Search Results - "Zavialov, Andrey"

Human adenosine deaminases ADA1 and ADA2 bind to different subsets of immune cells by Kaljas, Yuliia, Liu, Chengqian, Skaldin, Maksym, Wu, Chengxiang, Zhou, Qing, Lu, Yuanan, Aksentijevich, Ivona, Zavialov, Andrey V.

“…At sites of inflammation and tumor growth, the local concentration of extracellular adenosine rapidly increases and plays a role in controlling the immune…”
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Human adenosine deaminase 2 induces differentiation of monocytes into macrophages and stimulates proliferation of T helper cells and macrophages by Zavialov, Andrey V., Gracia, Eduard, Glaichenhaus, Nicolas, Franco, Rafael, Zavialov, Anton V., Lauvau, Grégoire

“…Discovery of the growth factor activity of ADA2. ADAs play a pivotal role in regulating the level of adenosine, a signaling molecule controlling a variety of…”
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Early-Onset Stroke and Vasculopathy Associated with Mutations in ADA2 by Zhou, Qing, Yang, Dan, Ombrello, Amanda K, Zavialov, Andrey V, Toro, Camilo, Zavialov, Anton V, Stone, Deborah L, Chae, Jae Jin, Rosenzweig, Sergio D, Bishop, Kevin, Barron, Karyl S, Kuehn, Hye Sun, Hoffmann, Patrycja, Negro, Alejandra, Tsai, Wanxia L, Cowen, Edward W, Pei, Wuhong, Milner, Joshua D, Silvin, Christopher, Heller, Theo, Chin, David T, Patronas, Nicholas J, Barber, John S, Lee, Chyi-Chia R, Wood, Geryl M, Ling, Alexander, Kelly, Susan J, Kleiner, David E, Mullikin, James C, Ganson, Nancy J, Kong, Heidi H, Hambleton, Sophie, Candotti, Fabio, Quezado, Martha M, Calvo, Katherine R, Alao, Hawwa, Barham, Beverly K, Jones, Anne, Meschia, James F, Worrall, Bradford B, Kasner, Scott E, Rich, Stephen S, Goldbach-Mansky, Raphaela, Abinun, Mario, Chalom, Elizabeth, Gotte, Alisa C, Punaro, Marilynn, Pascual, Virginia, Verbsky, James W, Torgerson, Troy R, Singer, Nora G, Gershon, Timothy R, Ozen, Seza, Karadag, Omer, Fleisher, Thomas A, Remmers, Elaine F, Burgess, Shawn M, Moir, Susan L, Gadina, Massimo, Sood, Raman, Hershfield, Michael S, Boehm, Manfred, Kastner, Daniel L, Aksentijevich, Ivona

“…Adenosine deaminase 2 (ADA2) is an enzyme involved in purine metabolism and a growth factor that influences the development of endothelial cells and…”
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Secreted Bacterial Adenosine Deaminase Is an Evolutionary Precursor of Adenosine Deaminase Growth Factor by Skaldin, Maksym, Tuittila, Minna, Zavialov, Andrey V, Zavialov, Anton V

“…Adenosine deaminases (ADAs) play a pivotal role in regulating the level of adenosine, an important signaling molecule that controls a variety of cellular…”
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Human ADA2 belongs to a new family of growth factors with adenosine deaminase activity by Zavialov, Andrey V, Engström, Ake

“…Two distinct isoenzymes of ADA (adenosine deaminase), ADA1 and ADA2, have been found in humans. Inherited mutations in ADA1 result in SCID (severe combined…”
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ELISA based assays to measure adenosine deaminases concentration in serum and saliva for the diagnosis of ADA2 deficiency and cancer by Luo, Wenwen, Dong, Liang, Chen, Fenghong, Lei, Wenbin, He, Liya, Zhou, Qing, Lamy, Thierry, Zavialov, Andrey V.

“…Adenosine deaminases (ADAs) are enzymes of purine metabolism converting adenosine to inosine. There are two types of ADAs in humans ADA1 and ADA2. While both…”
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Structural Basis for the Growth Factor Activity of Human Adenosine Deaminase ADA2 by Zavialov, Anton V., Yu, Xiaodi, Spillmann, Dorothe, Lauvau, Grégoire, Zavialov, Andrey V.

“…Two distinct adenosine deaminases, ADA1 and ADA2, are found in humans. ADA1 has an important role in lymphocyte function and inherited mutations in ADA1 result…”
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Dermatologic Features of ADA2 Deficiency in Cutaneous Polyarteritis Nodosa by Gonzalez Santiago, Tania M, Zavialov, Andrey, Saarela, Janna, Seppanen, Mikko, Reed, Ann M, Abraham, Roshini S, Gibson, Lawrence E

“…Mutations in the CERC1 gene associated with deficiency in the ADA2 protein (DADA2) have been implicated in the pathogenesis of cutaneous polyarteritis nodosa…”
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Adenosine deaminase 2 regulates the activation of the toll-like receptor 9 in response to nucleic acids by Dong, Liang, Luo, Wenwen, Maksym, Skaldin, Robson, Simon C., Zavialov, Andrey V.

“…Human cells contain two types of adenosine deaminases (ADA) each with unique properties: ADA1, which is present in all cells where it modulates intracellular…”
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The Bacterial Toxin RelE Displays Codon-Specific Cleavage of mRNAs in the Ribosomal A Site by Pedersen, Kim, Zavialov, Andrey V., Pavlov, Michael Yu, Elf, Johan, Gerdes, Kenn, Ehrenberg, Måns

“…The Escherichia coli relBE operon encodes a toxin-antitoxin pair, RelE-RelB. RelB can reverse inhibition of protein synthesis by RelE in vivo. We have found…”
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Application of ADA1 as a new marker enzyme in sandwich ELISA to study the effect of adenosine on activated monocytes by Liu, Chengqian, Skaldin, Maksym, Wu, Chengxiang, Lu, Yuanan, Zavialov, Andrey V.

“…Enzyme-linked immunosorbent assay (ELISA) is a valuable technique to detect antigens in biological fluids. Horse radish peroxidase (HRP) is one of the most…”
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Splitting of the Posttermination Ribosome into Subunits by the Concerted Action of RRF and EF-G by Zavialov, Andrey V., Hauryliuk, Vasili V., Ehrenberg, Måns

“…After peptide release by a class-1 release factor, the ribosomal subunits must be recycled back to initiation. We have demonstrated that the distance between a…”
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The Cryo-EM Structure of a Translation Initiation Complex from Escherichia coli by Allen, Gregory S., Zavialov, Andrey, Gursky, Richard, Ehrenberg, Måns, Frank, Joachim

“…The 70S ribosome and its complement of factors required for initiation of translation in E. coli were purified separately and reassembled in vitro with GDPNP,…”
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Peptidyl-tRNA Regulates the GTPase Activity of Translation Factors by Zavialov, Andrey V, Ehrenberg, Måns

“…Rapid protein synthesis in bacteria requires the G proteins IF2, EF-Tu, EF-G, and RF3. These factors catalyze all major steps of mRNA translation in a…”
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Specific Interaction between EF-G and RRF and Its Implication for GTP-Dependent Ribosome Splitting into Subunits by Gao, Ning, Zavialov, Andrey V., Ehrenberg, Måns, Frank, Joachim

“…After termination of protein synthesis, the bacterial ribosome is split into its 30S and 50S subunits by the action of ribosome recycling factor (RRF) and…”
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Structure of the Escherichia coli ribosomal termination complex with release factor 2 by van Heel, Marin, Klaholz, Bruno P, Pape, Tillmann, Zavialov, Andrey V, Myasnikov, Alexander G, Orlova, Elena V, Vestergaard, Bente, Ehrenberg, Måns

“…Termination of protein synthesis occurs when the messenger RNA presents a stop codon in the ribosomal aminoacyl (A) site. Class I release factor proteins (RF1…”
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Mechanism for the Disassembly of the Posttermination Complex Inferred from Cryo-EM Studies by Gao, Ning, Zavialov, Andrey V., Li, Wen, Sengupta, Jayati, Valle, Mikel, Gursky, Richard P., Ehrenberg, Måns, Frank, Joachim

“…Ribosome recycling, the disassembly of the posttermination complex after each round of protein synthesis, is an essential step in mRNA translation, but its…”
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A cryo-electron microscopic study of ribosome-bound termination factor RF2 by Frank, Joachim, Rawat, Urmila B. S, Zavialov, Andrey V, Sengupta, Jayati, Valle, Mikel, Grassucci, Robert A, Linde, Jamie, Vestergaard, Bente, Ehrenberg, Måns

“…Protein synthesis takes place on the ribosome, where genetic information carried by messenger RNA is translated into a sequence of amino acids. This process is…”
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RF3 Induces Ribosomal Conformational Changes Responsible for Dissociation of Class I Release Factors by Gao, Haixiao, Zhou, Zhihong, Rawat, Urmila, Huang, Chenhui, Bouakaz, Lamine, Wang, Chernhoe, Cheng, Zhihong, Liu, Yuying, Zavialov, Andrey, Gursky, Richard, Sanyal, Suparna, Ehrenberg, Måns, Frank, Joachim, Song, Haiwei

“…During translation termination, class II release factor RF3 binds to the ribosome to promote rapid dissociation of a class I release factor (RF) in a…”
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Class-1 release factor eRF1 promotes GTP binding by class-2 release factor eRF3 by Hauryliuk, Vasili, Zavialov, Andrey, Kisselev, Lev, Ehrenberg, Måns

“…In eukaryotes, termination of mRNA translation is triggered by the essential polypeptide chain release factors eRF1, recognizing all three stop codons, and…”
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