Zobrazeno 1 - 10
of 192
pro vyhledávání: '"G, Obmolova"'
Autor:
Mandy Jongeneelen, Maria P. Limberis, M. van der Neut Kolfschoten, A. van Eijgen, Ryan M. B. Hoffman, Nick S. Laursen, David Zuijdgeest, Steffen M. Bernard, Leo L.M. Poon, Ian A. Wilson, Jesper Pallesen, Hannah L. Turner, J. Luo, Sven Blokland, H. van Diepen, R. Straetemans, G. Obmolova, J.A. Kolkman, Jan Vermond, James M. Wilson, Travis Nieusma, Anna Tretiakova, Robert H. E. Friesen, Xueyong Zhu, Chan Tang, Ronald Vogels, Boerries Brandenburg, Andrew B. Ward
Publikováno v:
Science (New York, N.Y.). 362(6414)
Durable influenza protection Vaccines are indispensable for the control and prevention of influenza, but there are several challenges to efficacy. Some individuals respond poorly to vaccination, and virus variation makes targeting optimal antigens di
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ba4d62a5d4bf4454df09a6c0a7d6843
https://pubmed.ncbi.nlm.nih.gov/30573785
https://pubmed.ncbi.nlm.nih.gov/30573785
Autor:
Anastassis Perrakis, George S. Brush, Paula Sebastiao, Keith S. Wilson, G. Obmolova, Alexei Teplyakov, Maurice J. Bessman
Publikováno v:
The EMBO Journal. 15:3487-3497
NMP kinases catalyse the phosphorylation of the canonical nucleotides to the corresponding diphosphates using ATP as a phosphate donor. Bacteriophage T4 deoxynucleotide kinase (DNK) is the only member of this family of enzymes that recognizes three s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f355c36fbcaf5bc98e59f2a5042e3cb8
https://doi.org/10.1002/j.1460-2075.1996.tb00717.x
https://doi.org/10.1002/j.1460-2075.1996.tb00717.x
Autor:
F.J.T. van der Bolt, Andrea Mattevi, W.G.J. Hol, G. Obmolova, H. A. Schreuder, Kor H. Kalk, W.J.H. van Berkel
Publikováno v:
Scopus-Elsevier
The crystal structures of wild-type p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens, complexed with the substrate analogues 4-aminobenzoate, 2,4-dihydroxybenzoate, and 2-hydroxy-4-aminobenzoate have been determined at 2.3-, 2.5-, and 2.8-A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b8f979a4e7368bdabbfb93042295db36
https://doi.org/10.1021/bi00199a044
https://doi.org/10.1021/bi00199a044
Publikováno v:
Journal of Molecular Biology. 230:1200-1215
The structure of Pseudomonas fluorescens lipoamide dehydrogenase, a dimeric flavoenzyme with a molecular mass of 106,000 daltons, was solved by the molecular replacement method and refined to an R-factor of 19·4% at 2·8 A resolution. The root-mean-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::057ad424f6816b1f9cf26fbf2acd696a
https://doi.org/10.1006/jmbi.1993.1236
https://doi.org/10.1006/jmbi.1993.1236
Publikováno v:
European Journal of Biochemistry. 213:737-741
The three-dimensional structure of apo-neocarzinostatin, an antitumour antibiotic protein isolated from Streptomyces carzinostaticus, has been determined by X-ray diffraction at 0.15-nm resolution and refined to R = 17.2%. The crystal structure of ne
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a4686b6ffcc83fb74b2ea24e45f97ea
https://doi.org/10.1111/j.1432-1033.1993.tb17814.x
https://doi.org/10.1111/j.1432-1033.1993.tb17814.x
Publikováno v:
Journal of Molecular Biology. 230:1183-1199
Dihydrolipoyl transacetylase (E2p) is both structurally and functionally the central enzyme of the pyruvate dehydrogenase multienzyme complex. The crystal structure of the catalytic domain, i.e. residues 382 to 637, of Azotobacter vinelandii E2p (E2p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cde98263442290778f54f1780d1a475f
https://doi.org/10.1006/jmbi.1993.1235
https://doi.org/10.1006/jmbi.1993.1235
Publikováno v:
ChemInform. 33
Covering: up to June 2001This review summarizes the state of knowledge on D-glucosamine-6P synthesis catalyzed by glucosamine-6P synthase. The mechanisms of L-glutamine hydrolysis, ammonia transfer and fructose-6P conversion into D-glucosamine-6P are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::53fb6169240867c2b47cfb7e3b2442b0
https://doi.org/10.1002/chin.200218290
https://doi.org/10.1002/chin.200218290
Autor:
Michael Matz, Kostya Polyakov, Sergei Smulevitch, Olga V. Galperina, Andrei L. Osterman, Olga Zagnitko, Valentin M. Stepanov, Nikolai V. Grishin, B. V. Strokopytov, G. Obmolova, Alexei Teplyakov, Inna P. Kuranova
Publikováno v:
European Journal of Biochemistry. 208:281-288
The crystal structure of carboxypeptidase T from Thermoactinomyces vulgaris has been determined at 0.235-nm resolution by X-ray diffraction. Carboxypeptidase T is a remote homologue of mammalian Zn-carboxypeptidases. In spite of the low degree of ami
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5beb7c2d4f72d1cf202557c4a348e8cd
https://doi.org/10.1111/j.1432-1033.1992.tb17184.x
https://doi.org/10.1111/j.1432-1033.1992.tb17184.x
Autor:
Wim G. J. Hol, A. de Kok, Adrie H. Westphal, E. Schulze, G. Obmolova, Kor H. Kalk, Andrea Mattevi
Publikováno v:
Science. 255:1544-1550
The highly symmetric pyruvate dehydrogenase multienzyme complexes have molecular masses ranging from 5 to 10 million daltons. They consist of numerous copies of three different enzymes: pyruvate dehydrogenase, dihydrolipoyl transacetylase, and lipoam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4cda9462c53682daceb4c3d397959f3c
https://doi.org/10.1126/science.1549782
https://doi.org/10.1126/science.1549782
Publikováno v:
European Journal of Biochemistry. 201:561-568
Partial sequences of the dihydrolipoyl transacetylase component (E2p) of the pyruvate dehydrogenase complex from Azotobacter vinelandii and Escherichia coli, containing the catalytic domain, were cloned in pUC plasmids and over-expressed in E. coli T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b785d8592d21acd5528360f2b0f5371
https://doi.org/10.1111/j.1432-1033.1991.tb16315.x
https://doi.org/10.1111/j.1432-1033.1991.tb16315.x