Zobrazeno 1 - 10
of 258
pro vyhledávání: '"MESH: Substrate Specificity"'
Autor:
Marcele P. Martins, Mariana A. B. Morais, Gabriela F. Persinoti, Rafael H. Galinari, Li Yu, Yoshihisa Yoshimi, Fernanda B. Passos Nunes, Tatiani B. Lima, Shayla F. Barbieri, Joana L. M. Silveira, Vincent Lombard, Nicolas Terrapon, Paul Dupree, Bernard Henrissat, Mário T. Murakami
Publikováno v:
Martins, M P, Morais, M A B, Persinoti, G F, Galinari, R H, Yu, L, Yoshimi, Y, Passos Nunes, F B, Lima, T B, Barbieri, S F, Silveira, J L M, Lombard, V, Terrapon, N, Dupree, P, Henrissat, B & Murakami, M T 2022, ' Glycoside hydrolase subfamily GH5_57 features a highly redesigned catalytic interface to process complex hetero-β-mannans ', Acta Crystallographica Section D: Biological Crystallography, vol. 78, no. 11, pp. 1358-1372 . https://doi.org/10.1107/S2059798322009561
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2022, 78 (11), pp.1358-1372. ⟨10.1107/S2059798322009561⟩
Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2022, 78 (11), pp.1358-1372. ⟨10.1107/S2059798322009561⟩
International audience; Glycoside hydrolase family 5 (GH5) harbors diverse substrate specificities and modes of action, exhibiting notable molecular adaptations to cope with the stereochemical complexity imposed by glycosides and carbohydrates such a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffb34d1fd43c9a2230e1d9ded097768a
https://orbit.dtu.dk/en/publications/b865f68e-b3c0-4417-8051-6100ce204459
https://orbit.dtu.dk/en/publications/b865f68e-b3c0-4417-8051-6100ce204459
Publikováno v:
Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2020, 48 (21), pp.12204-12218. ⟨10.1093/nar/gkaa986⟩
Nucleic Acids Research, 2020, 48 (21), pp.12204-12218. ⟨10.1093/nar/gkaa986⟩
Nucleic Acids Research, Oxford University Press, 2020, 48 (21), pp.12204-12218. ⟨10.1093/nar/gkaa986⟩
Nucleic Acids Research, 2020, 48 (21), pp.12204-12218. ⟨10.1093/nar/gkaa986⟩
Family D DNA polymerase (PolD) is the essential replicative DNA polymerase for duplication of most archaeal genomes. PolD contains a unique two-barrel catalytic core absent from all other DNA polymerase families but found in RNA polymerases (RNAPs).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85fbf1b87ad50a09fe8aa5c33da49784
https://hal-pasteur.archives-ouvertes.fr/pasteur-03086156/document
https://hal-pasteur.archives-ouvertes.fr/pasteur-03086156/document
Autor:
Pierre Khalfi, Valérie Thiers, Jean-Pierre Vartanian, Noémie Berry, Wenjuan Jiao, Vincent Caval, Rodolphe Suspène, Emmanuelle Pitré, Simon Wain-Hobson
Publikováno v:
BMC Genomics
BMC Genomics, BioMed Central, 2019, 20 (1), pp.858. ⟨10.1186/s12864-019-6216-x⟩
BMC Genomics, 2019, 20 (1), pp.858. ⟨10.1186/s12864-019-6216-x⟩
BMC Genomics, Vol 20, Iss 1, Pp 1-12 (2019)
BMC Genomics, BioMed Central, 2019, 20 (1), pp.858. ⟨10.1186/s12864-019-6216-x⟩
BMC Genomics, 2019, 20 (1), pp.858. ⟨10.1186/s12864-019-6216-x⟩
BMC Genomics, Vol 20, Iss 1, Pp 1-12 (2019)
BackgroundAPOBEC1 (A1) enzymes are cytidine deaminases involved in RNA editing. In addition to this activity, a few A1 enzymes have been shown to be active on single stranded DNA. As two human ssDNA cytidine deaminases APOBEC3A (A3A), APOBEC3B (A3B)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6f7d56105aea4dcdf3ee2f4f07cdc7ee
https://hal-pasteur.archives-ouvertes.fr/pasteur-02545764
https://hal-pasteur.archives-ouvertes.fr/pasteur-02545764
Publikováno v:
Journal of Structural Biology
Journal of Structural Biology, Elsevier, 2019, 206 (2), pp.216-224. ⟨10.1016/j.jsb.2019.03.006⟩
Journal of Structural Biology, 2019, 206 (2), pp.216-224. ⟨10.1016/j.jsb.2019.03.006⟩
Journal of Structural Biology, Elsevier, 2019, 206 (2), pp.216-224. ⟨10.1016/j.jsb.2019.03.006⟩
Journal of Structural Biology, 2019, 206 (2), pp.216-224. ⟨10.1016/j.jsb.2019.03.006⟩
International audience; The crystal structure of the conserved hypothetical protein Rv2991 from Mycobacterium tuberculosis has been solved by SAD using seleno-methionine substituted protein. The dimeric biological assembly and the sequence and fold c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::95951736931054fcdccd0f2e937f758c
https://hal-pasteur.archives-ouvertes.fr/pasteur-03095980
https://hal-pasteur.archives-ouvertes.fr/pasteur-03095980
Autor:
Emeline Richard, Véronique Roig-Zamboni, Hugues Lortat-Jacob, Firas Fadel, Jérôme Hénault, Adeline Goulet, Christine Le Narvor, Yves Bourne, David Bonnaffé, Vincent Delauzun, C. Debarnot, Yoan R. Monneau, Bernard Priem, Romain R. Vivès
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, 116 (14), pp.6760-6765. ⟨10.1073/pnas.1818333116⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, pp.201818333. ⟨10.1073/pnas.1818333116⟩
Proceedings of the National Academy of Sciences of the United States of America, 2019, 116 (14), pp.6760-6765. ⟨10.1073/pnas.1818333116⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, 116 (14), pp.6760-6765. ⟨10.1073/pnas.1818333116⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, pp.201818333. ⟨10.1073/pnas.1818333116⟩
Proceedings of the National Academy of Sciences of the United States of America, 2019, 116 (14), pp.6760-6765. ⟨10.1073/pnas.1818333116⟩
Heparan sulfate (HS) is a linear, complex polysaccharide that modulates the biological activities of proteins through binding sites made by a series of Golgi-localized enzymes. Of these, glucuronyl C5-epimerase (Glce) catalyzes C5-epimerization of th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f534dfa4e1c1196a83a65edeecbf515
https://hal-amu.archives-ouvertes.fr/hal-02339215/document
https://hal-amu.archives-ouvertes.fr/hal-02339215/document
Autor:
Amal Seffouh, Hugues Lortat-Jacob, Zahra el Oula Hassoun, Rana El Masri, Jean-Pierre Andrieu, Romain R. Vivès, Evelyne Gout, Olga Makshakova
Publikováno v:
Cellular and Molecular Life Sciences
Cellular and Molecular Life Sciences, Springer Verlag, 2019
Cellular and Molecular Life Sciences, 2019, 76 (9), pp.1807-1819. ⟨10.1007/s00018-019-03027-2⟩
Cellular and Molecular Life Sciences, Springer Verlag, 2019, 76 (9), pp.1807-1819. ⟨10.1007/s00018-019-03027-2⟩
Cellular and Molecular Life Sciences, Springer Verlag, 2019
Cellular and Molecular Life Sciences, 2019, 76 (9), pp.1807-1819. ⟨10.1007/s00018-019-03027-2⟩
Cellular and Molecular Life Sciences, Springer Verlag, 2019, 76 (9), pp.1807-1819. ⟨10.1007/s00018-019-03027-2⟩
International audience; Through their ability to edit 6-O-sulfation pattern of Heparan sulfate (HS) polysaccharides, Sulf extracellular endosulfatases have emerged as critical regulators of many biological processes, including tumor progression. Howe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dae15b122eecdbac9b061ca2c582b74d
https://hal.archives-ouvertes.fr/hal-02043605
https://hal.archives-ouvertes.fr/hal-02043605
Autor:
Roland Brosch, María Noel Alvarez, Mariana Piuri, Alessandro Cascioferro, Analía Lima, Rosario Durán, Paulo C. Carvalho, Estefanía Urdániz, María-Natalia Lisa, Ana Denicola, Marco Bellinzoni, Otto Pritsch, Federico Carrion, Magdalena Gil, Annemarie Wehenkel, Pedro M. Alzari, Carlos Batthyány, Bernardina Rivera, Jessica Rossello
Publikováno v:
Journal of Proteomics
Journal of Proteomics, Elsevier, 2019, 192, pp.321-333. ⟨10.1016/j.jprot.2018.09.013⟩
Journal of Proteomics, 2019, 192, pp.321-333. ⟨10.1016/j.jprot.2018.09.013⟩
Journal of Proteomics, Elsevier, 2019, 192, pp.321-333. ⟨10.1016/j.jprot.2018.09.013⟩
Journal of Proteomics, 2019, 192, pp.321-333. ⟨10.1016/j.jprot.2018.09.013⟩
International audience; PknG from Mycobacterium tuberculosis is a multidomain Serine/Threonine protein kinase that regulates bacterial metabolism as well as the pathogen's ability to survive inside the host by still uncertain mechanisms. To uncover P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48d6e591b08630f1c8a11067058c5008
https://hal-pasteur.archives-ouvertes.fr/pasteur-02046106
https://hal-pasteur.archives-ouvertes.fr/pasteur-02046106
Autor:
Estefanía Giannini, Lisandro H. Otero, Antonela Rocio Palacios, Magdalena A. Taracila, Pedro M. Alzari, Sebastián Klinke, Christopher R. Bethel, Maria F. Mojica, Robert A. Bonomo, Leticia I. Llarrull, Alejandro J. Vila
Publikováno v:
Repositorio U. El Bosque
Universidad El Bosque
instacron:Universidad El Bosque
Antimicrobial Agents and Chemotherapy
Antimicrobial Agents and Chemotherapy, American Society for Microbiology, 2019, 63 (1), ⟨10.1128/AAC.01754-18⟩
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Antimicrobial Agents and Chemotherapy, 2019, 63 (1), ⟨10.1128/AAC.01754-18⟩
Universidad El Bosque
instacron:Universidad El Bosque
Antimicrobial Agents and Chemotherapy
Antimicrobial Agents and Chemotherapy, American Society for Microbiology, 2019, 63 (1), ⟨10.1128/AAC.01754-18⟩
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Antimicrobial Agents and Chemotherapy, 2019, 63 (1), ⟨10.1128/AAC.01754-18⟩
Carbapenems are "last resort" β-lactam antibiotics used to treat serious and life-threatening health care-associated infections caused by multidrug-resistant Gram-negative bacteria. Unfortunately, the worldwide spread of genes coding for carbapenema
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07bd3a48e1f34836367d2f135f8ca8d6
Publikováno v:
Antiviral Research
Antiviral Research, Elsevier Masson, 2017, 140, pp.25-36. ⟨10.1016/j.antiviral.2016.12.021⟩
Antiviral Research, 2017, 140, pp.25-36. ⟨10.1016/j.antiviral.2016.12.021⟩
Antiviral Research, Elsevier Masson, 2017, 140, pp.25-36. 〈10.1016/j.antiviral.2016.12.021〉
Antiviral Research, Elsevier Masson, 2017, 140, pp.25-36. ⟨10.1016/j.antiviral.2016.12.021⟩
Antiviral Research, 2017, 140, pp.25-36. ⟨10.1016/j.antiviral.2016.12.021⟩
Antiviral Research, Elsevier Masson, 2017, 140, pp.25-36. 〈10.1016/j.antiviral.2016.12.021〉
International audience; In targeting the essential viral RNA-dependent RNA-polymerase (RdRp), nucleotide analogues play a major role in antiviral therapies. In the Flaviviridae family, the hepatitis C virus (HCV) can be eradicated from chronically in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58cfcf5ab5748c81f2f90aa5c23349cb
https://hal.archives-ouvertes.fr/hal-01802946
https://hal.archives-ouvertes.fr/hal-01802946
Publikováno v:
Journal of Antimicrobial Chemotherapy
Journal of Antimicrobial Chemotherapy, 2015, 71 (2), pp.395-402. ⟨10.1093/jac/dkv375⟩
Journal of Antimicrobial Chemotherapy, 2015, 71 (2), pp.395-402. ⟨10.1093/jac/dkv375⟩
International audience; ObjectivesWe previously described extended-spectrum oxacillinase OXA-145 from Pseudomonas aeruginosa, which differs from narrow-spectrum OXA-35 by loss of Leu-155. The deletion results in loss of benzylpenicillin hydrolysis an