Zobrazeno 1 - 6
of 6
pro vyhledávání: '"MESH: Guanidine"'
Autor:
Anna Wozniak, Ana Cristina Sotomayor Pérez, Bruno Baron, Johanna C. Karst, Patrick England, Daniel Ladant, Alexandre Chenal
Publikováno v:
Biophysical Journal
Biophysical Journal, 2010, 99 (11), pp.3744-53. ⟨10.1016/j.bpj.2010.10.016⟩
Biophysical Journal, Biophysical Society, 2010, 99 (11), pp.3744-53. ⟨10.1016/j.bpj.2010.10.016⟩
Biophysical Journal, 2010, 99 (11), pp.3744-53. ⟨10.1016/j.bpj.2010.10.016⟩
Biophysical Journal, Biophysical Society, 2010, 99 (11), pp.3744-53. ⟨10.1016/j.bpj.2010.10.016⟩
International audience; The adenylate cyclase toxin (CyaA) is one of the major virulence factors of Bordetella pertussis, the causative agent of whooping cough. Its C-terminal region, the receptor-binding domain (RD), contains ∼40 calcium-binding R
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b79c92d2e8fbd75f6ddc7ee50e9f277b
https://doi.org/10.1016/j.bpj.2010.10.016
https://doi.org/10.1016/j.bpj.2010.10.016
Autor:
Christophe Bodenreider, Guillaume Sapriel, Philippe Delepelaire, Alain Chaffotte, Nicolas Wolff
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2003, 278 (40), pp.38247-38253. ⟨10.1074/jbc.M302322200⟩
Journal of Biological Chemistry, 2003, 278 (40), pp.38247-38253. ⟨10.1074/jbc.M302322200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2003, 278 (40), pp.38247-38253. ⟨10.1074/jbc.M302322200⟩
Journal of Biological Chemistry, 2003, 278 (40), pp.38247-38253. ⟨10.1074/jbc.M302322200⟩
International audience; We have previously shown that SecB, the ATP-independent chaperone of the Sec pathway, is required for the secretion of the HasA hemophore from Serratia marcescens via its type I secretion pathway, both in the reconstituted sys
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::662d5491699afe6dcc50d66d5b107a9c
https://doi.org/10.1074/jbc.m302322200
https://doi.org/10.1074/jbc.m302322200
Autor:
Philippe Clair, Bernard Lebleu, Gaelle Deglane, Hong M. Moulton, Saïd Abes, Michael J. Gait, Françoise Debart, Jean-Jacques Vasseur
Publikováno v:
Current Topics in Medicinal Chemistry
Current Topics in Medicinal Chemistry, Bentham Science Publishers, 2007, 7 (7), pp.727-37. ⟨10.2174/156802607780487704⟩
Current Topics in Medicinal Chemistry, Bentham Science Publishers, 2007, 7 (7), pp.727-37. ⟨10.2174/156802607780487704⟩
Specific control of gene expression by synthetic oligonucleotides (ON) is now widely used for target validation but clinical applications are limited by ON bioavailability. Moreover, most currently used strategies for physical and chemical delivery c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eb86b2e03df585ee7b78250f61c11887
https://pubmed.ncbi.nlm.nih.gov/17430212
https://pubmed.ncbi.nlm.nih.gov/17430212
Autor:
Alexander D. Dergunov, Michel Desmadril, Vanessa Clément-Collin, Lawrence P. Aggerbeck, Gérard Siest, Anne Barbier, Masa Takahashi, Athanase Visvikis
Publikováno v:
Biophysical Chemistry
Biophysical Chemistry, Elsevier, 2006, 119 (2), pp.170-85. ⟨10.1016/j.bpc.2005.07.009⟩
Biophysical Chemistry, Elsevier, 2006, 119 (2), pp.170-85. ⟨10.1016/j.bpc.2005.07.009⟩
The stabilities toward thermal and chemical denaturation of three recombinant isoforms of human apolipoprotein E (r-apoE2, r-apoE3 and r-apoE4), human plasma apoE3, the recombinant amino-terminal (NT) and the carboxyl-terminal (CT) domains of plasma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e91810836e47c8412b3067f550d81cbd
https://hal.archives-ouvertes.fr/hal-00132154
https://hal.archives-ouvertes.fr/hal-00132154
Publikováno v:
Protein Science
Protein Science, Wiley, 2002, 11 (11), pp.2697-705
Protein Science, Wiley, 2002, 11 (11), pp.2697-705
A mutational analysis of three co-variant pairs of residues, located at the surface of a single-chain fragment, variable (scFv), remote from the antigen-binding site, was performed to investigate the tolerance of these positions to amino acid changes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87fbee1fbd3d438dfebe328ce891ed50
https://hal.archives-ouvertes.fr/hal-00265246
https://hal.archives-ouvertes.fr/hal-00265246
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1997, 272 (40), pp.24843-9. ⟨10.1074/jbc.272.40.24843⟩
Journal of Biological Chemistry, 1997, 272 (40), pp.24843-9. ⟨10.1074/jbc.272.40.24843⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 1997, 272 (40), pp.24843-9. ⟨10.1074/jbc.272.40.24843⟩
Journal of Biological Chemistry, 1997, 272 (40), pp.24843-9. ⟨10.1074/jbc.272.40.24843⟩
International audience; We have shown previously that, in less than 4 ms, the unfolded/oxidized hen lysozyme recovered its native secondary structure, while the reduced protein remained fully unfolded. To investigate the role played by disulfide brid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6fa1a302a9816d0ebc77f3ff57bf1f2f
https://hal-pasteur.archives-ouvertes.fr/pasteur-00372851
https://hal-pasteur.archives-ouvertes.fr/pasteur-00372851