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- 1. ヒトTリンパ球好性ウイルスI型：疾患関連、診断、および治療 human t lymphotropic virus type i disease associations diagnosis and treatment
- 2. ヒトTリンパ球好性ウイルスI型：ウイルス学、病因、および疫学 human t lymphotropic virus type i virology pathogenesis and epidemiology
- 3. 成人T細胞性白血病/リンパ腫の臨床症状、病理学的特徴、および診断 clinical manifestations pathologic features and diagnosis of adult t cell leukemia lymphoma
- 4. 供血者スクリーニング：臨床検査 blood donor screening laboratory testing
- 5. 非ホジキンリンパ腫の病理の概要 overview of the pathobiology of the non hodgkin lymphomas
- The thioredoxin antioxidant system.
- Lu J1, Holmgren A2.Author information 1Division of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77 Stockholm, Sweden. Electronic address: Jun.email@example.comDivision of Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77 Stockholm, Sweden. Electronic address: Arne.Holmgren@ki.se.AbstractThe thioredoxin (Trx) system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin, is a key antioxidant system in defense against oxidative stress through its disulfide reductase activity regulating protein dithiol/disulfide balance. The Trx system provides the electrons to thiol-dependent peroxidases (peroxiredoxins) to remove reactive oxygen and nitrogen species with a fast reaction rate. Trx antioxidant functions are also shown by involvement in DNA and protein repair by reducing ribonucleotide reductase, methionine sulfoxide reductases, and regulating the activity of many redox-sensitive transcription factors. Moreover, Trx systems play critical roles in the immune response, virus infection, and cell death via interaction with thioredoxin-interacting protein. In mammalian cells, the cytosolic and mitochondrial Trx systems, in which TrxRs are high molecular weight selenoenzymes, together with the glutathione-glutaredoxin (Grx) system (NADPH, glutathione reductase, GSH, and Grx) control the cellular redox environment. Recently mammalian thioredoxin and glutathione systems have been found to be able to provide the electrons crossly and to serve as a backup system for each other. In contrast, bacteria TrxRs are low molecular weight enzymes with a structure and reaction mechanism distinct from mammalian TrxR. Many bacterial species possess specific thiol-dependent antioxidant systems, and the significance of the Trx system in the defense against oxidative stress is different. Particularly, the absence of a GSH-Grx system in some pathogenic bacteria such as Helicobacter pylori, Mycobacterium tuberculosis, and Staphylococcus aureus makes the bacterial Trx system essential for survival under oxidative stress. This provides an opportunity to kill these bacteria by targeting the TrxR-Trx system.
- Free radical biology & medicine.Free Radic Biol Med.2014 Jan 8;66:75-87. doi: 10.1016/j.freeradbiomed.2013.07.036. Epub 2013 Jul 27.
- The thioredoxin (Trx) system, which is composed of NADPH, thioredoxin reductase (TrxR), and thioredoxin, is a key antioxidant system in defense against oxidative stress through its disulfide reductase activity regulating protein dithiol/disulfide balance. The Trx system provides the electrons to thi
- PMID 23899494
- Retrovirus-specific differences in matrix and nucleocapsid protein-nucleic Acid interactions: implications for genomic RNA packaging.
- Sun M, Grigsby IF, Gorelick RJ, Mansky LM, Musier-Forsyth K.Author information Department of Chemistry and Biochemistry, Center for Retroviral Research, and Center for RNA Biology, The Ohio State University, Columbus, Ohio, USA.AbstractRetroviral RNA encapsidation involves a recognition event between genomic RNA (gRNA) and one or more domains in Gag. In HIV-1, the nucleocapsid (NC) domain is involved in gRNA packaging and displays robust nucleic acid (NA) binding and chaperone functions. In comparison, NC of human T-cell leukemia virus type 1 (HTLV-1), a deltaretrovirus, displays weaker NA binding and chaperone activity. Mutation of conserved charged residues in the deltaretrovirus bovine leukemia virus (BLV) matrix (MA) and NC domains affects virus replication and gRNA packaging efficiency. Based on these observations, we hypothesized that the MA domain may generally contribute to NA binding and genome encapsidation in deltaretroviruses. Here, we examined the interaction between HTLV-2 and HIV-1 MA proteins and various NAs in vitro. HTLV-2 MA displays higher NA binding affinity and better chaperone activity than HIV-1 MA. HTLV-2 MA also binds NAs with higher affinity than HTLV-2 NC and displays more robust chaperone function. Mutation of two basic residues in HTLV-2 MA α-helix II, previously implicated in BLV gRNA packaging, reduces NA binding affinity. HTLV-2 MA binds with high affinity and specificity to RNA derived from the putative packaging signal of HTLV-2 relative to nonspecific NA. Furthermore, an HIV-1 MA triple mutant designed to mimic the basic character of HTLV-2 MA α-helix II dramatically improves binding affinity and chaperone activity of HIV-1 MA in vitro and restores RNA packaging to a ΔNC HIV-1 variant in cell-based assays. Taken together, these results are consistent with a role for deltaretrovirus MA proteins in viral RNA packaging.
- Journal of virology.J Virol.2014 Jan;88(2):1271-80. doi: 10.1128/JVI.02151-13. Epub 2013 Nov 13.
- Retroviral RNA encapsidation involves a recognition event between genomic RNA (gRNA) and one or more domains in Gag. In HIV-1, the nucleocapsid (NC) domain is involved in gRNA packaging and displays robust nucleic acid (NA) binding and chaperone functions. In comparison, NC of human T-cell leukemia
- PMID 24227839
- Quantitative analysis of human T-lymphotropic virus type 1 (HTLV-1) gene expression using nucleo-cytoplasmic fractionation and splice junction-specific real-time RT-PCR (qRT-PCR).
- Cavallari I, Rende F, Ciminale V.Author information Department of Surgery, Oncology, and Gastroenterology, University of Padova, Padova, Italy.AbstractLike other complex retroviruses such as HIV-1, HTLV-1 encodes several regulatory and auxiliary non-structural proteins from overlapping open reading frames through the generation of alternatively spliced mRNAs. HTLV-1 expression is orchestrated by the Tax and Rex regulatory proteins; Tax drives the transcription of the viral genome, while Rex acts at the posttranscriptional level by enhancing the nuclear export and expression of unspliced and incompletely spliced mRNAs. The present chapter is focused on the techniques employed to quantitate HTLV-1 mRNAs in the nuclear and cytoplasmic compartments. To ensure a quantitative transcript-specific detection of the levels of individual HTLV-1 mRNAs in a complex mixture of closely related species, splice junction-specific primers and TaqMan probes were used. As HTLV-1 gene regulation is based on the controlled nucleo-cytoplasmic export of the different viral mRNAs, we quantitated the individual viral transcripts in the nuclear and cytoplasmic fractions.
- Methods in molecular biology (Clifton, N.J.).Methods Mol Biol.2014;1087:325-37. doi: 10.1007/978-1-62703-670-2_26.
- Like other complex retroviruses such as HIV-1, HTLV-1 encodes several regulatory and auxiliary non-structural proteins from overlapping open reading frames through the generation of alternatively spliced mRNAs. HTLV-1 expression is orchestrated by the Tax and Rex regulatory proteins; Tax drives the
- PMID 24158834
- HTLV-1感染と自己免疫疾患におけるclinical questions
- 岡山 昭彦
- 臨床免疫・アレルギー科 62(6), 686-691, 2014-12
- NAID 40020294737
- Prevalence of human T-lymphotropic virus type 1 carriers among pregnant women in Hokkaido, Japan
- Yamada Takahiro,Togashi Takehiro,Tsutsumi Hiroyuki [他]
- Microbiology and immunology 58(8), 427–431, 2014-08
- NAID 40020164438
- Intracellular cyclic adenosine monophosphate regulates the efficiency of intercellular transmission of human T-lymphotropic virus type I
- Nakamura Tatsufumi,Satoh Katsuya,Nakamura Hideki,Yamasaki Hironori
- Clinical and Experimental Neuroimmunology 5(2), 209-215, 2014-06
- … Objective To investigate the relationship between the intercellular transmission efficiency of human T-lymphotropic virus type I (HTLV-I) and the signaling involved in actin polymerization during cytoskeletal reorganization in a comparative study of HTLV-I-infected T-cell lines derived from an HTLV-I-associated myelopathy/tropical spastic paraparesis (HAM/TSP) patient or an HTLV-I carrier. …
- NAID 120005476999
- human T-cell leukemia virus type 1, human T-cell leukemia virus-1, HTLV-1
- 成人Tリンパ球向性ウイルス1、ヒトTリンパ好性ウイルス1、成人T細胞白血病ウイルス1型、ヒトTリンパ好性ウイルス1型、ヒトTリンパ球向性ウイルス1型、human T lymphotropic virus-1 human T-lymphotropic virus-1, human T-cell lymphotropic virus type 1, human T-cell lymphotropic viruses type I, human T lymphotropic virus type 1
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- computer virus