Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Julie Vandenameele"'
Autor:
Maximiliano Figueroa, Julie Vandenameele, Erik Goormaghtigh, Marie Valerio-Lepiniec, Philippe Minard, André Matagne, Cécile Van de Weerdt
Publikováno v:
Data in Brief, Vol 8, Iss , Pp 1221-1226 (2016)
The artificial protein Octarellin V.1 (http://dx.doi.org/10.1016/j.jsb.2016.05.004 [1]) was obtained through a direct evolution process over the de novo designed Octarellin V (http://dx.doi.org/10.1016/S0022-2836(02)01206-8 [2]). The protein has been
Externí odkaz:
https://doaj.org/article/1809eae09b074c8f8c0969f2c0e52c18
Autor:
Julie Vandenameele, Anne-Françoise Hennen, Ruth Kellner, André Matagne, Romain Malempré, Alexandre Di Paolo, Marylène Vandevenne, Noémie Rochus, Alain Brans
Publikováno v:
European biophysics journal : EBJ. 50(3-4)
Among various factors, the direct environment (e.g. pH, buffer components, salts, additives, etc.…) is known to have a crucial effect on both the stability and activity of proteins. In particular, proper buffer and pH conditions can improve their s
Autor:
Shrinivas G. Dumbre, Dominique Toye, Piet Herdewijn, Christopher Cozens, Vitor B. Pinheiro, Julie Vandenameele, Jean-Marie Frère, Marleen Renders, Mikhail Abramov, Donaat Kestemont, Eric Largy, Lia Margamuljana
Publikováno v:
Nucleic Acids Research
Six 1',5'-anhydrohexitol uridine triphosphates were synthesized with aromatic substitutions appended via a carboxamide linker to the 5-position of their bases. An improved method for obtaining such 5-substituted hexitol nucleosides and nucleotides is
Autor:
Moreno Galleni, Marylène Vandevenne, Elodie Duray, Frédéric Cawez, Cécile Vincke, Ema Romão, Julie Vandenameele, Yaozhong Hu, Mireille Dumoulin, Serge Muyldermans
Publikováno v:
Journal of molecular biology. 430(11)
Recent advances in transcriptome sequencing and analysis have revealed the complexity of the human genome. The majority (≈ 98%) of cellular transcripts is not translated into proteins and represents a vast, unchartered world of functional non-codin
Publikováno v:
The Analyst. 142(8)
We propose in this paper that protein microarrays could be analysed by infrared imaging in place of enzymatic or fluorescence labelling. This label-free method reports simultaneously a large series of data on the spotted sample (protein secondary str
Autor:
Erik Goormaghtigh, Julie Vandenameele, Marie Valerio-Lepiniec, Cécile Van de Weerdt, Philippe Minard, André Matagne, Maximiliano Figueroa
Publikováno v:
Data in Brief
Data in Brief, Elsevier, 2016, 8, 〈10.1016/j.dib.2016.07.036〉
Data in Brief, Elsevier, 2016, 8, ⟨10.1016/j.dib.2016.07.036⟩
Data in Brief, 8
Data in Brief, 2016, 8, ⟨10.1016/j.dib.2016.07.036⟩
Data in Brief, Vol 8, Iss, Pp 1221-1226 (2016)
Data in Brief, Elsevier, 2016, 8, 〈10.1016/j.dib.2016.07.036〉
Data in Brief, Elsevier, 2016, 8, ⟨10.1016/j.dib.2016.07.036⟩
Data in Brief, 8
Data in Brief, 2016, 8, ⟨10.1016/j.dib.2016.07.036⟩
Data in Brief, Vol 8, Iss, Pp 1221-1226 (2016)
The artificial protein Octarellin V.1 (http://dx.doi.org/10.1016/j.jsb.2016.05.004 [1]) was obtained through a direct evolution process over the de novo designed Octarellin V (http://dx.doi.org/10.1016/S0022-2836(02)01206-8 [2]). The protein has been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c954ef6db1b1acaa5d5df619e71396b8
https://hal.archives-ouvertes.fr/hal-01355827
https://hal.archives-ouvertes.fr/hal-01355827
Autor:
Dominique Maes, Philippe Minard, Jens Meiler, Julie Vandenameele, Mike Sleutel, Els Pardon, Christian Damblon, Marie Valerio-Lepiniec, André Matagne, Marylène Vandevenne, Agathe Urvoas, Maximiliano Figueroa, Dominique Durand, Gregory Parvizi, Sophie Attout, Erik Goormaghtigh, Jan Steyaert, Joseph Martial, Axel Fischer, Olivier Jacquin, Cécile Van de Weerdt
Publikováno v:
Journal of Structural Biology
Journal of Structural Biology, Elsevier, 2016, pp.19-30. ⟨10.1016/j.jsb.2016.05.004⟩
Journal of Structural Biology, Elsevier, 2016, pp.19-30. 〈10.1016/j.jsb.2016.05.004〉
Journal of Structural Biology, 2016, pp.19-30. ⟨10.1016/j.jsb.2016.05.004⟩
Journal of Structural Biology, Elsevier, 2016, pp.19-30. ⟨10.1016/j.jsb.2016.05.004⟩
Journal of Structural Biology, Elsevier, 2016, pp.19-30. 〈10.1016/j.jsb.2016.05.004〉
Journal of Structural Biology, 2016, pp.19-30. ⟨10.1016/j.jsb.2016.05.004⟩
International audience; Despite impressive successes in protein design, designing a well-folded protein of more 100 amino acids de novo remains a formidable challenge. Exploiting the promising biophysical features of the artificial protein Octarellin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::190ec1f8c1ef0482214541f705913f6a
https://hal.archives-ouvertes.fr/hal-01455488
https://hal.archives-ouvertes.fr/hal-01455488
Autor:
Danielle Baeyens-Volant, André Matagne, Laetitia Bolle, Ruddy Wattiez, Julie Vandenameele, Mohamed Azarkan
Publikováno v:
Phytochemistry. 72:1718-1731
The latex of Ficus carica constitutes an important source of many proteolytic components known under the general term of ficin (EC 3.4.22.3) which belongs to the cysteine proteases of the papain family. So far, no data on the purification and charact
Autor:
Jean Denis Docquier, Luca Bini, Julie Vandenameele, André Matagne, Luisa Borgianni, Robert A. Bonomo, Jean-Marie Frère, Gian Maria Rossolini
Publikováno v:
Antimicrobial Agents and Chemotherapy. 54:3197-3204
Metallo-β-lactamase (MBL)-producing bacteria are emerging worldwide and represent a formidable threat to the efficacy of relevant β-lactams, including carbapenems, expanded-spectrum cephalosporins, and β-lactamase inactivator/β-lactam combination
Autor:
Julie Vandenameele, André Matagne, Franz X. Schmid, Alexandre Di Paolo, Annabelle Lejeune, Alain Brans, Jean-Marie Frère
Publikováno v:
Biochemistry. 49:4264-4275
Class A beta-lactamases (M(r) approximately 29000) provide good models for studying the folding mechanism of large monomeric proteins. In particular, the highly conserved cis peptide bond between residues 166 and 167 at the active site of these enzym