J. Zurdo

发表

Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

C. Dobson, M. Bucciantini, E. Giannoni, 2002, Nature.

Protein engineering as a strategy to avoid formation of amyloid fibrils

L Serrano, C M Dobson, C. Dobson, 2000, Protein science : a publication of the Protein Society.

Short amino acid stretches can mediate amyloid formation in globular proteins: the Src homology 3 (SH3) case.

Salvador Ventura, Fabrizio Chiti, Francesc X Aviles, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases.

Michele Vendruscolo, Fabrizio Chiti, Christopher M Dobson, 2005, Journal of molecular biology.

Aggregation risk prediction for antibodies and its application to biotherapeutic development

Olga Obrezanova, Andreas Arnell, J. Zurdo, 2015, mAbs.

Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains.

Michele Vendruscolo, Fabrizio Chiti, Christopher M Dobson, 2004, Journal of molecular biology.

Enhancement of carotenoid-to-chlorophyll singlet energy transfer by carotenoid-carotenoid interaction.

J. Zurdo, J. Ramirez, C. Fernández-Cabrera, 1992, Biophysical journal.

The structural role of the carotenoid in the bacterial light-harvesting protein 2 (LH2) of Rhodonbacter capsulatus. A Fourier transform Raman spectroscopy and circular dichroism study

J. Zurdo, J. Odriozola, M. A. Centeno, 1995, Photosynthesis Research.

Assembly of Saccharomyces cerevisiae ribosomal stalk: binding of P1 proteins is required for the interaction of P2 proteins.

J. Ballesta, M. Remacha, J. Zurdo, 2000, Biochemistry.

De novo designed peptide-based amyloid fibrils

Andreas Hoenger, Luis Serrano, Christopher M Dobson, 2002, Proceedings of the National Academy of Sciences of the United States of America.

Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis.

P E Fraser, L. Serpell, P. Fraser, 2001, Journal of molecular biology.

A structural role of the carotenoid in the light-harvesting II protein of Rhodobacter capsulatus.

J. Zurdo, C. Fernández-Cabrera, J. Ramírez, 1993, The Biochemical journal.

Cryo‐electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing

Elena Orlova, C. Dobson, E. Orlova, 1999, The EMBO journal.

Developability assessment as an early de-risking tool for biopharmaceutical development

J. Zurdo, Jesús Zurdo, 2013 .

Protein folding and misfolding: a paradigm of self–assembly and regulation in complex biological systems

Michele Vendruscolo, Christopher M Dobson, Jesús Zurdo, 2003, Philosophical Transactions of the Royal Society of London. Series A: Mathematical, Physical and Engineering Sciences.

Protein aggregation and amyloid fibril formation by an SH3 domain probed by limited proteolysis.

C. Dobson, F. Chiti, J. Zurdo, 2003, Journal of molecular biology.

Transition from Natively Unfolded to Folded State Induced by Desiccation in an Anhydrobiotic Nematode Protein*

J. Zurdo, A. Tunnacliffe, J. Browne, 2003, The Journal of Biological Chemistry.

Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy

C M Dobson, C. Dobson, C. Robinson, 2000, Protein science : a publication of the Protein Society.

Rational design of aggregation-resistant bioactive peptides: reengineering human calcitonin.

C. Dobson, F. Chiti, J. Zurdo, 2005, Proceedings of the National Academy of Sciences of the United States of America.

Ultrastructural organization of amyloid fibrils by atomic force microscopy.

C M Dobson, C. Dobson, J. Zurdo, 2000, Biophysical journal.

Molecular recycling within amyloid fibrils

Christopher M. Dobson, Ernest Giralt, Carol V. Robinson, 2005, Nature.

Amyloid fibril formation and seeding by wild-type human lysozyme and its disease-related mutational variants.

C. Dobson, J. Zurdo, V. Receveur, 2000, Journal of structural biology.

Preparation and characterization of purified amyloid fibrils.

C. Dobson, J. Zurdo, J. Guijarro, 2001, Journal of the American Chemical Society.

A highly amyloidogenic region of hen lysozyme.

Angelo Fontana, Christopher M Dobson, C. Dobson, 2004, Journal of molecular biology.

Formation and seeding of amyloid fibrils from wild-type hen lysozyme and a peptide fragment from the beta-domain.

C M Dobson, C. Dobson, C. Robinson, 2000, Journal of molecular biology.

Developability Assessment Workflows to De-Risk Biopharmaceutical Development

Noel Smith, Olga Obrezanova, Jesús Zurdo, 2015 .

Early Implementation of QbD in Biopharmaceutical Development: A Practical Example

Olga Obrezanova, Andreas Arnell, Thomas R. A. Gallagher, 2015, BioMed research international.

Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation.

C. Dobson, J. Zurdo, B. Luisi, 2006, Journal of molecular biology.

Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain.

C. Dobson, J. Zurdo, H. Saibil, 2001, Journal of molecular biology.

Amyloidogenicity and aggregate cytotoxicity of human glucagon-like peptide-1 (hGLP-1).

C. Dobson, J. Zurdo, B. Luisi, 2009, Protein and peptide letters.

The exchangeable yeast ribosomal acidic protein YP2beta shows characteristics of a partly folded state under physiological conditions.

J. Ballesta, J. Zurdo, M. Rico, 1997, Biochemistry.

Exploring amyloid formation by a de novo design.

Christopher M Dobson, Shirley A Müller, C. Dobson, 2004, Proceedings of the National Academy of Sciences of the United States of America.

Structure of the Yeast Ribosomal Stalk

J. Ballesta, M. Remacha, J. Zurdo, 2000 .

Competing intrachain interactions regulate the formation of β‐sheet fibrils in bovine PrP peptides

J. Zurdo, W. James, A. Tahiri-Alaoui, 2003, Protein science : a publication of the Protein Society.

Structural differences between Saccharomyces cerevisiae ribosomal stalk proteins P1 and P2 support their functional diversity.

J. Ballesta, M. Remacha, J. Zurdo, 2000, Biochemistry.