Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Paola Bazzacco"'
Autor:
Emmanuelle Billon-Denis, Jean-Luc Popot, Christel Le Bon, K. Shivaji Sharma, Christine Ebel, Frank Gabel, Grégory Durand, Laurent Catoire, Paola Bazzacco, Bernard Pucci
Publikováno v:
Langmuir
Langmuir, American Chemical Society, 2012, ⟨10.1021/la205026r⟩
Langmuir, 2012, ⟨10.1021/la205026r⟩
Langmuir, American Chemical Society, 2012, ⟨10.1021/la205026r⟩
Langmuir, 2012, ⟨10.1021/la205026r⟩
International audience; A novel type of nonionic amphipols for handling membrane proteins in detergent-free aqueous solutions has been obtained through free-radical homo-telomerization of an acrylamide-based monomer comprising a C 11 alkyl chain and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b744a9b164db719a699681da5f9c6e7d
https://doi.org/10.1021/la205026r
https://doi.org/10.1021/la205026r
Autor:
Christine Ebel, Paola Bazzacco, Jean-Luc Popot, K. Shivaji Sharma, Bernard Pucci, Fabrice Giusti, Grégory Durand
Publikováno v:
Biomacromolecules
Biomacromolecules, 2009, 10 (12), pp.3317-3326. ⟨10.1021/bm900938w⟩
Biomacromolecules, American Chemical Society, 2009, 10 (12), pp.3317-3326. ⟨10.1021/bm900938w⟩
Biomacromolecules, 2009, 10 (12), pp.3317-3326. ⟨10.1021/bm900938w⟩
Biomacromolecules, American Chemical Society, 2009, 10 (12), pp.3317-3326. ⟨10.1021/bm900938w⟩
Amphipols (APols) are short amphipathic polymers designed to adsorb onto the transmembrane surface of membrane proteins, keeping them water-soluble in the absence of detergent. Current APols carry charged groups, which is a limitation for certain typ
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1991567a1470735b7de520ccbf2e6636
https://doi.org/10.1021/bm900938w
https://doi.org/10.1021/bm900938w
Autor:
Yoon Jae Kim, Hector Serrano, Elizabeth A. Burks, Gerrit J. Poelarends, Andy-Mark W. H. Thunnissen, Christian P. Whitman, William H. Johnson, Bauke W. Dijkstra, René M. de Jong, Paola Bazzacco
Publikováno v:
Journal of Biological Chemistry. 282:2440-2449
The bacterial degradation pathways for the nematocide 1,3-dichloropropene rely on hydrolytic dehalogenation reactions catalyzed by cis- and trans-3-chloroacrylic acid dehalogenases (cis-CaaD and CaaD, respectively). X-ray crystal structures of native
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5deed9c9976e9b5458280762da16fea6
https://doi.org/10.1074/jbc.m608134200
https://doi.org/10.1074/jbc.m608134200
Autor:
Grégory Durand, K. Shivaji Sharma, Laurent Catoire, Jean-Louis Banères, Emmanuelle Billon-Denis, Sophie Mary, Elodie Point, Francesca Zito, Christel Le Bon, Jean-Luc Popot, Bernard Pucci, Paola Bazzacco
Publikováno v:
Biochemistry
Biochemistry, American Chemical Society, 2012, 51 (7), pp.1416-1430. ⟨10.1021/bi201862v⟩
Biochemistry, American Chemical Society, 2012, ⟨10.1021/bi201862v⟩
Biochemistry, American Chemical Society, 2012, 51 (7), pp.1416-1430. ⟨10.1021/bi201862v⟩
Biochemistry, American Chemical Society, 2012, ⟨10.1021/bi201862v⟩
International audience; Nonionic amphipols (NAPols) synthesized by homotelomerization of an amphiphatic monomer are able to keep membrane proteins (MPs) stable and functional in the absence of detergent. Some of their biochemical and biophysical prop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9940e867d986eb1733cc187b997e1bea
https://pubmed.ncbi.nlm.nih.gov/22304405
https://pubmed.ncbi.nlm.nih.gov/22304405
Autor:
C. van Heijenoort, Jonathan N. Sachs, Werner Kühlbrandt, Yann Gohon, Melanie Picard, Manuela Zoonens, Delphine Charvolin, L M de la Maza, Emmanuelle Billon-Denis, B Pucci, Philippe Champeil, Melanie J. Cocco, F Gabel, Emmanuel-Pierre Guittet, Fabrice Giusti, J-L Popot, Tassadite Dahmane, Laurent J. Catoire, Christophe Tribet, D Bagnard, Thorsten Althoff, G Crémel, J-L Banères, C. Le Bon, Francesca Zito, Erik Goormaghtigh, Christine Ebel, Jörg H. Kleinschmidt, Karen L. Martinez, Frank Wien, Paola Bazzacco
Publikováno v:
Annual Review of Biophysics and Biomolecular Structure
Annual Review of Biophysics and Biomolecular Structure, Annual Reviews, 2011, 40 (1), pp.379-408. ⟨10.1146/annurev-biophys-042910-155219⟩
Annual Review of Biophysics and Biomolecular Structure, 2011, 40 (1), pp.379-408. ⟨10.1146/annurev-biophys-042910-155219⟩
Annual Reviews of Biophysics
Annual Reviews of Biophysics, Annual Reviews, 2011, 40, pp.379-408. ⟨10.1146/annurev-biophys-042910-155219⟩
Annual Review of Biophysics and Biomolecular Structure, Annual Reviews, 2011, 40 (1), pp.379-408. ⟨10.1146/annurev-biophys-042910-155219⟩
Annual Review of Biophysics and Biomolecular Structure, 2011, 40 (1), pp.379-408. ⟨10.1146/annurev-biophys-042910-155219⟩
Annual Reviews of Biophysics
Annual Reviews of Biophysics, Annual Reviews, 2011, 40, pp.379-408. ⟨10.1146/annurev-biophys-042910-155219⟩
International audience; Amphipols (APols) are short amphipathic polymers that can substitute for detergents to keep integral membrane proteins (MPs) water soluble. In this review, we discuss their structure and solution behavior; the way they associa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b35c1502e890a2b7c8c3fb7e36217d57
https://hal.archives-ouvertes.fr/hal-02327349
https://hal.archives-ouvertes.fr/hal-02327349
Autor:
Paola Bazzacco, Anne-Sylvie Fabiano, Bernard Pucci, Fabrice Giusti, Christine Ebel, Jean-Luc Popot, Grégory Durand, Tassadite Dahmane, K. Shivaji Sharma, Blandine Olivier
Publikováno v:
Langmuir
Langmuir, American Chemical Society, 2008, 24 (23), pp.13581-13590. ⟨10.1021/la8023056⟩
Langmuir, 2008, 24 (23), pp.13581-13590. ⟨10.1021/la8023056⟩
Langmuir, American Chemical Society, 2008, 24 (23), pp.13581-13590. ⟨10.1021/la8023056⟩
Langmuir, 2008, 24 (23), pp.13581-13590. ⟨10.1021/la8023056⟩
A novel class of nonionic amphipols (NAPols) designed to handle membrane proteins in aqueous solutions has been synthesized, and its solution properties have been examined. These were synthesized through free radical cotelomerization of glucose-based
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e14c221075df3296f9dd8f3f5c858a67
https://hal.archives-ouvertes.fr/hal-02329735
https://hal.archives-ouvertes.fr/hal-02329735
Autor:
René M, de Jong, Paola, Bazzacco, Gerrit J, Poelarends, William H, Johnson, Yoon Jae, Kim, Elizabeth A, Burks, Hector, Serrano, Andy-Mark W H, Thunnissen, Christian P, Whitman, Bauke W, Dijkstra
Publikováno v:
The Journal of biological chemistry. 282(4)
The bacterial degradation pathways for the nematocide 1,3-dichloropropene rely on hydrolytic dehalogenation reactions catalyzed by cis- and trans-3-chloroacrylic acid dehalogenases (cis-CaaD and CaaD, respectively). X-ray crystal structures of native
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5579e0770b238a5b62237e406d4b5c2b
https://pubmed.ncbi.nlm.nih.gov/17121835
https://pubmed.ncbi.nlm.nih.gov/17121835
Autor:
Paola Bazzacco, K. Shivaji Sharma, Grégory Durand, Fabrice Giusti, Christine Ebel, Jean-Luc Popot, Bernard Pucci
Publikováno v:
Biomacromolecules; Dec2009, Vol. 10 Issue 12, p3317-3326, 10p
Autor:
K. Shivaji Sharma, Grégory Durand, Fabrice Giusti, Blandine Olivier, Anne-Sylvie Fabiano, Paola Bazzacco, Tassadite Dahmane, Christine Ebel, Jean-Luc Popot, Bernard Pucci
Publikováno v:
Langmuir; Dec2008, Vol. 24 Issue 23, p13581-13590, 10p
Autor:
Florent Rouvière, Delphine Charvolin, Jean-Luc Popot, Jean-Baptiste Perez, Fabrice Rappaport, Karen L. Martinez, Fabrice Giusti, Paola Bazzacco, Alaa Abdine
Publikováno v:
University of Copenhagen
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, 2009, 106 (2), pp.405-410. ⟨10.1073/pnas.0807132106⟩
Proceedings of the National Academy of Sciences of the United States of America, 2009, 106 (2), pp.405-410. ⟨10.1073/pnas.0807132106⟩
Charvolin, D, Perez, J-B, Rouviere, F, Giusti, F, Bazzacco, P, Abdine, A, Rappaport, F, Martinez, K L & Popot, J-L 2009, ' The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports ', Proceedings of the National Academy of Science of the United States of America, vol. 106, no. 2, pp. 405-10 .
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, 2009, 106 (2), pp.405-410. ⟨10.1073/pnas.0807132106⟩
Proceedings of the National Academy of Sciences of the United States of America, 2009, 106 (2), pp.405-410. ⟨10.1073/pnas.0807132106⟩
Charvolin, D, Perez, J-B, Rouviere, F, Giusti, F, Bazzacco, P, Abdine, A, Rappaport, F, Martinez, K L & Popot, J-L 2009, ' The use of amphipols as universal molecular adapters to immobilize membrane proteins onto solid supports ', Proceedings of the National Academy of Science of the United States of America, vol. 106, no. 2, pp. 405-10 .
Because of the importance of their physiological functions, cell membranes represent critical targets in biological research. Membrane proteins, which make up ≈1/3 of the proteome, interact with a wide range of small ligands and macromolecular part
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b8d5f55854de6b88225d853852bacd1
https://curis.ku.dk/portal/en/publications/the-use-of-amphipolsas-universal-molecular-adapters-to-immobilize-membrane-proteins-onto-solid-supports(dba2e0c0-b0fe-11de-bc73-000ea68e967b).html
https://curis.ku.dk/portal/en/publications/the-use-of-amphipolsas-universal-molecular-adapters-to-immobilize-membrane-proteins-onto-solid-supports(dba2e0c0-b0fe-11de-bc73-000ea68e967b).html