Sabiia Seb
PortuguêsEspañolEnglish
Embrapa
        Busca avançada

Botão Atualizar


Botão Atualizar

Ordenar por: 

RelevânciaAutorTítuloAnoImprime registros no formato resumido
Registros recuperados: 5
Primeira ... 1 ... Última
Imagem não selecionada

Imprime registro no formato completo
Advances and challenges in therapeutic monoclonal antibodies drug development BJPS
Santos,Mariana Lopes dos; Quintilio,Wagner; Manieri,Tania Maria; Tsuruta,Lilian Rumi; Moro,Ana Maria.
The use of serum containing polyclonal antibodies from animals immunized with toxins marked the beginning of the application of antibody-based therapy in late nineteenth century. Advances in basic research led to the development of the hybridoma technology in 1975. Eleven years later, the first therapeutic monoclonal antibody (mAb) was approved, and since then, driven by technological advances, the development of mAbs has played a prominent role in the pharmaceutical industry. In this review, we present the developments to circumvent problems of safety and efficacy arising from the murine origin of the first mAbs and generate structures more similar to human antibodies. As of October 2017, there are 61 mAbs and 11 Fc-fusion proteins in clinical use. An...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Immunotherapy; CDR grafting; Phage display; Transgenic mice; Single B cell sorting..
Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1984-82502018000700406
Imagem não selecionada

Imprime registro no formato completo
Expression of anti-Z-DNA single chain antibody variable fragment on the filamentous phage surface BJMBR
Maranhão,A.Q.; Brígido,M.M..
We describe the expression of an anti-Z-DNA single chain variable region antibody fragment (scFv) on a filamentous phage surface. Four vectors for phage display were constructed. Two of them are able to display multiple copies of the antibody fragment, and the others can be used to make monovalent libraries. The vectors use different promoter/leader sequences to direct the expression of the fused proteins. All were able to promote the assembly of fusion virion particles. In this paper we also show the affinity selection (biopanning) of those phage-antibodies based on the capacity of their products to recognize the antigen. We used biotinylated Z-DNA and the selection was performed in a solution phase fashion. The data presented here indicate that these...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Anti-nucleic acid antibodies; Phage display; Biopanning; ScFv; Z-DNA.
Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000500012
Imagem não selecionada

Imprime registro no formato completo
Improved affinity selection using phage display technology and off-rate based selection Electron. J. Biotechnol.
Yuan,Bin; Schulz,Philip; Liu,Ruitian; Sierks,Michael R..
Flow systems such as a BIAcore biosensor can be very efficient tools to isolate high affinity antibody fragments from affinity matured phage display libraries. Here we show that using flow based selection, we can readily isolate a variant with a 35-fold higher affinity, especially with a 7 fold better off-rate, compared to the parent clone after only a single round of selection from a second generation affinity matured phage display library. The flow system represents a fast method to isolate affinity improved antibody fragments and can be particularly useful for isolating antibodies to antigens that have poor solubility, are toxic to the host cell, or prone to aggregation.
Tipo: Journal article Palavras-chave: Affinity maturation; Beta-amyloid (Abeta); Dissociation rate; Phage display.
Ano: 2006 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582006000200011
Imagem não selecionada

Imprime registro no formato completo
Isolation of recombinant antibodies directed against surface proteins of Clostridium difficile BJM
Shirvan,Ali Nazari; Aitken,Robert.
Abstract Clostridium difficile has emerged as an increasingly important nosocomial pathogen and the prime causative agent of antibiotic-associated diarrhoea and pseudomembranous colitis in humans. In addition to toxins A and B, immunological studies using antisera from patients infected with C. difficile have shown that a number of other bacterial factors contribute to the pathogenesis, including surface proteins, which are responsible for adhesion, motility and other interactions with the human host. In this study, various clostridial targets, including FliC, FliD and cell wall protein 66, were expressed and purified. Phage antibody display yielded a large panel of specific recombinant antibodies, which were expressed, purified and characterised....
Tipo: Info:eu-repo/semantics/article Palavras-chave: Clostridium difficile; Recombinant antibody; Phage display.
Ano: 2016 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822016000200394
Imagem não selecionada

Imprime registro no formato completo
Phage display technology: applications and innovations Genet. Mol. Biol.
Arap,Marco Antonio.
The expression of exogenous peptides on the surface of filamentous bacteriophage was initially described by Smith in 1985. Since his first study, different molecules such as small peptides and antibodies have been displayed on coat proteins of phage, greatly expanding the applications of the technology. The past decade has seen considerable progress in the techniques and applications of phage libraries. In addition, different screening methods have allowed isolation and characterization of peptides binding to several molecules in vitro, in the context of living cells, in animals and in humans. Here we review the applications, recent innovations, and future directions of phage display technology.
Tipo: Info:eu-repo/semantics/article Palavras-chave: Phage display; Applications.
Ano: 2005 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572005000100001
Registros recuperados: 5
Primeira ... 1 ... Última
 

Empresa Brasileira de Pesquisa Agropecuária - Embrapa
Todos os direitos reservados, conforme Lei n° 9.610
Política de Privacidade
Área restrita

Embrapa
Parque Estação Biológica - PqEB s/n°
Brasília, DF - Brasil - CEP 70770-901
Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco

Valid HTML 4.01 Transitional