Academic literature on the topic 'Trimers or higher oligomers of RNase A'

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Journal articles on the topic "Trimers or higher oligomers of RNase A"

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LIBONATI, Massimo, and Giovanni GOTTE. "Oligomerization of bovine ribonuclease A: structural and functional features of its multimers." Biochemical Journal 380, no. 2 (2004): 311–27. http://dx.doi.org/10.1042/bj20031922.

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Bovine pancreatic RNase A (ribonuclease A) aggregates to form various types of catalytically active oligomers during lyophilization from aqueous acetic acid solutions. Each oligomeric species is present in at least two conformational isomers. The structures of two dimers and one of the two trimers have been solved, while plausible models have been proposed for the structures of a second trimer and two tetrameric conformers. In this review, these structures, as well as the general conditions for RNase A oligomerization, based on the well known 3D (three-dimensional) domain-swapping mechanism, a
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Wootton, Sarah K., and Dongwan Yoo. "Homo-Oligomerization of the Porcine Reproductive and Respiratory Syndrome Virus Nucleocapsid Protein and the Role of Disulfide Linkages." Journal of Virology 77, no. 8 (2003): 4546–57. http://dx.doi.org/10.1128/jvi.77.8.4546-4557.2003.

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ABSTRACT As a step toward understanding the assembly pathway of the porcine reproductive and respiratory syndrome virus (PRRSV), the oligomeric properties of the nucleocapsid (N) protein were investigated. In this study, we have demonstrated that under nonreducing conditions the N protein forms disulfide-linked homodimers. However, inclusion of an alkylating agent (N-ethylmaleimide [NEM]) prevented disulfide bond formation, suggesting that these intermolecular disulfide linkages were formed as a result of spurious oxidation during cell lysis. In contrast, N protein homodimers isolated from ext
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Kanbara, K., K. Nagai, H. Nakashima, N. Yamamoto, R. J. Suhadolnik, and H. Takaku. "The Relationship between Conformation and Biological Activity of 8-substituted Analogues of 2′,5′-Oligoadenylates." Antiviral Chemistry and Chemotherapy 5, no. 1 (1994): 1–5. http://dx.doi.org/10.1177/095632029400500101.

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Analogues of the 2′,5′-linked adenylate trimer 5′-monophosphates, p5′A2′p5′A2′p5′A (pA3) (1a), containing 8-hydroxyadenosine and 8-mercaptoadenosine in the first, second, and third nucleotide positions were tested for their ability to bind to and activate RNase L of mouse L cells. The oligomer, p5′ASH2′p5′ASH2′p5′ASH (pASH3) (1c) had little capacity to bind to RNase L. On the other hand, an analogue of the p5′AOH2′p5′AOH2′p5′AOH (pAOH3) (1b) bound almost as well as the parent 2-5A [pppA(2′p5′A)2] (P3A3) (1d) to RNase L. The 8-substituted analogues of 2-5A were more resistant to degradation by
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LIBONATI, Massimo, Mariarita BERTOLDI, and Salvatore SORRENTINO. "The activity on double-stranded RNA of aggregates of ribonuclease A higher than dimers increases as a function of the size of the aggregates." Biochemical Journal 318, no. 1 (1996): 287–90. http://dx.doi.org/10.1042/bj3180287.

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Stable bovine RNase A aggregates larger than dimers (identified as trimers, tetramers, pentamers and hexamers) were obtained by lyophilization of RNase A from 40–50% acetic acid solutions. The RNase activity of these aggregates was compared with that of monomeric RNase A on single- and double-stranded polyribonucleotides. Their activity toward poly(U) and yeast RNA slightly decreases as a function of the size of the aggregates. In contrast, their action on poly(A).poly(U) as substrate progressively increases from a relative activity of 1 for the RNase monomer to 10 for the hexamer. These resul
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Filipovic, Dragana, Marija Radojcic, and Bratoljub Milosavljevic. "Determination of the critical molar mass of ovalbumin oligomers degraded by ultrasound." Journal of the Serbian Chemical Society 65, no. 2 (2000): 123–30. http://dx.doi.org/10.2298/jsc0002123f.

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An experimental method has been developed which enables the determination of the critical molar mass (Mmc) of ovalbumin oligomers degraded by ultrasound of known frequency. To test the validity of the Mmc postulate, a series of ovalbumin oligomers was prepared by the radiolytic cross-linking of 1% solutions of ovalbumin monomer dissolved in 50mMNa/K-phosphate buffer pH 7.0 saturated withN2O. Under these conditions, irradiation with 5 kGy from a 60 Co source, yielded ovalbumin dimers, trimers, tetramers, and higher order oligomers. On the basis of the results obtained with the ovalbumin oligome
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Markovic, Ingrid, Helena Pulyaeva, Alexander Sokoloff, and Leonid V. Chernomordik. "Membrane Fusion Mediated by Baculovirus gp64 Involves Assembly of Stable gp64 Trimers into Multiprotein Aggregates." Journal of Cell Biology 143, no. 5 (1998): 1155–66. http://dx.doi.org/10.1083/jcb.143.5.1155.

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The baculovirus fusogenic activity depends on the low pH conformation of virally-encoded trimeric glycoprotein, gp64. We used two experimental approaches to investigate whether monomers, trimers, and/or higher order oligomers are functionally involved in gp64 fusion machine. First, dithiothreitol (DTT)- based reduction of intersubunit disulfides was found to reversibly inhibit fusion, as assayed by fluorescent probe redistribution between gp64-expressing and target cells (i.e., erythrocytes or Sf9 cells). This inhibition correlates with disappearance of gp64 trimers and appearance of dimers an
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Salveson, Patrick J., Ryan K. Spencer та James S. Nowick. "X-ray Crystallographic Structure of Oligomers Formed by a Toxic β-Hairpin Derived from α-Synuclein: Trimers and Higher-Order Oligomers". Journal of the American Chemical Society 138, № 13 (2016): 4458–67. http://dx.doi.org/10.1021/jacs.5b13261.

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Jorba, Núria, Estela Area, and Juan Ortín. "Oligomerization of the influenza virus polymerase complex in vivo." Journal of General Virology 89, no. 2 (2008): 520–24. http://dx.doi.org/10.1099/vir.0.83387-0.

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The influenza virus polymerase is a heterotrimer formed by the PB1, PB2 and PA subunits and is responsible for virus transcription and replication. We have expressed the virus polymerase complex by co-transfection of the subunit cDNAs, one of which was tandem affinity purification (TAP)-tagged, into human cells. The intracellular polymerase complexes were purified by the TAP approach, involving two affinity chromatography steps, IgG–Sepharose and calmodulin–agarose. Gel-filtration analysis indicated that, although most of the purified polymerase behaved as a heterotrimer, a significant proport
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Wojciechowska, Daria, Michał Taube, Karolina Rucińska, Joanna Maksim, and Maciej Kozak. "Oligomerization of Human Cystatin C—An Amyloidogenic Protein: An Analysis of Small Oligomeric Subspecies." International Journal of Molecular Sciences 23, no. 21 (2022): 13441. http://dx.doi.org/10.3390/ijms232113441.

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Human cystatin C (HCC), an amyloidogenic protein, forms dimers and higher oligomers (trimers, tetramers and donut like large oligomers) via a domain-swapping mechanism. The aim of this study was the characterization of the HCC oligomeric states observed within the pH range from 2.2 to 10.0 and also in conditions promoting oligomerization. The HCC oligomeric forms obtained in different conditions were characterized using size exclusion chromatography, dynamic light scattering and small-angle X-ray scattering. The marked ability of HCC to form tetramers at low pH (2.3 or 3.0) and dimers at pH 4.
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Ganderton, Tim, Jason W. H. Wong, Christina Schroeder, and Philip J. Hogg. "Lateral self-association of VWF involves the Cys2431-Cys2453 disulfide/dithiol in the C2 domain." Blood 118, no. 19 (2011): 5312–18. http://dx.doi.org/10.1182/blood-2011-06-360297.

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Abstract VWF is a plasma protein that binds platelets to an injured vascular wall during thrombosis. When exposed to the shear forces found in flowing blood, VWF molecules undergo lateral self-association that results in a meshwork of VWF fibers. Fiber formation has been shown to involve thiol/disulfide exchange between VWF molecules. A C-terminal fragment of VWF was expressed in mammalian cells and examined for unpaired cysteine thiols using tandem mass spectrometry (MS). The VWF C2 domain Cys2431-Cys2453 disulfide bond was shown to be reduced in approximately 75% of the molecules. Fragments
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Dissertations / Theses on the topic "Trimers or higher oligomers of RNase A"

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VOTTARIELLO, FRANCESCA. "OLIGOMERIZATION OF RNase A:a) A STUDY OF THE INFLUENCE OF SERINE 80 RESIDUE ON THE 3D DOMAIN SWAPPING MECHANISMb) “ZERO-LENGTH” DIMERS OF RNase A AND THEIR CATIONIZATION WITH PEI." Doctoral thesis, 2010. http://hdl.handle.net/11562/344075.

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"Zero-length" dimers of ribonuclease A, a novel type of dimers formed by two RNase A molecules bound to each other through a zero-length amide bond [Simons, B.L. et al. (2007) Proteins 66, 183-195], were analyzed, and tested for their possible in vitro cytotoxic activity. Results: (i) Besides dimers, also trimers and higher oligomers can be identified among the products of the covalently linking reaction. (ii) The "zero-length" dimers prepared by us appear not to be a unique species, as was instead reported by Simons et al. The product is heterogeneous, as shown by the involvement in the amide
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Book chapters on the topic "Trimers or higher oligomers of RNase A"

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Mark, James E., Dale W. Schaefer, and Gui Lin. "Preparation, Analysis, and Degradation." In The Polysiloxanes. Oxford University Press, 2015. http://dx.doi.org/10.1093/oso/9780195181739.003.0004.

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Elemental silicon on which the entire technology is based is typically obtained by reduction of the mineral silica with carbon at high temperatures: . . . SiO2 + 2C → Si 2CO (2.1) . . . The silicon is then converted directly to tetrachlorosilane by the reaction . . . Si + 2Cl2 → SiCl4 (2.2) . . Tetrachlorosilane can be used to form an organosilane by the Grignard Reaction . . . SiCl4 + 2 RMgX → R2SiCl2 + 2 MgClX (2.3). . . This relatively complicatreaction has been replaced by the so-called Direct Process or Rochow Process, which starts from elemental silicon as is illustrated by the reaction . . . Si + 2 RCl → R2SiCl2 (2.4) . . . This process also yields RSiCl3 and R3SiCl, which­­ can be removed by distillation. Compounds of formula R2SiCl2 are extremely important as intermediates to a variety of substances having both organic and inorganic character. Hydrolysis gives dihydroxy structures, which can condense to give the basic [–SiR2O–] repeat unit. The nature of the product obtained depends greatly on the reaction conditions. Basic catalysts and higher temperatures favor higher molecular weight linear polymers. Acidic catalysts tend to produce cyclic small molecules or low molecular weight polymers. The hydrolysis approach to polysiloxane synthesis has been largely replaced by ring-opening polymerization of organosilicon cyclic trimers and tetramers, with ionic initiation. These cyclic monomers are produced by the hydrolysis of dimethyldichlorosilane. Under the right conditions, at least 50 wt % of the products are cyclic oligomers. The desired cyclic species are separated from the mixture for use in ring-opening polymerizations such as those described in the following section. In addition, “click” chemistry has been developed for new synthesis techniques in general, and polymerizations in particular. These approaches have been used to prepare polysiloxane elastomers and polydimethylsiloxane (PDMS) copolymers that can function as thermoplastic elastomers. New synthetic strategies for structured silicones, based on B(C6F5)3 have also been developed. Another new approach involves enzymes, such as the lipase enzymatically catalyzed synthesis of silicone aromatic polyesters and silicone aromatic polyamides.
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