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Conformational and molecular responses to pH variation of the purified membrane adenosine triphosphatase of Micrococcus lysodeikticus.
Nieto M, Muñoz E, Carreira J, Andreu JM. Nieto M, et al. Among authors: munoz e. Biochim Biophys Acta. 1975 Dec 16;413(3):394-414. doi: 10.1016/0005-2736(75)90123-6. Biochim Biophys Acta. 1975. PMID: 91
Polymorphism and conformational dynamics of F1-ATPases from bacterial membranes. A model for the regulation of these enzymes on the basis of molecular plasticity.
Muñoz E. Muñoz E. Biochim Biophys Acta. 1982 May 12;650(4):233-65. doi: 10.1016/0304-4157(82)90018-1. Biochim Biophys Acta. 1982. PMID: 6178434 Review. No abstract available.
Molecular organization in bacterial cell membranes. I. Sodium dodecyl sulphate solubilization and fractionation of the components of a depleted membrane from Micrococcus lysodeikticus.
Estrugo SF, Larraga V, Corrales MA, Duch C, Muñoz E. Estrugo SF, et al. Among authors: munoz e. Biochim Biophys Acta. 1972 Mar 17;255(3):960-73. doi: 10.1016/0005-2736(72)90406-3. Biochim Biophys Acta. 1972. PMID: 5020232 No abstract available.
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.
Larraga V, Nieto M, Muñoz E. Larraga V, et al. Among authors: munoz e. Biochim Biophys Acta. 1974 Aug 21;363(1):26-38. doi: 10.1016/0005-2736(74)90004-2. Biochim Biophys Acta. 1974. PMID: 4853248 No abstract available.
Membrane ATPase of Escherichia coli K 12. Selective solubilization of the enzyme and its stimulation by trypsin in the soluble and membrane-bound states.
Carreira J, Leal JA, Rojas M, Muñoz E. Carreira J, et al. Among authors: munoz e. Biochim Biophys Acta. 1973 May 25;307(3):541-56. doi: 10.1016/0005-2736(73)90299-x. Biochim Biophys Acta. 1973. PMID: 4268887 No abstract available.
The effect of low concentrations of glutaraldehyde on Micrococcus lysodeikticus membranes: changes in the release of membrane-associated enzymes and membrane structure.
Ellar DJ, Muñoz E, Salton MR. Ellar DJ, et al. Among authors: munoz e. Biochim Biophys Acta. 1971 Jan 5;225(1):140-50. doi: 10.1016/0005-2736(71)90292-6. Biochim Biophys Acta. 1971. PMID: 4250836 No abstract available.
Molecular organization in bacterial cell membranes. 3. Components of a "soluble" fraction obtained by n-butanol extraction of Streptomyces albus membranes.
Larraga V, Muñoz E. Larraga V, et al. Among authors: munoz e. Biochim Biophys Acta. 1974 Aug 21;363(1):9-25. doi: 10.1016/0005-2736(74)90003-0. Biochim Biophys Acta. 1974. PMID: 4137065 No abstract available.
Molecular organization in bacterial cell membranes. II. Reevaluation and identification of some chemical components of Micrococcus lysodeikticus membranes.
Estrugo SF, Coll J, Leal JA, Muñoz E. Estrugo SF, et al. Among authors: munoz e. Biochim Biophys Acta. 1973 Jun 22;311(2):153-62. doi: 10.1016/0005-2736(73)90262-9. Biochim Biophys Acta. 1973. PMID: 4197962 No abstract available.
Membrane adenosine triphosphatase of Micrococcus lysodeikticus. Purification, properties of the "soluble" enzyme and properties of the membrane-bound enzyme.
Muñoz E, Salton MR, Ng MH, Schor MT. Muñoz E, et al. Eur J Biochem. 1969 Feb;7(4):490-501. Eur J Biochem. 1969. PMID: 4237904 No abstract available.
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.
Ayala J, Carreira J, Nieto M, Muñoz E. Ayala J, et al. Among authors: munoz e. Mol Cell Biochem. 1977 Aug 19;17(1):17-23. doi: 10.1007/BF01732550. Mol Cell Biochem. 1977. PMID: 143600
Both forms underwent changes in their molecular properties as a consequence of being enzymically active, i.e., upon incubation with substrates at an adequate temperature. ...
Both forms underwent changes in their molecular properties as a consequence of being enzymically active, i.e., upon incubation with s …
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