Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Tarun J, Narwani"'
Autor:
Akhila Melarkode Vattekatte, Nicolas Ken Shinada, Tarun J. Narwani, Floriane Noël, Olivier Bertrand, Jean-Philippe Meyniel, Alain Malpertuy, Jean-Christophe Gelly, Frédéric Cadet, Alexandre G. de Brevern
Publikováno v:
PeerJ, Vol 8, p e8408 (2020)
Antigen binding by antibodies requires precise orientation of the complementarity- determining region (CDR) loops in the variable domain to establish the correct contact surface. Members of the family Camelidae have a modified form of immunoglobulin
Externí odkaz:
https://doaj.org/article/12fc66473bc242b3baf0e78022ec6ed9
Publikováno v:
International Journal of Molecular Sciences
Integrin αIIbβ3, a glycoprotein complex expressed at the platelet surface, is involved in platelet aggregation and contributes to primary haemostasis. Several integrin αIIbβ3 polymorphisms prevent the aggregation that causes haemorrhagic syndrome
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::010928dc06322e9b65834663b800fb8b
https://pubmed.ncbi.nlm.nih.gov/35055046
https://pubmed.ncbi.nlm.nih.gov/35055046
Publikováno v:
International Journal of Molecular Sciences; Volume 23; Issue 2; Pages: 858
International Journal of Molecular Sciences
International Journal of Molecular Sciences, MDPI, 2022, 23 (2), pp.858. ⟨10.3390/ijms23020858⟩
International Journal of Molecular Sciences, Vol 23, Iss 858, p 858 (2022)
International Journal of Molecular Sciences
International Journal of Molecular Sciences, MDPI, 2022, 23 (2), pp.858. ⟨10.3390/ijms23020858⟩
International Journal of Molecular Sciences, Vol 23, Iss 858, p 858 (2022)
Integrin αIIbβ3, a glycoprotein complex expressed at the platelet surface, is involved in platelet aggregation and contributes to primary haemostasis. Several integrin αIIbβ3 polymorphisms prevent the aggregation that causes haemorrhagic syndrome
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9b292c5f3d5f73834e58b81949f28fb
https://doi.org/10.3390/ijms23020858
https://doi.org/10.3390/ijms23020858
Autor:
Pierrick, Craveur, Agnel P, Joseph, Jeremy, Esque, Tarun J, Narwani, Floriane, Noël, Nicolas, Shinada, Matthieu, Goguet, Sylvain, Leonard, Pierre, Poulain, Olivier, Bertrand, Guilhem, Faure, Joseph, Rebehmed, Amine, Ghozlane, Lakshmipuram S, Swapna, Ramachandra M, Bhaskara, Jonathan, Barnoud, Stéphane, Téletchéa, Vincent, Jallu, Jiri, Cerny, Bohdan, Schneider, Catherine, Etchebest, Narayanaswamy, Srinivasan, Jean-Christophe, Gelly, Alexandre G, de Brevern
Publikováno v:
Frontiers in Molecular Biosciences
Protein structures are valuable tools to understand protein function. Nonetheless, proteins are often considered as rigid macromolecules while their structures exhibit specific flexibility, which is essential to complete their functions. Analyses of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::02b6f852d69f67dfb6da027a8e11e870