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7篇 您的检索式:作者名="Volt H"
    题名 作者 年代 出处 被引量
1Random number generation from right- skewed, symmetric, and left-skewed distributions显示文摘Volt E O Schwacke L H 2000Risk Analysis2000,20,:1
2Function of the intrathoracic stomach as esophageal replacement显示文摘HOLSCHER A H VOlT H BUTTERMANN G 1988World J Surg1988,12,6:1
3Hyperbranched thermolabile polycarbonates derived from a A2+ B3 monomer system显示文摘Scheel A Komber H Volt B 2004Macromol Syrup2004,210,1:1
4Function of the intrathoracic stomach- as esophageal replacement 显示文摘Holscher AH Volt H Buttermann G 1998World J surg1998,12,7:1
5Safety and efficacy of drisapersen for the treatment of Duchenne muscular dystrophy ( DEMAND II ): an exploratory, randomised, placebo- controlled phase 2 study显示文摘Volt T Topaloglu H Straub V 2014Lancet Neurol2014,13,10:1
6All-aromatic hyperbranched polyesters with phenol and acetate end groups: synthesis and characterization 显示文摘RICHARD TURNER S BRIGITYE I VOLT THOMAS H MOUREY 1993Macromolecules1993,26,17:1
7The 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
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