expression, Genetics, 0303 health sciences, Multidisciplinary, Base Sequence, Daphnia/genetics/physiology, Metabolic Networks and Pathways/genetics, Gene Expression Profiling, fungi, Chromosome Mapping, Molecular Sequence Annotation, Sequence Analysis, DNA, biology.organism_classification, Adaptation, Physiological, Gene expression profiling, Daphnia, Gene Expression Regulation, Genes, Multigene Family, Metabolic Networks and Pathways
Abstract

We describe the draft genome of the microcrustacean Daphnia pulex, which is only 200 megabases and contains at least 30,907 genes. The high gene count is a consequence of an elevated rate of gene duplication resulting in tandem gene clusters. More than a third of Daphnia's genes have no detectable homologs in any other available proteome, and the most amplified gene families are specific to the Daphnia lineage. The coexpansion of gene families interacting within metabolic pathways suggests that the maintenance of duplicated genes is not random, and the analysis of gene expression under different environmental conditions reveals that numerous paralogs acquire divergent expression patterns soon after duplication. Daphnia-specific genes, including many additional loci within sequenced regions that are otherwise devoid of annotations, are the most responsive genes to ecological challenges.

Published
2011
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174. The François Vase in the context of the earliest Attic imports to Etruria

Author

Shapiro, H A, Iozzo, Mario, Lezzi-Hafter, Adrienne, Shapiro, H A ( H A ), Iozzo, M ( Mario ), Lezzi-Hafter, A ( Adrienne ), Reusser, Christoph, Shapiro, H A, Iozzo, Mario, Lezzi-Hafter, Adrienne, Shapiro, H A ( H A ), Iozzo, M ( Mario ), Lezzi-Hafter, A ( Adrienne ), and Reusser, Christoph

Published
2013

175. Cellular immune response to anaerobic exercise among gymnasts and untrained girls.

Author

Wolach B, Falk B, Kodesh E, Radnay J, Shapiro H, Yarom Y, and Eliakim A

Abstract

The purpose of the present study was to investigate the effect of anaerobic exercise on aspects of cellular immune function among 10-12-year-old highly trained female gymnasts (n = 7) compared with age- and maturity-matched untrained girls (n = 6). Blood samples were drawn before, immediately after, and 24 hr following exercise. Leukocyte number, particularly neutrophils and lymphocytes, increased following 30 s of supramaximal exercise and returned to baseline values following 24 hr in both groups. Total T-cell and B-cell concentrations, as well as T-helper (CD4) and T-suppressor (CD8) number increased immediately after exercise and decreased following 24 hr in both groups. The CD4:CD8 ratio was reduced following exercise mainly due to an increase in CD8. Natural killer cell count was elevated following exercise and continued to be elevated 24 hr following exercise in both groups. In summary, the exercise-induced changes in cellular immune function among both groups were similar to changes described in adults. [ABSTRACT FROM AUTHOR]

Published
1998
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181. Human lung cancer cell lines express cell membrane complement inhibitory proteins and are extremely resistant to complement-mediated lysis; a comparison with normal human respiratory epitheliumin vitro, and an insight into mechanism(s) of resistance

Author

Mark-Bentankur T, Rashkovsky L, Dov Ophir, Varsano S, and Shapiro H

Subjects
Lung Neoplasms, Lysis, Immunology, Cell, CD59 Antigens, CD59, Biology, Membrane Cofactor Protein, Cell membrane, Phosphoinositide Phospholipase C, Antigens, CD, Carcinoma, Non-Small-Cell Lung, Tumor Cells, Cultured, medicine, Humans, Immunology and Allergy, Complement Activation, Decay-accelerating factor, Complement Inactivator Proteins, Membrane Glycoproteins, CD55 Antigens, Phosphatidylinositol Diacylglycerol-Lyase, Cell Membrane, Epithelial Cells, Complement system, Nasal Mucosa, Cytolysis, medicine.anatomical_structure, Cell culture, Type C Phospholipases, Original Article
Abstract

SUMMARYHuman lung cancer expresses cell membrane complement inhibitory proteins (CIP). We investigated whether human lung cancer cell lines also express cell-membrane CIP molecules and whether the biology of CIP molecules in these cell lines differs from that of CIP in normal human respiratory epithelium in culture. The cell lines ChaGo K-1 and NCI-H596 were compared with normal human nasal epithelium in primary cultures in respect to the level of cell membrane CIP expression of membrane cofactor protein (MCP; CD46), decay-accelerating factor (DAF; CD55) and CD59, in respect to the level of cell resistance to complement-mediated lysis, and in respect to the contribution of cell membrane CIP to cell resistance against complement-mediated lysis. We found, using flow cytometry, that both human lung cancer cell lines expressed MCP, DAF and CD59, as did normal nasal epithelial cells. However, normal cells showed a large subpopulation of low DAF-expressing cells (60% of all cells) and a smaller subpopulation of high DAF-expressing cells (40%), while the lung cancer cell lines showed only one cell population, of high DAF expression. In addition, both lung cancer cell lines expressed higher MCP levels, and NCI-H596 cells showed higher levels of CD59. Cell resistance to complement-mediated lysis of both lung cancer cell lines was much higher than that of normal cells. Fifty percent normal human serum, under the same concentrations of complement activators, induced lysis of less than a mean of 10% of lung cancer cells, while lysing up to a mean of 50% of nasal epithelial cells. Lung cancer cell resistance to complement was due to its ability to prevent significant activation of complement upon its cell membrane, as manifested by a failure of complement activators to increase cell membrane deposition of C3-related fragments. The exact mechanism for this resistance remains obscure. Unexpectedly, neutralizing antibodies, anti-MCP and anti-DAF were entirely ineffective and anti-CD59 was only slightly effective (18% mean cell lysis) in increasing the susceptibility of the lung cancer cell lines to complement, while the same antibodies were very effective in facilitating complement-mediated lysis of the normal nasal epithelial cells (50% mean cell lysis with CD59 MoAb). On the other hand, detachment of DAF and CD59 by phosphatidylinositol-specific phospholipase C (PIPLC) from the lung cancer cell lines abrogated their resistance to lysis. We suggest that the biology of cell membrane CIP molecules in human lung cancer cell lines is different from that of CIP in normal respiratory epithelial cells. Human lung cancer cell lines are able to prevent significant complement activation upon its cell membrane and are therefore especially resistant to complement-mediated lysis. Complement resistance may serve this common and highly lethal human cancer as an escape mechanism from the body's immunosurveillance and prevent effective immunotherapy with tumour-specific MoAbs.

Published
1998
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182. Abstracts

Author

O’Callaghan, J. P., Williams, R. T., Cruise, C. J. E., Crago, R. R., Paluck, S. M., Carmichael, F. J., Shulman, D., Volgyesi, G., Brown, K., Lerman, J., England, S., Bryan, A. C., Wexler, H. R., Pikul, J., Thomas, T. C., Zornow, M. H., Scheller, M. S., Unger, R. J., Sosis, M., Heller, S., Maltby, J. R., Koehli, N., Ewen, A., Schaffer, E. A., Cramb, R. J., Fargas-Babjak, A., Diamond, M. J., Bailey, D., McPhee, A., Loper, K., Dorman, B., Ready, L. B., Hutchinson, A., Collman, P. I., Seal, R. F., Manning, G. T., Growe, G. H., Jenkins, L. C., Nathan, H. J., Harrison, M., Dubé, L., Sweet, J., Foster, C., Bourke, M., Cattran, C., Salle, G. de la, Robblee, J., Schwieger, I. M., Gallagher, C. J., Finlayson, D. C., Bryan, J. A., Daley, W., Skrobik, Y., Webster, R., Marquez-Julio, A., David, T., Cruise, C., Blaise, G. A., Lenis, S. G., Girard, D., Hollmann, C., Meloche, R., Ralley, F. E., Ramsay, J. R., Wynands, J. E., O’Connor, J. P., Bilodeau, J., O’Leary, G., Bimbaum, P., Weisel, R. D., Mullen, J. C., Young, P., Madonik, M., Ivanov, J., Teasdale, S. J., Burrows, F. A., Williams, W. G., Teoh, K. H., Edmonds, J., Belo, S., Mazer, C. D., Lim, G., Skinner, M. I., Rose, E. A., Knill, R. L., DeJesus, J. M., Robbins, G. R., Crosby, E. T., Miller, D. R., Hamilton, P. P., Badner, N. H., Nielson, W. R., Munk, S., Gelb, A. W., Smith, H., Yu, P. Y. H., Gambling, D. R., Cole, C., McMorland, G. H., Cheng, D. C. H., Chung, F., Burns, R. J., Feindel, C. M., Irish, C. X., Manninen, P. H., Wong, H., Kehler, C. H., Beattie, W. S., Fallen, E. L., Martin, R., McKenty, S., Tétrault, J. P., Russell, G. B., Snider, M. T., Loomis, J. L., Richard, R. B., Rutherford, T. M., McLeod, M. E., McEvedy, B. A. B., Kirpalani, H., Volgyesi, G. A., Vaghadia, H., Ford, R. W., Wong, D. T., Valley, R. D., Bissonnette, B., Flanagan, M. L., Fuller, J., Ross, P. L., Wolf, G. L., Simpson, J. I., McEllistrem, R., Schell, J., O’Matley, K., Cunningham, A. J., Berman, S., Rosenquist, R. W., Finucane, B. T., Bucyk, B., Carle, H. L., LeGatt, D., Finegan, B., Bigeleisen, P. E., Schisler, J. Q., Tateishi, A., Drummond, J. C., Fleischer, J. E., Shearman, G. T., Strong, H. A., Miyasaka, K., Sinclair, L., Moote, C. A., Lim, C., Code, W. E., Roth, S. H., Bland, B. H., Strunin, L., Lam, A., Nantau, W. E., Robertson, K. M., Hramiak, I. M., Elphinstone, M. G., Archer, D. P., Pappius, H. M., Bickler, P., Gregory, G. A., Severinghaus, J. W., Spintge, R., Droh, R., Chung, A., Taylor, A. E., Stone, R. M., Meier, H. M. R., Lautenschlaeger, E., Seyone, C., Devitt, J. H., McLean, R. F., Byrick, R. J., Mullen, J. B. M., Bell, R. S., Forbes, D., Kay, J. C., Swartz, J., Fear, D. W., Boylan, J. F., Carton, E., McDonald, N. J., Scarlett, W. P., Moriarty, J., Tessler, M. J., Biehl, D. R., Naughler, M. A., Liepert, D. J., Douglas, M. J., Kim, J. H. K., Ross, P. L. E., Oyston, J., Bell, S. D., Berman, R., Ensalada, L., Chan, V., Kirby, T. J., Sandler, A., Grant, R., Morgan, C., Page, M., Malm, D., Huckel, V., Jenkins, L., Salevsky, F. C., Whalley, D. G., O’Toole, D. P., Malviya, S., Benson, L., Johnston, A. E., Finegan, B. A., Clanachan, A. S., Buckley, D. N., Deguzman, C., Hewson, J. R., Forrest, J. B., Sharpe, M. D., Lam, A. M., Merchant, R., Irish, C. L., Murkin, J. M., Cleland, A., MacDonald, J. L., Mayer, R., Dobson, J. A. R., Davies, J. M., Hodgson, G. H., Tough, J., Cattran, C. B., Nolan, K., Allen, G., Erian, R. F., Donati, F., Bevan, D. R., VanDerSpek, A. F. L., Reynolds, P. I., Ashton-Miller, J. A., Stohler, C. J., Smith, C. E., Katz, J. M., Ruta, T. S., Mutch, W. A. C., Cole, D. J., Shapiro, H. M., Hagen, B. A., Labrecque, P., Tyler, J. L., Meyer, E., Casey, W. F., Trop, D., Farrar, J. K., Tweed, W. A., Meschino, A., Schwartz, M. L., Koch, J. P., Couper, J. L., Lombard, T. P., Arciszewski, S. A., Browne, R. A., Ashworth, E. J., Duke, P. C., Sitar, D. S., Benthuysen, J. L., Smith, N. T., Hall, R. I., Hug, C. C., Hudson, R. J., Bergstrom, R., Thomson, I. R., Sabourin, M. A., Rosenbloom, M. R., Chapman, K. R., Romanelli, J., Leenen, F. H. H., Broadman, L. M., Rice, L. J., Hannallah, R. S., Forbes, R. B., Croskey, K. L., Dull, D. L., Murray, D. J., Dillman, J. B., Murphy, K., Kaplan, R. F., Welborn, L. G., Fink, R., Sandhar, B. K., Goresky, G. V., Shaffer, E. A., Roy, W. L., Christensen, S. K., Farrow-Gillespie, A. C., Plante, J. M., Denault, P., Sloan, I. A., Koren, G., O’Callaghan, A. C., Goodman, A., Godfrey, S., Pudimat, M. A., Chong, C., Andrien, H. K., and Rose, D. K.

Published
1988
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199. Advanced Problems: 5200-5208

Author

Head, T. J., Wilansky, A., Hayes, David R., Newman, D. J., Greenberg, Ralph, Duemmel, James, Spira, Robert, Shapiro, H. S., and Carlitz, L.

Published
1964
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200. Advanced Problems: 5253-5260

Author

Hammer, Joseph, Gleason, A. M., Cohn, J. H. E., Taylor, K. D., Shapiro, H. S., Singmaster, David, Mahler, K., Rajagopalan, M., and Wilansky, A.

Published
1965
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