Y. Guillou

发表

Kinetic resolution of peptide bond and side chain far-UV circular dichroism during the folding of hen egg white lysozyme.

A. Chaffotte, M. Goldberg, Y. Guillou, 1992, Biochemistry.

Fourier transform infrared investigation of the Escherichia coli methionine aporepressor.

H. Mantsch, O. Bârzu, I. Saint-Girons, 1987, Biochemistry.

Reversible dissociation of aspartokinase I/homoserine dehydrogenase I from Escherichia coli K 12. The active species is the tetramer.

G. Cohen, Y. Guillou, M. Véron, 1985, European journal of biochemistry.

A new phosphagen, N'-phosphorylguanidinoethylphospho-O-( -N,N-dimethyl)serine (phosphothalassemine).

Y. Guillou, Y. Robin, N. van Thoai, 1972, Biochemistry.

Interactions of DNA-binding proteins with the 5' region of the human transferrin gene.

S. Cereghini, G. Cohen, M. Zakin, 1988, The Journal of biological chemistry.

Inclusion bodies of the thermophilic endoglucanase D from Clostridium thermocellum are made of native enzyme that resists 8 M urea.

A. Chaffotte, M. Goldberg, Y. Guillou, 1992, European journal of biochemistry.

A spermatozoa-specific isoenzyme of arginine kinase in sabellid worms. Biochemical and immunological comparison with muscle enzyme.

C. Klotz, Y. Guillou, Y. Benyamin, 1975, Comparative biochemistry and physiology. B, Comparative biochemistry.

An ion-exchange column chromatographic method for the isolation of octopine from Sepia officinalis L. muscle.

Y. Guillou, Y. Robin, 1977, Analytical biochemistry.

Lack of coupling between secondary structure formation and collapse in a model polypeptide that mimics early folding intermediates, the F2 fragment of the Escherichia coli tryptophan‐synthase β chain

A. Chaffotte, M. Goldberg, Y. Guillou, 1997, Protein science : a publication of the Protein Society.

Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozyme

Y. Guillou, M. E. Goldberg, 1994, Protein science : a publication of the Protein Society.

Phascoline and Phascolosomine:New Catabolic Products of Pyrimidines in Sipunculid Worms

Y. Guillou, Y. Robin, 1989 .

Phascoline (N-(3-guanidinopropionyl)-2-hydroxy-n-heptylamine) and phascolosomine (N-(3-guanidinoisobutyryl)-2-methoxy-n-heptylamine), two new guanidino compounds from sipunculid worms. Isolation and structure.

Y. Guillou, Y. Robin, 1973, The Journal of biological chemistry.

A possible initial folding intermediate: the C-terminal proteolytic domain of tryptophan synthase beta chains folds in less than 4 milliseconds into a condensed state with non-native-like secondary structure.

A. Chaffotte, M. Goldberg, Y. Guillou, 1992, Biochemistry.

Operator-constitutive mutations of the Escherichia coli metF gene

I. Saint Girons, Y. Guillou, D. Perrin, 1987, Journal of Bacteriology.

Crystallization of the met repressor from Escherichia coli.

S. Phillips, J. Rafferty, I. Saint-Girons, 1988, Journal of molecular biology.

Interactions of the Escherichia coli methionine repressor with the metF operator and with its corepressor, S-adenosylmethionine.

G N Cohen, O. Bârzu, I. Saint-Girons, 1986, The Journal of biological chemistry.

A hybrid proteolytic fragment of Escherichia coli aspartokinase I-homoserine dehydrogenase I. Structure, inhibition pattern, dissociation properties, and generation of two homodimers.

G. Cohen, Y. Guillou, A. Fazel, 1983, The Journal of biological chemistry.

Importance of Residues 2–9 in the Immunoreactivity, Subunit Interactions, and Activity of the β2 Subunit of Escherichia coli Tryptophan Synthase (*)

B. Friguet, M. Goldberg, F. Baleux, 1995, The Journal of Biological Chemistry.

The “Pre-Molten Globule,” a New Intermediate in Protein Folding

M. Delepierre, A. Chaffotte, Y. Guillou, 1997, Journal of protein chemistry.

Isolation of the aspartokinase domain of bifunctional aspartokinase I‐homoserine dehydrogenase I from E.coli K12

G. Cohen, Y. Guillou, M. Véron, 1985, FEBS letters.

The isolated C-terminal (F2) fragment of the Escherichia coli tryptophan synthase beta 2-subunit folds into a stable, organized nonnative conformation.

M. Delepierre, A. Chaffotte, M. Goldberg, 1991, Biochemistry.