Search Results - (Author, Cooperation:A. L. Osterman)
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1Latest Papers from Table of Contents or Articles in PressL. V. Blanton ; M. R. Charbonneau ; T. Salih ; M. J. Barratt ; S. Venkatesh ; O. Ilkaveya ; S. Subramanian ; M. J. Manary ; I. Trehan ; J. M. Jorgensen ; Y. M. Fan ; B. Henrissat ; S. A. Leyn ; D. A. Rodionov ; A. L. Osterman ; K. M. Maleta ; C. B. Newgard ; P. Ashorn ; K. G. Dewey ; J. I. Gordon
American Association for the Advancement of Science (AAAS)
Published 2016Staff ViewPublication Date: 2016-02-26Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Bacteria/*classification ; Bifidobacterium/physiology ; Body Weight ; Bone Development ; Clostridiales/physiology ; Disease Models, Animal ; Feces/microbiology ; Femur/growth & development ; Gastrointestinal Microbiome/*physiology ; Germ-Free Life ; Humans ; Infant ; Infant Nutrition Disorders/metabolism/*microbiology ; Malawi ; Male ; Mice ; Mice, Inbred C57BLPublished by: -
2Latest Papers from Table of Contents or Articles in PressM. Wu ; N. P. McNulty ; D. A. Rodionov ; M. S. Khoroshkin ; N. W. Griffin ; J. Cheng ; P. Latreille ; R. A. Kerstetter ; N. Terrapon ; B. Henrissat ; A. L. Osterman ; J. I. Gordon
American Association for the Advancement of Science (AAAS)
Published 2015Staff ViewPublication Date: 2015-10-03Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Bacteroides/*genetics/*metabolism ; DNA Transposable Elements/*genetics ; *Diet ; Gastrointestinal Tract/*microbiology ; Gene Library ; Genetic Fitness/*genetics ; Genetic Loci ; Genetic Markers ; Germ-Free Life ; Humans ; Mice ; Mutagenesis, Insertional/*methods ; Prebiotics ; Sequence Analysis, DNA/*methods ; Xylans/metabolismPublished by: -
3Latest Papers from Table of Contents or Articles in PressS. I. Yoon ; O. Kurnasov ; V. Natarajan ; M. Hong ; A. V. Gudkov ; A. L. Osterman ; I. A. Wilson
American Association for the Advancement of Science (AAAS)
Published 2012Staff ViewPublication Date: 2012-02-22Publisher: American Association for the Advancement of Science (AAAS)Print ISSN: 0036-8075Electronic ISSN: 1095-9203Topics: BiologyChemistry and PharmacologyComputer ScienceMedicineNatural Sciences in GeneralPhysicsKeywords: Animals ; Crystallography, X-Ray ; Dimerization ; Flagellin/*chemistry/metabolism ; Models, Molecular ; Mutagenesis ; Protein Conformation ; Salmonella enterica ; *Signal Transduction ; Structure-Activity Relationship ; Toll-Like Receptor 5/*chemistry/genetics/metabolism ; Zebrafish ; Zebrafish Proteins/*chemistry/genetics/metabolismPublished by: -
4Articles: DFG German National LicensesChestukhina, G. G. ; Tyurin, S. A. ; Kostina, L. I. ; Osterman, A. L. ; Zalunin, I. A. ; Khodova, O. A. ; Stepanov, V. M.
Springer
Published 1990Staff ViewISSN: 1573-4943Keywords: Bacillus thuringiensis, δ-endotoxins ; limited proteolysisSource: Springer Online Journal Archives 1860-2000Topics: Chemistry and PharmacologyNotes: Abstract N-Terminal domain (65 kD) of δ-endotoxin produced byBacillus thuringiensis ssp.alesti, as shown by limited proteolysis, consists of two subdomains of molecular mass 30 and 33 kD that correspond, respectively, to conservative and variable regions of the δ-endotoxin primary structure. Furthermore, proteolysis of these subdomains leads to their conversion into at least two fragments of molecular mass 10 kD stable to proteinase action. Such a pattern of molecular organization appears to be common for several structurally related δ-endotoxins that belong to thekurstaki group. Entomicidal protein produced by ssp.israelensis (70 kD), which differs strongly fromalesti and otherkurstaki group δ-endotoxins, retains a similar type of molecular organization and consists of two subdomains with molecular mass of ∼35 kD. Apparently, the characteristic pattern of the δ-endotoxins' molecular structure reflects separation of functions (e.g., host recognition and toxicityper se) between domains and subdomains of these proteins.Type of Medium: Electronic ResourceURL: -
5Articles: DFG German National LicensesOsterman, A. L. ; Grishin, N. V. ; Smulevitch, S. V. ; Matz, M. V. ; Zagnitko, O. P. ; Revina, L. P. ; Stepanov, V. M.
Springer
Published 1992Staff ViewISSN: 1573-4943Keywords: Primary structure ; carboxypeptidase T ; carboxypeptidase family ; alignmentSource: Springer Online Journal Archives 1860-2000Topics: Chemistry and PharmacologyNotes: Abstract The primary structure of carobxypeptidase T—a Zn-dependent extracellular enzyme ofThermoactinomyces vulgaris—was determined from the clonedcpT gene nucleotide sequence and compared to Zn-carboxypeptidases from various organisms. The compilation and analysis of multiple alignment accompanied by consideration of available tertiary structure data have shown that in the overall spatial structure and active site arrangement CpT is similar to other enzymes constituting the Zn-carboxypeptidase family. Nine of 16 amino acid residues found to be strictly invariant are presumably located close to the active site. The preservation of His69, Glu72, Asn144, Arg145, His196, Tyr248, and Glu270 identified previously as essential catalytic site participants implicates basically the same catalytic mechanism in the Zn-carboxy-peptidase family. It is proposed that Pro205 and Asp256 should play an important role in proper S1′-pocket spatial arrangement. The comparative analysis of amino acid variations in S1′-pocket enabled us to reveal structural determinants of the Zn-carboxypeptidase primary specificity. The relatively reduced size of the pocket and negative charge of Asp253 are supposed to contribute correspondingly to A- and B-type substrate preferences of carboxypeptidase T endowed with dual primary specificity.Type of Medium: Electronic ResourceURL: