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Javier sancho
Javier sancho
professor of biochemistry, universidad de zaragoza
Bestätigte E-Mail-Adresse bei unizar.es
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Histidine-aromatic interactions in barnase: Elevation of histidine pKa and contribution to protein stability
R Loewenthal, J Sancho, AR Fersht
Journal of molecular biology 224 (3), 759-770, 1992
2691992
Effect of alanine versus glycine in α-helices on protein stability
L Serrano, JL Neira, J Sancho, AR Fersht
Nature Publishing Group 356 (6368), 453-455, 1992
2591992
α-Helix stability in proteins: I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at …
L Serrano, J Sancho, M Hirshberg, AR Fersht
Journal of molecular biology 227 (2), 544-559, 1992
2571992
Flavodoxins: sequence, folding, binding, function and beyond
J Sancho
Cellular and Molecular Life Sciences CMLS 63 (7-8), 855-864, 2006
2082006
Circular dichroism studies of barnase and its mutants: characterization of the contribution of aromatic side chains
S Vuilleumier, J Sancho, R Loewenthal, AR Fersht
Biochemistry 32 (39), 10303-10313, 1993
1961993
Identification of pharmacological chaperones as potential therapeutic agents to treat phenylketonuria
AL Pey, M Ying, N Cremades, A Velazquez-Campoy, T Scherer, B Thöny, ...
The Journal of clinical investigation 118 (8), 2858-2867, 2008
1852008
Small molecule inhibits α-synuclein aggregation, disrupts amyloid fibrils, and prevents degeneration of dopaminergic neurons
J Pujols, S Peña-Díaz, DF Lázaro, F Peccati, F Pinheiro, D González, ...
Proceedings of the National Academy of Sciences 115 (41), 10481-10486, 2018
1752018
Histidine residues at the N-and C-termini of. alpha.-helixes: perturbed pKas and protein stability
J Sancho, L Serrano, AR Fersht
Biochemistry 31 (8), 2253-2258, 1992
1681992
Histidine residues at the N-and C-termini of alpha-helices: perturbed pKas and protein stability.
J Sancho, L Serrano, AR Fersht
Biochemistry 31 (8), 2253-2258, 1992
1681992
Fluorescence spectrum of barnase: contributions of three tryptophan residues and a histidine-related pH dependence
R Loewenthal, J Sancho, AR Fersht
Biochemistry 30 (27), 6775-6779, 1991
1661991
Miglustat (NB-DNJ) works as a chaperone for mutated acid β-glucosidase in cells transfected with several Gaucher disease mutations
P Alfonso, S Pampín, J Estrada, JC Rodríguez-Rey, P Giraldo, J Sancho, ...
Blood Cells, Molecules, and Diseases 35 (2), 268-276, 2005
1572005
The tryptophan/histidine interaction in α-helices
J Fernández-Recio, A Vázquez, C Civera, P Sevilla, J Sancho
Journal of molecular biology 267 (1), 184-197, 1997
1151997
Long-range surface charge-charge interactions in proteins: comparison of experimental results with calculations from a theoretical method
R Loewenthal, J Sancho, T Reinikainen, AR Fersht
Journal of molecular biology 232 (2), 574-583, 1993
1131993
Differential stabilization of the three FMN redox forms by tyrosine 94 and tryptophan 57 in flavodoxin from Anabaena and its influence on the redox potentials
A Lostao, C Gómez-Moreno, SG Mayhew, J Sancho
Biochemistry 36 (47), 14334-14344, 1997
1121997
The active site of pepsin is formed in the intermediate conformation dominant at mildly acidic pH
LA Campos, J Sancho
FEBS letters 538 (1-3), 89-95, 2003
1112003
The tryptophan/histidine interaction in α-helices
J Fernández-Recio, A Vázquez, C Civera, P Sevilla, J Sancho
Journal of molecular biology 267 (1), 184-197, 1997
1091997
An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate
J Sancho, JL Neira, AR Fersht
Journal of molecular biology 224 (3), 749-758, 1992
1081992
Closure of a tyrosine/tryptophan aromatic gate leads to a compact fold in apo flavodoxin
CG Genzor, A Perales-Alcón, J Sancho, A Romero
Nature structural biology 3 (4), 329-332, 1996
1061996
Closure of a tyrosine/tryptophan aromatic gate leads to a compact fold in apo flavodoxin
CG Genzor, A Perales-Alcón, J Sancho, A Romero
Nature structural biology 3 (4), 329-332, 1996
1061996
Dissection of an enzyme by protein engineering: The N and C-terminal fragments of barnase form a native-like complex with restored enzymic activity
J Sancho, AR Fersht
Journal of molecular biology 224 (3), 741-747, 1992
1021992
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