Výsledky vyhledávání - "MESH: Enzyme Stability"

Biochemical and structural studies of two tetrameric nucleoside 2′-deoxyribosyltransferases from psychrophilic and mesophilic bacteria: Insights into cold-adaptation

Autor: Javier Acosta, Jesús Fernández-Lucas, Miguel Arroyo, Pierre Alexandre Kaminski, Iván Acebrón, Andrzej Joachimiak, José M. Mancheño, Boguslaw Nocek, Isabel de la Mata, Yohana Alfaro, Ruiying Y. Wu

Publikováno v: Digital.CSIC. Repositorio Institucional del CSIC
instname
REDICUC-Repositorio CUC
Corporación Universidad de la Costa
instacron:Corporación Universidad de la Costa
E-Prints Complutense. Archivo Institucional de la UCM
'International Journal of Biological Macromolecules ', vol: 192, pages: 138-150 (2021)
International Journal of Biological Macromolecules
International Journal of Biological Macromolecules, 2021, 192, pp.138-150. ⟨10.1016/j.ijbiomac.2021.09.164⟩

13 págs., 6 figs., 3 tabs.
Nucleoside 2′-deoxyribosyltransferases (NDTs) catalyze the cleavage of glycosidic bonds of 2′-deoxynucleosides and the following transfer of the 2′-deoxyribose moiety to acceptor nucleobases. Here, we report the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c52d9c7633a2cfed4df23ffe3deeb5e2
http://hdl.handle.net/10261/255525

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Secretory lipase from the human pathogen Leishmania major: Heterologous expression in the yeast Pichia pastoris and biochemical characterization

Autor: Madiha Bou Ali, Youssef Gargouri, Saoussen Ben Ayed, Aymen Bali, Yassine Ben Ali, Dhafer Laouini

Publikováno v: Biochimie
Biochimie, Elsevier, 2018, 146, pp.119--126. ⟨10.1016/j.biochi.2017.12.002⟩

International audience; Leishmaniasis is a parasitic reticuloendotheliosis whose pathogen is a zooflagellate belonging to the genus Leishmania transmitted by the bite of an infected phlebotome. Recently, a unique secretory lipase from the human patho

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e746040dc0853d4dd4b53b5f22d4d85e
https://hal.archives-ouvertes.fr/hal-01876258

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Activation of a Unique Flavin-Dependent tRNA-Methylating Agent

Autor: Eduardo M. Bruch, Marc Fontecave, Martin J. Field, Sun Un, Djemel Hamdane

Publikováno v: Biochemistry
Biochemistry, American Chemical Society, 2013, 52 (49), pp.8949-8956. 〈10.1021/bi4013879〉
Biochemistry, American Chemical Society, 2013, 52 (49), pp.8949-8956. ⟨10.1021/bi4013879⟩
Biochemistry, 2013, 52 (49), pp.8949-8956. ⟨10.1021/bi4013879⟩

International audience; TrmFO is a tRNA methyltransferase that uses methylenetetrahydrofolate (CH2THF) and flavin adenine dinucleotide hydroquinone as cofactors. We have recently shown that TrmFO from Bacillus subtilis stabilizes a TrmFO-CH2-FADH add

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::569c75d096d6fc0e4062c0c8b37545a7
https://doi.org/10.1021/bi4013879

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Sampling the Conformational Energy Landscape of a Hyperthermophilic Protein by Engineering Key Substitutions

Autor: Martin J. Field, Alexey Aleksandrov, Nicolas Coquelle, Dominique Madern, Elena Mendoza-Barberá, Sonia Mraihi, Jacques-Philippe Colletier

Publikováno v: Molecular Biology and Evolution
Molecular Biology and Evolution, Oxford University Press (OUP), 2012, 29 (6), pp.1683-94. ⟨10.1093/molbev/mss015⟩
Molecular Biology and Evolution, 2012, 29 (6), pp.1683-94. ⟨10.1093/molbev/mss015⟩

International audience; Proteins exist as a dynamic ensemble of interconverting substates, which defines their conformational energy landscapes. Recent work has indicated that mutations that shift the balance between conformational substates (CSs) ar

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cad6f4acec81c3293db17169f4ea99a
https://doi.org/10.1093/molbev/mss015

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The Glycine-Rich Motif of Pyrococcus abyssi DNA Polymerase D Is Critical for Protein Stability

Autor: Benoît Castrec, Jean-Paul Raffin, Ghislaine Henneke, Sébastien Laurent, Didier Flament

Publikováno v: Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2010, 396 (4), pp.840-848. ⟨10.1016/j.jmb.2010.01.006⟩
Journal Of Molecular Biology (0022-2836) (Academic Press Ltd-Elsevier Science Ltd), 2010-03, Vol. 396, N. 4, P. 840-848

En libre-accès sur Archimer : http://archimer.ifremer.fr/doc/00002/11293/7879.pdf; International audience; A glycine-rich motif described as being involved in human polymerase delta proliferating cell nuclear antigen (PCNA) binding has also been ide

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41fae5d9b3810b0dd8c43b0475c7f630
https://doi.org/10.1016/j.jmb.2010.01.006

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Catalytic Activity and Inhibition of Wegener Antigen Proteinase 3 on the Cell Surface of Human Polymorphonuclear Neutrophils

Autor: Francis Gauthier, Alexandre Gauthier, Sylvie Attucci, Brice Korkmaz, Marie-Lise Jourdan, Jérôme Jaillet

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (30), pp.19896-902. ⟨10.1074/jbc.M901471200⟩
Journal of Biological Chemistry, 2009, 284 (30), pp.19896-902. ⟨10.1074/jbc.M901471200⟩

International audience; Proteinase 3 (Pr3), the main target of anti-neutrophil cytoplasmic antibodies, is a neutrophil serine protease that may be constitutively expressed at the surface of quiescent circulating neutrophils. This raises the question

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::28df0fc88dc7383465dafea959bc4ed3
https://doi.org/10.1074/jbc.m901471200

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Interaction of human 3-phosphoglycerate kinase with l-ADP, the mirror image of d-ADP

Autor: Beáta Flachner, Tom Barman, Christian Périgaud, Andrea Varga, Béatrice Roy, Judit Szabó, Corinne Lionne, Peter V. Konarev, Mária Vas, Péter Závodszky, Dmitri I. Svergun

Publikováno v: Biochemical and Biophysical Research Communications
Biochemical and Biophysical Research Communications, Elsevier, 2008, 366 (4), pp.994-1000. ⟨10.1016/j.bbrc.2007.12.061⟩

International audience; l-Nucleoside-analogues, mirror images of the natural d-nucleosides, are a new class of antiviral and anticancer agents. In the cell they have to be phosphorylated to pharmacologically active triphosphate forms, the last step s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71677d849278452e68c0b53bc53185a3
https://doi.org/10.1016/j.bbrc.2007.12.061

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Molecular Dynamics Simulations Show That Bound Mg2+ Contributes to Amino Acid and Aminoacyl Adenylate Binding Specificity in Aspartyl-tRNA Synthetase through Long Range Electrostatic Interactions

Autor: Thomas Simonson, Damien Thompson

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2006, 281 (33), pp.23792-803. ⟨10.1074/jbc.M602870200⟩

International audience; Molecular recognition between the aminoacyl-tRNA synthetase enzymes and their cognate amino acid ligands is essential for the faithful translation of the genetic code. In aspartyl-tRNA synthetase (AspRS), the co-substrate ATP

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::025006c959f245fba03a60a27447857d
https://doi.org/10.1074/jbc.m602870200

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Structural and Functional Characterization of the TgDRE Multidomain Protein, a DNA Repair Enzyme from Toxoplasma gondii

Autor: Stanislas Tomavo, Karine Wecker, Isabelle Callebaut, Nicolas Wolff, Muriel Delepierre, Ada Prochnicka-Chalufour, Najoua Dendouga, Karine Frénal, Sophie Zinn-Justin

Publikováno v: Biochemistry
Biochemistry, 2006, 45 (15), pp.4867-74. ⟨10.1021/bi051948e⟩
Biochemistry, American Chemical Society, 2006, 45 (15), pp.4867-74. ⟨10.1021/bi051948e⟩

The parasite Toxoplasma gondii expresses a 55 kDa protein or TgDRE that belongs to a novel family of proteins characterized by the presence of three domains, a human splicing factor 45-like motif (SF), a glycine-rich motif (G-patch), and a RNA recogn

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d35d2ce451644e57f6512aa934aacef7
https://doi.org/10.1021/bi051948e

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Mutations of acetylcholinesterase which confer insecticide resistance in insect populations

Autor: Didier Fournier

Publikováno v: Chemico-Biological Interactions
Chemico-Biological Interactions, Elsevier, 2005, 157-158, pp.257-261
Chemico-Biological Interactions, Elsevier, 2005, 157-158, pp.257-61. ⟨10.1016/j.cbi.2005.10.040⟩

Resistance-modified acetylcholinesterases have been described in many insect species and sequencing of their genes has allowed several point mutations to be described. Most mutations line the active site gorge. Each mutation provides a specific resis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1665fb199b911f5de0be770f562f7729
https://doi.org/10.1016/j.cbi.2005.10.040

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