D
Dario Neri
Researcher at École Polytechnique Fédérale de Lausanne
Publications - 577
Citations - 29859
Dario Neri is an academic researcher from École Polytechnique Fédérale de Lausanne. The author has contributed to research in topics: Antibody & Antigen. The author has an hindex of 85, co-authored 558 publications receiving 26922 citations. Previous affiliations of Dario Neri include Medical Research Council & Mario Negri Institute for Pharmacological Research.
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Interfering with pH regulation in tumours as a therapeutic strategy
Dario Neri,Claudiu T. Supuran +1 more
TL;DR: Key pH regulators in tumour cells include: isoforms 2, 9 and 12 of carbonic anhydrase, isoforms of anion exchangers, Na+/HCO3− co-transporters, Na+./H+ exchanger, monocarboxylate transporters and the vacuolar ATPase.
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Tumour vascular targeting
Dario Neri,Roy Bicknell +1 more
TL;DR: Evidence that vascular targeting is an effective antitumour strategy in animal models is presented, strategies for identifying putative tumour vascular targets are described and future prospects for vascular targeting in the clinic are discussed.
Journal ArticleDOI
Design and Use of a Phage Display Library: HUMAN ANTIBODIES WITH SUBNANOMOLAR AFFINITY AGAINST A MARKER OF ANGIOGENESIS ELUTED FROM A TWO-DIMENSIONAL GEL *
Alessandro Pini,Francesca Viti,Annalisa Santucci,Barbara Carnemolla,Luciano Zardi,Paolo Neri,Dario Neri +6 more
TL;DR: A large repertoire of functional antibodies with similar properties was produced by appending short variable complementarity-determining region 3 (CDR3) onto the two antibody germ line segments most frequently found in human antibodies by concentrating sequence diversity in regions of the antibody structure that are centrally located in the antigen binding site.
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Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling.
TL;DR: Experience gained with the present project and a previous application of the same principles with the cyclic polypeptide cyclosporin A provides a basis for the selection of the optimal NMR experiments to be used in conjunction with biosynthetic fractional 13C labeling of proteins and peptides.
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NMR determination of residual structure in a urea-denatured protein, the 434-repressor.
TL;DR: A nuclear magnetic resonance (NMR) structure determination is reported for the polypeptide chain of a globular protein in strongly denaturing solution and a model for the early phase of refolding of the 434-repressor(1-63) is proposed.