Institution
Texas Medical Center
Healthcare•Houston, Texas, United States•
About: Texas Medical Center is a healthcare organization based out in Houston, Texas, United States. It is known for research contribution in the topics: Population & Cancer. The organization has 2845 authors who have published 2394 publications receiving 79426 citations.
Topics: Population, Cancer, Stroke, Gene, Health care
Papers published on a yearly basis
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36 citations
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TL;DR: The effect of oxygen on sensitivity to x radiation was measured in mouse fibroblast cells growing in culture after sensitization of the cells to radiation by incorporation of 5bromodesoxyuridine into the desoxyribonucleic acid.
Abstract: The effect of oxygen on sensitivity to x radiation was measured in mouse fibroblast cells growing in culture after sensitization of the cells to radiation by incorporation of 5bromodesoxyuridine into the desoxyribonucleic acid. The radiosensitivity of cells irradiated in oxygen and in nitrogen was approximately the same. (C.H.)
36 citations
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TL;DR: In this paper, the authors used an antibody raised against the head portion of the Drosophila kinesin heavy chain to reveal the presence of this protein in membranous organelles from rat brain.
Abstract: Kinesin, a mechanochemical enzyme that translocates membranous organelles, was initially identified and purified from soluble extracts from vertebrate brains. However, immunocytochemical and morphological approaches have demonstrated that kinesin could be associated to intracellular membranous organelles. We used an antibody raised against the head portion of the Drosophila kinesin heavy chain to reveal the presence of this protein in membranous organelles from rat brain. By using differential centrifugation and immunoblotting we observed a 116 kDa protein that crossreacts with this antibody in microsomes, synaptic vesicles, and mitochondria. This protein could be extracted from mitochondria with low salt concentrations or ATP. The 116 kDa solubilized protein has been identified as conventional kinesin based on limited sequence analysis. We also show that a polyclonal antibody raised against mitochondria-associated kinesin recognizes soluble bovine brain kinesin. The soluble and mitochondrial membrane-associated kinesins show a different isoform pattern. These results are consistent with the idea that kinesin exists as multiple isoforms that might be differentially distributed within the cell. In addition digitonin fractionation of mitochondria combined with KI extraction revealed that kinesin is a peripheral protein, preferentially located in a cholesterol-free outer membrane domain; this domain has the features of contact points between the mitochondrial outer and inner membranes. The significance of these observations on the functional regulation of the mitochondria-associated kinesin is discussed. © 1994 Wiley-Liss, Inc.
36 citations
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University of Southern California1, University of Tennessee Health Science Center2, University of Washington3, Children's Mercy Hospital4, University of California, Davis5, Northwestern University6, Brown University7, Naval Medical Center Portsmouth8, University of Chicago9, Texas Medical Center10, Kaiser Permanente11, University of Miami12, Thomas Jefferson University13, University of Colorado Denver14, University of Louisville15, Memorial Hermann Healthcare System16
TL;DR: Pre-reduction antibiotics are unnecessary, non-operative outpatient management should be maximized, and minimally invasive techniques may be used to avoid laparotomy regarding intussusception in hemodynamically stable children without critical illness.
36 citations
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TL;DR: Oleic acid had a greater stimulatory effect on apoB-100 secretion in control HepG2 cells than in AdMTP-transduced cells, and adenoviral transduction partially attenuated the increase in triglyceride synthesis in response to lMTP overexpression.
Abstract: The intracellular concentration of the microsomal triglyceride transfer protein large subunit (lMTP), the abetalipoproteinemia gene product, is tightly controlled. To date, attempts at overexpressing lMTP in vivo or in vitro have been unsuccessful. We successfully overexpressed lMTP in HepG2 cells using an adenoviral vector containing an lMTP cDNA, AdMTP. AdMTP-transduced HepG2 cells overexpressed MTP activity. They secreted increased amounts of apoB-100 lipoproteins with LDL and HDL density into the medium. lMTP overexpression alone minimally changed the density profile of apoB-containing lipoproteins, but addition of oleic acid shifted the profile toward lower densities. Oleic acid had a greater stimulatory effect on apoB-100 secretion in control HepG2 cells than in AdMTP-transduced cells, because (i) adenoviral transduction per se suppressed protein synthesis, affecting apoB-100 and albumin equally, and (ii) adenoviral transduction partially attenuated the increase in triglyceride synthesis in response...
36 citations
Authors
Showing all 2878 results
Name | H-index | Papers | Citations |
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Eric N. Olson | 206 | 814 | 144586 |
Scott M. Grundy | 187 | 841 | 231821 |
Joseph Jankovic | 153 | 1146 | 93840 |
Geoffrey Burnstock | 141 | 1488 | 99525 |
George Perry | 139 | 923 | 77721 |
David Y. Graham | 138 | 1047 | 80886 |
James R. Lupski | 136 | 844 | 74256 |
Savio L. C. Woo | 135 | 785 | 62270 |
Henry T. Lynch | 133 | 925 | 86270 |
Joseph P. Broderick | 130 | 504 | 72779 |
Huda Y. Zoghbi | 127 | 463 | 65169 |
Paul M. Vanhoutte | 127 | 868 | 62177 |
Meletios A. Dimopoulos | 122 | 1371 | 71871 |
John B. Holcomb | 120 | 733 | 53760 |
John S. Mattick | 116 | 367 | 64315 |