J
Jan Atienza-Garriga
Publications - 3
Citations - 6
Jan Atienza-Garriga is an academic researcher. The author has contributed to research in topics: Biology & Chemistry. The author has an hindex of 1, co-authored 3 publications receiving 6 citations.
Papers
More filters
Journal ArticleDOI
Recombinant vaccines in 2022: a perspective from the cell factory
Marianna Teixeira de Pinho Favaro,Jan Atienza-Garriga,Carlos Martínez-Torró,Eloi Parladé,Esther Vázquez,José Luis Corchero,Neus Ferrer-Miralles,Antonio Villaverde +7 more
TL;DR: The diversity of recombinant antimicrobial vaccines and vaccine prototypes is revised here considering the cell factory types, through relevant examples of prototypes under development as well as already approved products as mentioned in this paper . But despite these fast-developing approaches, subunit vaccines still show a wide spectrum of interesting potentialities and an important margin for further development.
Journal ArticleDOI
Enhanced recombinant protein capture, purity and yield from crude bacterial cell extracts by N-Lauroylsarcosine-assisted affinity chromatography
Jose Vicente Carratalá,Jan Atienza-Garriga,Hèctor López-Laguna,Esther Vázquez,Antonio Villaverde,Julieta M. Sánchez,Neus Ferrer-Miralles +6 more
TL;DR: In this paper , a novel procedure has been developed based on supplementing crude cell extracts with non-denaturing concentrations of the anionic detergent N -Lauroylsarcosine.
Journal ArticleDOI
Biofabrication of Self-Assembling Covalent Protein Nanoparticles through Histidine-Templated Cysteine Coupling
Hèctor López-Laguna,Ariana Rueda,Carlos Martínez-Torró,Lucía Sánchez-Alba,Jose Vicente Carratalá,Jan Atienza-Garriga,Eloi Parladé,Julieta M. Sánchez,Naroa Serna,Eric Voltà-Durán,Neus Ferrer-Miralles,David Reverter,Ramon Mangues,Antonio Villaverde,Esther Vázquez,Ugutz Unzueta +15 more
TL;DR: In this paper , a histidine-templated cysteine-coupling concept was proposed to enable the spontaneous and efficient self-assembling of tagged proteins into monodisperse nanoparticles through a highly ordered covalent binding process.