Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Andrés González-Techera"'
Autor:
Ana Maite Folle, Sofía Lagos Magallanes, Martín Fló, Romina Alvez-Rosado, Federico Carrión, Cecilia Vallejo, David Watson, Josep Julve, Gualberto González-Sapienza, Otto Pristch, Andrés González-Techera, Ana María Ferreira
Publikováno v:
Frontiers in Cellular and Infection Microbiology, Vol 14 (2024)
Cestodes use own lipid-binding proteins to capture and transport hydrophobic ligands, including lipids that they cannot synthesise as fatty acids and cholesterol. In E. granulosus s.l., one of these lipoproteins is antigen B (EgAgB), codified by a mu
Externí odkaz:
https://doaj.org/article/6e066fc267e646fd9ba82bbbffe35c50
Autor:
Triana Delfin-Riela, Andrés González-Techera, Gabriel Lassabe, Romina Alvez-Rosado, Álvaro Modernell, Gualberto González-Sapienza, Martina Scarrone
Publikováno v:
New Biotechnology. 64:9-16
Nanobodies are the smallest antibody fragments which bind to antigens with high affinity and specificity. Due to their outstanding physicochemical stability, simplicity and cost-effective production, nanobodies have become powerful agents in therapeu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ecc275bac6de299fba4bb968b0288947
https://doi.org/10.1016/j.nbt.2021.05.002
https://doi.org/10.1016/j.nbt.2021.05.002
Autor:
Aylén Di Tocco, Gabriela Porcal, Gabriel Lassabe, Andrés González-Techera, María Zón, Héctor Fernández, Gualberto González-Sapienza, Sebastian Robledo, Fernando Javier Arévalo
Publikováno v:
Sensors and Actuators B: Chemical. 367:132126
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::114d9f23ea01ca99f34d1be7a4a95d56
https://doi.org/10.1016/j.snb.2022.132126
https://doi.org/10.1016/j.snb.2022.132126
Autor:
Gabriel Lassabe, Bruce D. Hammock, Gualberto González-Sapienza, Karl Kramer, Andrés González-Techera
Publikováno v:
Analytical chemistry, vol 90, iss 10
Our group has previously developed immunoassays for noncompetitive detection of small molecules based on the use of phage borne anti-immunocomplex peptides. Recently, we substituted the phage particles by biotinylated synthetic anti-immunocomplex pep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bdbce1b891e6b8810740824e5df1749
https://doi.org/10.1021/acs.analchem.8b00657
https://doi.org/10.1021/acs.analchem.8b00657
Publikováno v:
Analytical Chemistry
Small compounds cannot bind simultaneously to two antibodies, and thus, their immunodetection is limited to competitive formats in which the analyte is indirectly quantitated by measuring the unoccupied antibody binding sites using a competing report
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::00d48a097d2be3b340e776823bf1f995
https://doi.org/10.1021/ac500926f
https://doi.org/10.1021/ac500926f
Publikováno v:
Analytical Chemistry. 85:1177-1182
There is a great demand for rapid tests that can be used on-site for the detection of small analytes, such as pesticides, persistent organic pollutants, explosives, toxins, medicinal and abused drugs, hormones, etc. Dipsticks and lateral flow devices
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9b6601d1c7a70a1e228b7cccb03ccf4
https://doi.org/10.1021/ac3031114
https://doi.org/10.1021/ac3031114
Autor:
Gualberto González-Sapienza, Carmen Leizagoyen, Bruce D. Hammock, Yongliang Cui, Christophe Morisseau, Candace S. Bever, Macarena Pírez, Martín A. Rossotti, Andrés González-Techera, Shirley J. Gee, Kin Sing Stephen Lee
Publikováno v:
Analytical chemistry, vol 87, iss 23
Single domain heavy-chain binders (nanobodies) obtained from camelid antibody libraries hold a great promise for immunoassay development. However, there is no simple method to select the most valuable nanobodies from the crowd of positive clones obta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07009021baf4fb6c9b804db39a1335c6
https://europepmc.org/articles/PMC4666776/
https://europepmc.org/articles/PMC4666776/
Autor:
Martín A. Rossotti, José A. Chabalgoity, Lucía Yim, Marcelo Fernández, Ximena Camacho, Pablo Cabral, Gualberto González-Sapienza, Julio Guarnaschelli, Carmen Leizagoyen, Andrés González-Techera
Recombinant single domain antibodies (nanobodies) constitute an attractive alternative for the production of neutralizing therapeutic agents. Their small size warrants rapid bioavailability and fast penetration to sites of toxin uptake, but also rapi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::13659b93f14b4686fa308a3b2d81181d
https://europepmc.org/articles/PMC4622952/
https://europepmc.org/articles/PMC4622952/
Autor:
Martín A. Rossotti, Gualberto González-Sapienza, Gabriel Lassabe, Andrés González-Techera, Mariana Carlomagno, Lucia Vanrell
Publikováno v:
Analytical Chemistry
Short peptide loops selected from phage libraries can specifically recognize the formation of hapten-antibody immunocomplexes and can thus be used to develop phage anti-immunocomplex assays (PHAIA) for noncompetitive detection of small molecules. In
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a43b619752fc843abe2a5dce45284a8
https://pubmed.ncbi.nlm.nih.gov/25257512
https://pubmed.ncbi.nlm.nih.gov/25257512
Autor:
María Alicia Zon, Patricia G. Molina, Gualberto González-Sapienza, Fernando Javier Arévalo, Andrés González-Techera, Héctor Fernández
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
The development of immunosensors for the detection of small molecules is of great interest because of their simplicity, high sensitivity and extended analytical range. Due to their size, small compounds cannot be simultaneously recognized by two anti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef9bdec3369bd1346f53ba5c4dd726f2
https://pubmed.ncbi.nlm.nih.gov/25441414
https://pubmed.ncbi.nlm.nih.gov/25441414