M. Nieto

发表

Membrane-bound DD-carboxypeptidase and transpeptidase activities from Bacillus megaterium KM at pH 7. General properties, substrate specificity and inhibition by beta-lactam antibiotics.

A. Marquet, T. Díaz-Mauriño, M. Nieto, 1976, European journal of biochemistry.

The active centres in penicillin-sensitive enzymes.

J. Frère, J. Ghuysen, H. Perkins, 1980, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

Physicochemical properties of vancomycin and iodovancomycin and their complexes with diacetyl-L-lysyl-D-alanyl-D-alanine.

H. Perkins, M. Nieto, 1971, Biochemical Journal.

Modifications of the acyl-D-alanyl-D-alanine terminus affecting complex-formation with vancomycin.

H. Perkins, M. Nieto, 1971, The Biochemical journal.

THE CHEMICAL BASIS FOR THE ACTION OF THE VANCOMYCIN GROUP OF ANTIBIOTICS

H. Perkins, M. Nieto, H. R. Perkins, 1974, Annals of the New York Academy of Sciences.

The significance of D-alanyl-D-alanine termini in the biosynthesis of bacterial cell walls and the action of penicillin, vancomycin and ristocetin

H. Perkins, M. Nieto, 1973 .

THE PENICILLIN RECEPTOR IN STREPTOMYCES *

J. Frère, J. Ghuysen, J. Dusart, 1974, Annals of the New York Academy of Sciences.

Structure of the wall peptidoglycan of Streptomyces R39 and the specificity profile of its exocellular DD-carboxypeptidase--transpeptidase for peptide acceptors.

J. Frère, J. Ghuysen, C. Duez, 1973, Biochemistry.

Transpeptidase activity of Streptomyces D-alanyl-D carboxypeptidases.

J. Frère, J. Ghuysen, J. J. Pollock, 1972, Proceedings of the National Academy of Sciences of the United States of America.

Penicillin-sensitive DD-carboxypeptidases from Streptomyces strains R39 and K11.

J. Frère, J. Ghuysen, H. Perkins, 1972, Biochemistry.

On the Streptomyces albus G DD carboxypeptidase mechanism of action of penicillin, vancomycin, and ristocetin.

K. Schleifer, O. Kandler, J. Ghuysen, 1970, Biochemistry.

dd-Carboxypeptidase-Transpeptidase and Killing Site of β-Lactam Antibiotics in Streptomyces Strains R39, R61, and K11

J. Frère, J. Ghuysen, J. Dusart, 1973, Antimicrobial Agents and Chemotherapy.

Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61.

J. Ghuysen, J. Coyette, H. Perkins, 1971, Biochemistry.

Bacterial transpeptidases and penicillin.

J. Frère, J. Ghuysen, J. Dusart, 1975 .

Fluorescence and circular dichroism studies on the Streptomyces R61 DD-carboxypeptidase-transpeptidase. Penicillin binding by the enzyme.

J. Frère, J. Ghuysen, H. Perkins, 1973, The Biochemical journal.

The specificity of combination between ristocetins and peptides related to bacterial cell wall mucopeptide precursors.

H. Perkins, M. Nieto, 1971, The Biochemical journal.

[51] Exocellular dd-carboxypeptidases-transpeptidases from Streptomyces

J. Frère, J. Ghuysen, H. Perkins, 1976 .

Exocellular DD-carboxypeptidases-transpeptidases from Streptomyces.

J. Frère, J. Ghuysen, H. Perkins, 1976, Methods in enzymology.

Molecular weight and amino acid composition of the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61.

J. Frère, J. Ghuysen, H. Perkins, 1973, The Biochemical journal.

Kinetics of concomitant transfer and hydrolysis reactions catalysed by the exocellular DD-carboxypeptidase-transpeptidase of streptomyces R61.

J. Frère, J. Ghuysen, H. Perkins, 1973, The Biochemical journal.

Streptomyces DD-carboxypeptidases as transpeptidases. The specificity for amino compounds acting as carboxyl acceptors.

J. Frère, J. Ghuysen, H. Perkins, 1973, The Biochemical journal.

Peptide inhibitors of Streptomyces DD-carboxypeptidases.

J. Frère, J. Ghuysen, H. Perkins, 1973, The Biochemical journal.

Milk fat globule membranes. Inhibition by sucrose of the alkaline phosphomonoesterase.

T. Díaz-Mauriño, M. Nieto, 1976, Biochimica et biophysica acta.

The preparation of iodinated vancomycin and its distribution in bacteria treated with the antibiotic.

H. Perkins, M. Nieto, 1970, The Biochemical journal.

Prediction of a putative fusion peptide in the S protein of hepatitis B virus.

I. Rodrı́guez-Crespo, F. Gavilanes, D. Peterson, 1994, The Journal of general virology.

Site-directed mutagenesis of cysteine residues of hepatitis B surface antigen. Analysis of two single mutants and the double mutant.

I. Rodrı́guez-Crespo, F. Gavilanes, D. Peterson, 1994, European journal of biochemistry.

TEMPERATURE AND DNA TURNOVER IN THE GOLDFISH

H. Johnson, M. Nieto, 1972, Cell and tissue kinetics.

Micrococcus lysodeikticus membrane ATPase. Effect of trypsin on stimulation of a purified form of the enzyme and idenfification of its natural inhibitor.

J. Andreu, E. Muñoz, J. Carreira, 1976, Biochimica et biophysica acta.

Milk-fat globule membranes: chemical composition and phosphoesterase activities during lactation

T. Díaz-Mauriño, M. Nieto, 1977, Journal of Dairy Research.

Confomational and molecular responses to pH variation of the purified membrane adenosine triphospate of Micrococcus lysodeikticus

J. Andreu, J. Carreira, M. Nieto, 1975 .

Membrane adenosine triphosphatase of Micrococcus lysodeikticus. Isolation of two forms of the enzyme complex and correlation between enzymatic stability, latency and activity.

J. Andreu, E. Muñoz, J. Carreira, 1976, Molecular and Cellular Biochemistry.

PENICILLIN PRODUCTION BY RECOMBINANT STRAINS OF Penicillium chrysogenum OBTAINED BY FUSION OF PROTOPLASTS

J. Martín, I. García-Acha, M. Nieto, 1981 .

Substrate requirements of the Streptomyces albus G DD carboxypeptidase.

K. Schleifer, O. Kandler, J. Ghuysen, 1970, Biochemistry.

Activation parameters and molecular changes induced by substrate hydrolysis of the adenosine triphosphatase of Micrococcus lysodeikticus. A comparison of three different soluble forms of the enzyme

J. Ayala, E. Muñoz, J. Carreira, 1977, Molecular and Cellular Biochemistry.

Activation parameters of the adenosine triphosphatase of Micrococcus lysodeikticus. A comparison of the soluble and membrane-bound forms of the enzyme.

J. Ayala, E. Muñoz, J. Carreira, 1976, European journal of biochemistry.

Molecular organization in bacterial cell membranes. IV. Isolation by preparative electrophoresis in sodium dodecylsulphate and properties of the two major polypeptide groups of a "soluble" fraction from Streptomyces albus membranes.

V. Larraga, E. Muñoz, M. Nieto, 1974, Biochimica et biophysica acta.