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911.
Ribosomal proteins mediate the hepatitis C virus IRES-HeLa 40S interaction 总被引:9,自引:0,他引:9
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Translation of the hepatitis C virus genomic RNA is mediated by an internal ribosome entry site (IRES). The 330-nt IRES RNA forms a binary complex with the small 40S ribosomal subunit as a first step in translation initiation. Here chemical probing and 4-thiouridine-mediated crosslinking are used to characterize the interaction of the HCV IRES with the HeLa 40S subunit. No IRES-18S rRNA contacts were detected, but several specific crosslinks to 40S ribosomal proteins were observed. The identity of the crosslinked proteins agrees well with available structural information and provides new insights into HCV IRES function. The protein-rich surface of the 40S subunit thus mediates the IRES-ribosome interaction. 相似文献
912.
Man WJ White IR Bryant D Bugelski P Camilleri P Cutler P Heald G Lord PG Wood J Kramer K 《Proteomics》2002,2(11):1577-1585
This study has investigated the protein changes in rat liver elicited by a group of model hepatotoxicants, methapyrilene, cyproterone acetate and dexamethasone and offers a compelling argument in support of the use of two-dimensional polyacrylamide gel electrophoresis and mass spectrometry for the identification of compound specific biomarkers. The different treatments caused distinct changes to the rat liver proteome. Many of the protein changes could be associated with the known pharmacological and toxicological mechanisms of action of these drugs, whereas for other proteins, the rationale behind the alterations was less obvious. Furthermore, these changes can be used to classify the treatments with a view to utilising them as 'molecular signatures' to further our understanding of less well studied drugs such as SKF-106686 (an adrenoreceptor agonist). This approach has the potential for opening up new avenues for the exploration of molecular mechanisms of toxicity. This paper has explored the feasibility of proteomics to provide valuable information on the biochemical consequences elicited by hepatototoxic drugs. 相似文献
913.
Mutation of a novel gene results in abnormal development of spermatid flagella,loss of intermale aggression and reduced body fat in mice 总被引:4,自引:0,他引:4
Campbell PK Waymire KG Heier RL Sharer C Day DE Reimann H Jaje JM Friedrich GA Burmeister M Bartness TJ Russell LD Young LJ Zimmer M Jenne DE MacGregor GR 《Genetics》2002,162(1):307-320
ROSA22 male mice are sterile due to a recessive gene-trap mutation that affects development of the spermatid flagellum. The defect involves the flagellar axoneme, which becomes unstable around the time of its assembly. Despite a subsequent complete failure in flagellar assembly, development of the spermatid head appears normal and the spermatid head is released at the correct stage in spermatogenesis. The mutation is pleiotropic. Although ROSA22 homozygote males have normal levels of circulating testosterone and display normal mating behavior, they do not exhibit intermale aggressive behavior and have reduced body fat. The mutated gene (Gtrgeo22) maps to mouse chromosome 10 and is closely flanked by two known genes, Madcam1 and Cdc34. Ribonuclease protection analysis indicates that expression of the flanking genes is unaffected by the mutation. Gtrgeo22 is expressed at low levels in epithelial cells in several tissues, as well as in testis and brain. Analysis of the peptide coding sequence suggests that Gtrgeo22 encodes a novel transmembrane protein, which contains dileucine and tyrosine-based motifs involved in intracellular sorting of transmembrane proteins. Analysis of the Gtrgeo22 gene product should provide novel insight into the molecular basis for intermale aggression and sperm flagellar development. 相似文献
914.
Austin RC Fox JE Werstuck GH Stafford AR Bulman DE Dally GY Ackerley CA Weitz JI Ray PN 《The Journal of biological chemistry》2002,277(49):47106-47113
Utrophin is a component of the platelet membrane cytoskeleton and participates in cytoskeletal reorganization (Earnest, J. P., Santos, G. F., Zuerbig, S., and Fox, J. E. B. (1995) J. Biol. Chem. 270, 27259-27265). Although platelets do not contain dystrophin, the identification of smaller C-terminal isoforms of dystrophin, including Dp71, which are expressed in a wide range of nonmuscle tissues and cell lines, has not been investigated. In this report, we have identified Dp71 protein variants of 55-60 kDa (designated Dp71Delta(110)) in the membrane cytoskeleton of human platelets. Both Dp71Delta(110) and utrophin sediment from lysed platelets along with the high speed detergent-insoluble pellet, which contains components of the membrane cytoskeleton. Like the membrane cytoskeletal proteins vinculin and spectrin, Dp71Delta(110) and utrophin redistributed from the high speed detergent-insoluble pellet to the integrin-rich low speed pellet of thrombin-stimulated platelets. Immunoelectron microscopy provided further evidence that Dp71Delta(110) was localized to the submembranous cytoskeleton. In addition to Dp71Delta(110), platelets contained several components of the dystrophin-associated protein complex, including beta-dystroglycan and syntrophin. To better understand the potential function of Dp71Delta(110), collagen adhesion assays were performed on platelets isolated from wild-type or Dp71-deficient (mdx(3cv)) mice. Adhesion to collagen in response to thrombin was significantly decreased in platelets isolated from mdx(3cv) mice, compared with wild-type platelets. Collectively, our results provide evidence that Dp71Delta(110) is a component of the platelet membrane cytoskeleton, is involved in cytoskeletal reorganization and/or signaling, and plays a role in thrombin-mediated platelet adhesion. 相似文献
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917.
Schwarzenbacher R von Delft F Abdubek P Ambing E Biorac T Brinen LS Canaves JM Cambell J Chiu HJ Dai X Deacon AM DiDonato M Elsliger MA Eshagi S Floyd R Godzik A Grittini C Grzechnik SK Hampton E Jaroszewski L Karlak C Klock HE Koesema E Kovarik JS Kreusch A Kuhn P Lesley SA Levin I McMullan D McPhillips TM Miller MD Morse A Moy K Ouyang J Page R Quijano K Robb A Spraggon G Stevens RC van den Bedem H Velasquez J Vincent J Wang X West B Wolf G Xu Q Hodgson KO Wooley J Wilson IA 《Proteins》2004,54(4):810-813
918.
Erlandsen H Canaves JM Elsliger MA von Delft F Brinen LS Dai X Deacon AM Floyd R Godzik A Grittini C Grzechnik SK Jaroszewski L Klock HE Koesema E Kovarik JS Kreusch A Kuhn P Lesley SA McMullan D McPhillips TM Miller MD Morse A Moy K Ouyang J Page R Robb A Quijano K Schwarzenbacher R Spraggon G Stevens RC van den Bedem H Velasquez J Vincent J Wang X West B Wolf G Hodgson KO Wooley J Wilson IA 《Proteins》2004,54(4):806-809
919.
Schwarzenbacher R Deacon AM Jaroszewski L Brinen LS Canaves JM Dai X Elsliger MA Floyd R Godzik A Grittini C Grzechnik SK Klock HE Koesema E Kovarik JS Kreusch A Kuhn P Lesley SA McMullan D McPhillips TM Miller MD Morse A Moy K Nelson MS Ouyang J Page R Robb A Quijano K Spraggon G Stevens RC van den Bedem H Velasquez J Vincent J von Delft F Wang X West B Wolf G Hodgson KO Wooley J Wilson IA 《Proteins》2004,54(4):801-805
920.
Levin I Schwarzenbacher R McMullan D Abdubek P Ambing E Biorac T Cambell J Canaves JM Chiu HJ Dai X Deacon AM DiDonato M Elsliger MA Godzik A Grittini C Grzechnik SK Hampton E Jaroszewski L Karlak C Klock HE Koesema E Kreusch A Kuhn P Lesley SA McPhillips TM Miller MD Morse A Moy K Ouyang J Page R Quijano K Reyes R Robb A Sims E Spraggon G Stevens RC van den Bedem H Velasquez J Vincent J von Delft F Wang X West B Wolf G Xu Q Hodgson KO Wooley J Wilson IA 《Proteins》2004,56(3):629-633