Zobrazeno 1 - 10
of 307
pro vyhledávání: '"Structural alphabet"'
Autor:
Aline Floch, Tatiana Galochkina, France Pirenne, Christophe Tournamille, Alexandre G. de Brevern
Publikováno v:
Frontiers in Chemistry, Vol 12 (2024)
Introduction: Blood group antigens of the RH system (formerly known as “Rhesus”) play an important role in transfusion medicine because of the severe haemolytic consequences of antibodies to these antigens. No crystal structure is available for R
Externí odkaz:
https://doaj.org/article/b9e0b30885cd4f1c8b8bbe2513c226c1
Autor:
Denis V. Petrovskiy, Kirill S. Nikolsky, Vladimir R. Rudnev, Liudmila I. Kulikova, Tatiana V. Butkova, Kristina A. Malsagova, Arthur T. Kopylov, Anna L. Kaysheva
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 19, p 14439 (2023)
The development and improvement of methods for comparing and searching for three-dimensional protein structures remain urgent tasks in modern structural biology. To solve this problem, we developed a new tool, SAFoldNet, which allows for searching, a
Externí odkaz:
https://doaj.org/article/bd3ed7fa776440339a7385274daae58f
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 19, p 14586 (2023)
Camelids have the peculiarity of having classical antibodies composed of heavy and light chains as well as single-chain antibodies. They have lost their light chains and one heavy-chain domain. This evolutionary feature means that their terminal heav
Externí odkaz:
https://doaj.org/article/fc9deafbd3c74a12b1ed6273204ceccc
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 17, p 13280 (2023)
Plasmodium vivax malaria affects 14 million people each year. Its invasion requires interactions between the parasitic Duffy-binding protein (PvDBP) and the N-terminal extracellular domain (ECD1) of the host’s Duffy antigen/receptor for chemokines
Externí odkaz:
https://doaj.org/article/875c5ee88ecc404b82515647921d1022
Autor:
Akhila Melarkode Vattekatte, Julien Diharce, Joseph Rebehmed, Frédéric Cadet, Fabrice Gardebien, Catherine Etchebest, Alexandre G. de Brevern
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 5, p 4511 (2023)
Conformational flexibility plays an essential role in antibodies’ functional and structural stability. They facilitate and determine the strength of antigen–antibody interactions. Camelidae express an interesting subtype of single-chain antibody,
Externí odkaz:
https://doaj.org/article/874e1da153014e579857add084302e21
Autor:
Pierre Laville, Sandrine Fartek, Natacha Cerisier, Delphine Flatters, Michel Petitjean, Leslie Regad
Publikováno v:
BMC Molecular and Cell Biology, Vol 21, Iss 1, Pp 1-15 (2020)
Abstract Background Drug resistance is a severe problem in HIV treatment. HIV protease is a common target for the design of new drugs for treating HIV infection. Previous studies have shown that the crystallographic structures of the HIV-2 protease (
Externí odkaz:
https://doaj.org/article/bdf3e463bf1a4265b0cb6fc2c68d31a2
Autor:
Pierre Tufféry, Sjoerd de Vries
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 18, Iss , Pp 1790-1799 (2020)
Protein engineering or candidate therapeutic peptide optimization are processes in which the identification of relevant sequence variants is critical. Starting from one amino-acid sequence, the choice of the substitutions must meet the objective of n
Externí odkaz:
https://doaj.org/article/408ec15d068849518462e3ca9fd34710
Akademický článek
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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, Vol 23, Iss 2, 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://doaj.org/article/7286e1b8c402451ab065c249f9bd9575