✦ LIBER ✦

Structure of the complex of an Fab fragment of a neutralizing antibody with foot-and-mouth disease virus: positioning of a highly mobile antigenic loop

✍ Scribed by Hewat, E. A.

Book ID: 111745290
Publisher: Nature Publishing Group
Year: 1997
Tongue: English
Weight: 896 KB
Volume: 16
Category: Article
ISSN: 0261-4189
DOI: 10.1093/emboj/16.7.1492

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Flexibility of the Major Antigenic Loop

Flexibility of the Major Antigenic Loop of Foot-and-Mouth Disease Virus Bound to a Fab Fragment of a Neutralising Antibody: Structure and Neutralisation

✍ Nuria Verdaguer; Guy Schoehn; Wendy F. Ochoa; Ignacio Fita; Sharon Brookes; Andr 📂 Article 📅 1999 🏛 Elsevier Science 🌐 English ⚖ 549 KB

Conformational flexibility in a highly m

Conformational flexibility in a highly mobile protein loop of foot-and-mouth disease virus: distinct structural requirements for integrin and antibody binding

✍ Jordi X. Feliu; Antoni Benito; Baldomero Oliva; Francesc X. Avilés; Antonio Vill 📂 Article 📅 1998 🏛 Elsevier Science 🌐 English ⚖ 307 KB

Solution conformation of an immunogenic

Solution conformation of an immunogenic peptide from HRV2: comparison with the conformation found in a complex with a Fab fragment of an anti-HRV2 neutralizing antibody

✍ M. Antònia Molins; Miquel Àngel Contreras; Ignacio Fita; Miquel Pons 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 175 KB 👁 2 views

The conformation of a [15]-peptide (H-VKAETRLNPDLQPTE-NH 2 ) from VP2 of rhinovirus HRV2 complexed with a Fab fragment was previously shown by X-ray crystallographic studies to be similar to the one found in the corresponding region of HRV1A. Antibodies raised against this peptide bind to and neutra

Structure of Foot-and-mouth disease viru

Structure of Foot-and-mouth disease virus serotype A1061 alone and complexed with oligosaccharide receptor: receptor conservation in the face of antigenic variation

✍ Fry, E. E. 📂 Article 📅 2005 🏛 Society for General Microbiology 🌐 English ⚖ 980 KB

The Solution Conformational Features of

The Solution Conformational Features of Two Highly Homologous Antigenic Peptides of Foot-and-mouth Disease Virus Serotype A, Variants A and USA, Correlate with their Serological Properties

✍ M. Pegna; H. Molinari; L. Zetta; G. Melacini; W. A. Gibbons; F. Brown; D. Rowlan 📂 Article 📅 1996 🏛 John Wiley and Sons 🌐 English ⚖ 871 KB

The solution structure of a peptide corresponding to the VP1 region 141-160 of foot-and-mouth disease virus (FMDV) serotype A variant USA has been studied by NMR and computer calculations and compared with the results from a study on a highly homologous peptide deriving from serotype A, variant A. T

Identification of a major antibody bindi

Identification of a major antibody binding epitope in the non-structural protein 3D of foot-and-mouth disease virus in cattle and the development of a monoclonal antibody with diagnostic applications

✍ Ming Yang; Alfonso Clavijo; Mingyi Li; Kate Hole; Hilary Holland; He Wang; Ming 📂 Article 📅 2007 🏛 Elsevier Science 🌐 English ⚖ 629 KB