Result Number | Material Type | Add to My Shelf Action | Record Details and Options |
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1 |
Material Type: Artigo
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Bound Water Molecules and Conformational Stabilization Help Mediate an Antigen-Antibody AssociationBhat, T. Narayana ; Bentley, Graham A. ; Boulot, Ginette ; Greene, Mark I. ; Tello, Diana ; Dall'Acqua, William ; Souchon, Helene ; Schwarz, Frederick P. ; Mariuzza, Roy A. ; Poljak, Robert J.Proceedings of the National Academy of Sciences - PNAS, 1994-02, Vol.91 (3), p.1089-1093 [Periódico revisado por pares]Washington, DC: National Academy of Sciences of the United States of AmericaTexto completo disponível |
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2 |
Material Type: Artigo
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Structure and Thermodynamics of Antigen Recognition by AntibodiesBRADEN, BRADFORD C. ; CAUERHFF, ANA ; DALL'ACQUA, WILLIAM ; FIELDS, BARRY A. ; GOLDBAUM, FERNANDO A. ; MALCHIODI, EMILIO L. ; MARIUZZA, ROY A. ; POLJAK, ROBERTO J. ; SCHWARZ, FREDERICK P. ; YSERN, XAVIER ; BHAT, T. N.Annals of the New York Academy of Sciences, 1995-09, Vol.764 (1), p.315-327 [Periódico revisado por pares]Oxford, UK: Blackwell Publishing LtdSem texto completo |
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3 |
Material Type: Artigo
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Crystal Structure of the Complex of the Variable Domain of Antibody D1.3 and Turkey Egg White Lysozyme: A Novel Conformational Change in Antibody CDR-L3 Selects for AntigenBraden, Bradford C. ; Fields, Barry A. ; Ysern, Xavier ; Goldbaum, Fernando A. ; Dall'Acqua, William ; Schwarz, Frederick P. ; Poljak, Roberto J. ; Mariuzza, Roy A.Journal of molecular biology, 1996-04, Vol.257 (5), p.889-894 [Periódico revisado por pares]England: Elsevier LtdTexto completo disponível |
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4 |
Material Type: Artigo
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Structural and physicochemical analysis of the reaction between the anti-lysozyme antibody D1.3 and the anti-idiotopic antibodies E225 and E5.2Tello, Diana ; Eisenstein, Edward ; Schwarz, Frederick P. ; Goldbaum, Fernando A. ; Fields, Barry A. ; Mariuzza, Roy A. ; Poljak, Roberto J.Journal of molecular recognition, 1994-03, Vol.7 (1), p.57-62 [Periódico revisado por pares]Chichester, UK: John Wiley & Sons, LtdSem texto completo |