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Enzymatic Degradation of PrPSc by a Protease Secreted from Aeropyrum pernix K1. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
Sako, Y., Nomura, N., Uchida, A., Ishida, Y., Morii, H., Koga, Y., Hoaki, T., and Maruyama, T. 1996. Aeropyrum pernix gen. nov., sp. nov., a novel aerobic hyperthermophilic archaeon growing at temperatures up to 100 degrees C. Int. J. Syst. Bacteriol. 46:1070-1077 ...
ID AEPER1_1_PE483 STANDARD; PRT; 370 AA. AC AEPER1_1_PE483; Q9YE84; DT 00-JAN-0000 (Rel. 1, Created) DT 00-JAN-0000 (Rel. 2, Last sequence update) DT 00-JAN-0000 (Rel. 3, Last annotation update) DE RecName: Full=Putative methylthioribose-1-phosphate isomerase; DE Short=M1Pi; Short=MTR-1-P isomerase; EC=5.3.1 23;AltName: Full=MTNA-like DE protein; Short=aMTNA;AltName: Full=S-methyl-5-thioribose-1-phosphate DE isomerase; (AEPER1_1.PE483). GN OrderedLocusNames=APE_0686; OS AEROPYRUM PERNIX K1. OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; OC Desulfurococcaceae; Aeropyrum. OX NCBI_TaxID=272557; RN [0] RP -.; RG -.; RL -.; CC -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS AEPER1_1.PE483. CC Aeropyrum pernix K1, complete genome. CC annotated by Ensembl Genomes CC -!- ANNOTATIONS ORIGIN:MTNA_AERPE CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1- CC phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P) CC (By similarity). CC -!- CATALYTIC ACTIVITY: ...
Proteome IDi ,p>The proteome identifier (UPID) is the unique identifier assigned to the set of proteins that constitute the ,a href=http://www.uniprot.org/manual/proteomes_manual>proteome,/a>. It consists of the characters UP followed by 9 digits, is stable across releases and can therefore be used to cite a UniProt proteome.,p>,a href=/help/proteome_id target=_top>More...,/a>,/p> ...
Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C/D sRNAs.
In publishing the research results obtained by use of the BIOLOGICAL RESOURCE, the USER is expected to cite the literature specified by the DEPOSITOR ...
Affiliation:国立研究開発法人産業技術総合研究所,その他部局等,研究員, Research Field:Applied molecular and cellular biology,Applied materials science/Crystal engineering,Digestive surgery,Functional biochemistry,Laboratory medicine, Keywords:糖鎖,NMR,糖認識ドメイン,レクチン,蛋白質,Aeropyrum pernix K1,進化,Aminoacyl-tRNA synthetase,肝線維化,バイオマーカー, # of Research Projects:7, # of Research Products:27, Ongoing Project:動脈硬化性大動脈瘤の網羅的糖鎖解析による新たな疾患関連指標の探索
Biological membranes, defining the boundary of cells and eukaryotic organelles, are mainly composed of lipids and membrane proteins. Interactions between these lipids and proteins are needed to preserve the tight seal of the membrane, but also to induce structure for proper function in many membrane proteins. In this thesis, interactions between three different kinds of peptides, i.e. small proteins, and model membranes are studied by spectroscopic methods.. First, the membrane interaction of two paddle domains, KvAPp, from the voltage-gated potassium channel KvAP from Aeropyrum pernix, and HsapBKp, from the human, large conductance, calcium-activated potassium channel HsapBK, was studied (paper I and II). In paper I, a high-resolution solution NMR structure of HsapBKp in detergent micelles is presented revealing a helix-turn-helix motif. Small structural differences between HsapBKp and KvAPp, positioning the arginines differently, are presented. These structural differences may explain why BK ...
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The virions of members of the Guttaviridae have an ovoid shape, measuring 55 x 75 nm (for Aeropyrum pernix ovoid virus 1 (APOV1), Betaguttavirus) to 80 x 130 nm (for Sulfolobus newzealandicus droplet-shaped virus (SNDV), Alphaguttavirus), when analysed by cryo-electron microscopy [{Arnold et al., 2000:10873785RJOHTXArnold et al., 2000, SNDV, a novel virus of the extremely thermophilic and acidophilic archaeon Sulfolobus, Virology, 272, 2, 409-16RJOMREFMochizuki et al., 2011:21784945RJOHTXMochizuki et al., 2011, Provirus induction in hyperthermophilic archaea: characterization of Aeropyrum pernix spindle-shaped virus 1 and Aeropyrum pernix ovoid virus 1, J Bacteriol, 193, 19, 5412-9}]. The virion surface is covered by globular subunits, which are ~3.5 nm in width. In negative-contrast electron micrographs, the virions are slightly pleomorphic, most displaying a droplet-like shape. Virions of SNDV are decorated with dense filaments attached to the pointed end of the virion; such appendages were ...
Archaeal viruses have evolved to infect hosts often thriving in extreme conditions such as high temperatures. However, there is a paucity of information on archaeal virion structures, genome packaging, and determinants of temperature resistance. The rod-shaped virus APBV1 (Aeropyrum pernix bacilliform virus 1) is among the most thermostable viruses known; it infects a hyperthermophile Aeropyrum pernix, which grows optimally at 90 °C. Here we report the structure of APBV1, determined by cryo-electron microscopy at near-atomic resolution. Tight packing of the major virion glycoprotein (VP1) is ensured by extended hydrophobic interfaces, and likely contributes to the extreme thermostability of the helical capsid. The double-stranded DNA is tightly packed in the capsid as a left-handed superhelix and held in place by the interactions with positively charged residues of VP1. The assembly is closed by specific capping structures at either end, which we propose to play a role in DNA packing and delivery.
Archaeal viruses have evolved to infect hosts often thriving in extreme conditions such as high temperatures. However, there is a paucity of information on archaeal virion structures, genome packaging, and determinants of temperature resistance. The rod-shaped virus APBV1 (Aeropyrum pernix bacilliform virus 1) is among the most thermostable viruses known; it infects a hyperthermophile Aeropyrum pernix, which grows optimally at 90 °C. Here we report the structure of APBV1, determined by cryo-electron microscopy at near-atomic resolution. Tight packing of the major virion glycoprotein (VP1) is ensured by extended hydrophobic interfaces, and likely contributes to the extreme thermostability of the helical capsid. The double-stranded DNA is tightly packed in the capsid as a left-handed superhelix and held in place by the interactions with positively charged residues of VP1. The assembly is closed by specific capping structures at either end, which we propose to play a role in DNA packing and delivery.
fig 3 conservation of glutamate switch in AAA+ proteins. (a) Sequence alignments of selected members of each clade for which the crystal structures are known. The color scheme follows that used in Figure 4. RFCs, replication factor C small subunit from Archaeoglobus fulgidus; Orc1, Orc1 protein from Aeropyrum pernix; p97D1, p97 D1 AAA+ domain from Mus musculus; SV40, SV40 large T antigen; PspF, PspF from Escherichia coli; HslU, HslU from E. coli; RuvBL1, RuvB-like 1 (TIP49a, Pontin) from Homo sapiens. (b) Plot of side chain torsion angles for 50 active site glutamate (DExx box) residues from AAA+ protein structures in the Protein Data Bank (http://www.rcsb.org/) with a resolution better than 3.5 Å. Only one copy from the asymmetric unit was used if angles were similar, to reduce redundancy. The appropriate glutamate residue was selected from individual PDB files and the side chain torsion angles were calculated using the CCP4 program ANGLES40, then normalized to 0-360° for display. The values ...
MORRISTOWN, N.J., May 09, 2016-- Pernix Therapeutics Holdings, Inc., a specialty pharmaceutical company, today announced that on May 6, 2016, the Patent Trial and Appeal Board of the United States Patent and Trademark Office denied a petition for inter partes review filed by Graybar Pharmaceuticals, LLC against Pozen, Inc. This petition, which was filed on November...
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Staphylothermus marinus is a marine organism that was isolated from hydrothermal sediment off the the coast of Vulcano Island in Italy. It can also be found from black smokers on the ocean floor. In a rich medium, Staphylothermus marinus grows in an optimum temperature of 92 degrees Celsius, but when nutrients are sparce, the optimum temperature drops to 85 degrees Celsius. For growth in a lab, a complex nutrient source is needed for optimum growth. The morphology of the Staphylothermus marinus can differ depending on the nutrients available. When nutrients are plentiful, Staphylothermus marinus grow as giant cells in a slightly irregular coccus shape with diameters up to 15 mm. Low nutrient concentrations produce little cells with diameters ranging from 0.5 to 1.0 mm. Up to 100 of these cells can cluster together to form grape-like groups. S. marinus is related to Aeropyrum pernix, Hyperthermus butylicus, and Ignicoccus hospitalis. (5) Describe the appearance, habitat, etc. of the organism, ...
BrunchClust produces 7 clusters: two complete for ATP-A and ATP-B and one incomplete for ATP-F. ATP-A and ATP-B clusters contain paralogs that are also reported as a result of clustering. There are two paralogs on the ATP-A branch one is of Rhodopirellula baltica and the second is of Methanosarcina acetivorans, and there are three paralogs on the ATP-B branch: two are from the same species as those on the ATP-A branch, i.e. Rhodopirellula baltica and Methanosarcina acetivoran, and the third is from Chlorobium tepidum. List of 30 taxa: 16 Bacteria: Aquifex aeolicus, Bacillus subtilis, Chlorobium tepidum, Corynebacterium glutamicum, Deinococcus radiodurans, Geobacillus kaustophilus, Geobacter sulfurreducens, Gloeobacter violaceus, Nostoc sp., Pseudomonas aeruginosa, Rhodopirellula baltica, Rhodopseudomonas palustris, Streptococcus thermophilus, Streptomyces coelicolor, Thermotoga maritime, Thermus thermophilus, and 14 Archaea: Aeropyrum pernix,Archaeoglobus fulgidus,Haloarcula marismortui, ...
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1BTZ: Episelection: novel Ki approximately nanomolar inhibitors of serine proteases selected by binding or chemistry on an enzyme surface.
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Acylpeptide hydrolase catalyzes the removal of the terminal blocking group together with the first amino acid residue of a peptide substrate: Acyl - AA1 - AA2 - AA3… AAn → Acyl - AA1 + AA2 - AA3… AAn...
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