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9篇 您的检索式:作者名="Parlad"
    题名 作者 年代 出处 被引量
1Tracking mycorrhizas and extraradical mycelium of the edible fungus Lactarius deliciosus under field com- petition with Rhizopogonspp显示文摘Hortal S Pera J Parlade' J 2008Mycorrhiza2008,18,:1
2Anticipatory smiling:Linking early affective communication and social outcome显示文摘Parlade M V Messinger D S Delgado F 0,,:1
3Effects of ectomycorrhizal inocu- lation and the type of substrate on mycorrhization, growth and nutrition of containerised Pinus pinea L seedlings produced in a commercial nursery 显示文摘Rinc6n A Parlad J Pera J 2005Annals of Forest Science2005,62,8:1
4Evaluation of fungicides for the control of Botryosphaeria corticola on cork oak in Catalonia (NE Spain) 显示文摘LUQUE J PERA J PARLADE J 2008Forest Pathology2008,38,3:1
5Anticipatory smiling:linking early affective communication and social outcome显示文摘Parlade MV Messinger DS Delgado CE 2009Infant Behav Dev2009,32,1:1
6Coinoculation of aseptically grown Douglas fir with pairs of ectomycorrhizal fungi显示文摘Javier Parladé Isabel F. Alvarez 1993Mycorrhiza1993,,2:1
7Evaluation of fungicides for the control of Botryosphaeria corticola on cork oak in Catalonia ( NE Spain) 显示文摘LUQUE J PERA J PARLADE J 2008Forest Pathology2008,38,3:1
8The spectrum of building block conformers sustains the biophysical properties of clinically-oriented self-assembling protein nanoparticles显示文摘Histidine-rich peptides confer self-assembling properties to recombinant proteins through the supramolecular coordination with divalent cations.This fact allows the cost-effective,large-scale generation of microscopic and macroscopic protein materials with intriguing biomedical properties.Among such materials,resulting from the simple bioproduction of protein building blocks,homomeric nanoparticles are of special value as multivalent interactors and drug carriers.Interestingly,we have here identified that the assembly of a given His-tagged protein might render distinguishable categories of self-assembling protein nanoparticles.This fact has been scrutinized through the nanobody-containing fusion proteins EM1-GFP-H6 and A3C8-GFP-H6,whose biosynthesis results in two distinguishable populations of building blocks.In one of them,the assembling and disassembling is controllable by cations.However,a second population immediately self-assembles upon purification through a non-regulatable pathway,rendering larger nanoparticles with specific biological properties.The structural analyses of both model proteins and nanoparticles revealed important conformational variability in the building blocks.This fact renders different structural and functional categories of the final soft materials resulting from the participation of energetically unstable intermediates in the oligomerization process.These data illustrate the complexity of the Hismediated protein assembling in recombinant proteins but they also offer clues for a better design and refinement of protein-based nanomedicines,which,resulting from biological fabrication,show an architectonic flexibility unusual among biomaterials.Eric Voltà-Durán Julieta M Sánchez Hèctor-López-Laguna Eloi Parladé Laura Sánchez-García Alejandro Sánchez-Chardi Ario de Marco Ugutz Unzueta Esther Vázquez Antonio Villaverde 2022Science China Materials2022,65,6:0
9Site-directed cysteine coupling of disulfide-containing non-antibody carrier proteins(THIOCAPs)显示文摘The development of a new generation of nonantibody protein drug delivery systems requires site-directed conjugation strategies to produce homogeneous,reproducible and scalable nanomedicines.For that,the genetic addition of cysteine residues into solvent-exposed positions allows the thiol-mediated cysteine coupling of therapeutic drugs into protein-based nanocarriers.However,the high reactivity of unpaired cysteine residues usually reduces protein stability,consequently imposing the use of more methodologically demanding purification procedures.This is especially relevant for disulfide-containing nanocarriers,as previously observed in THIOMABs.Moreover,although many protein scaffolds and targeting ligands are also rich in disulfide bridges,the use of these methodologies over emerging non-antibody carrier proteins has been completely neglected.Here,we report the development of a simple and straightforward procedure for a onestep production and site-directed cysteine conjugation of disulfide-containing non-antibody thiolated carrier proteins(THIOCAPs).This method is validated in a fluorescent C-X-C chemokine receptor 4(CXCR4)-targeted multivalent nanocarrier containing two intramolecular disulfide bridges and one reactive cysteine residue strategically placed into a solvent-exposed position(THIO-T22-GFP-H6)for drug conjugation and in a humanized alternative intended for clinical applications(T22-HSNBT-H6).Thus,we produce very stable,homogeneous and fully functional antitumoral nanoconjugates(THIO-T22-GFP-H6-MMAE and T22-HSNBT-H6-MMAE)that selectively eliminate target cancer cells via CXCR4-receptor.Altogether,the developed methodology appears as a powerful tool for the rational engineering of emerging non-antibody,cell-targeted protein nanocarriers that contain disulfide bridges together with a solvent-exposed reactive cysteine(THIOCAP).This should pave the way for the development of a new generation of stable,homogeneous and efficient nanomedicines.Ariana Rueda Julian I.Mendoza Lorena Alba-Castellon Eloi Parladé Eric Voltà-Durán David Paez Anna Avino Ramon Eritja Esther Vázquez Antonio Villaverde Ramón Mangues Ugutz Unzueta 2023Science China Materials2023,66,10:0
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