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Structural characterization and biological properties of human gastrokine 1.
Pavone LM, Del Vecchio P, Mallardo P, Altieri F, De Pasquale V, Rea S, Martucci NM, Di Stadio CS, Pucci P, Flagiello A, Masullo M, Arcari P, Rippa E. Pavone LM, et al. Among authors: masullo m. Mol Biosyst. 2013 Mar;9(3):412-21. doi: 10.1039/c2mb25308a. Epub 2013 Jan 14. Mol Biosyst. 2013. PMID: 23319233
Expression in Escherichia coli of thermostable elongation factor 1 alpha from the archaeon Sulfolobus solfataricus.
Ianniciello G, Masullo M, Gallo M, Arcari P, Bocchini V. Ianniciello G, et al. Among authors: masullo m. Biotechnol Appl Biochem. 1996 Feb;23(1):41-5. Biotechnol Appl Biochem. 1996. PMID: 8867895
The N-terminal sequence of the first 30 amino acid residues of recSsEF-1 alpha was identical with that translated from the nucleotide sequence of the corresponding gene, except for the initial residue, which in recSsEF-1 alpha was Ser instead of Met. The M(r) of recSsEF-1 …
The N-terminal sequence of the first 30 amino acid residues of recSsEF-1 alpha was identical with that translated from the nucleotide sequen …
A NAD(P)H oxidase isolated from the archaeon Sulfolobus solfataricus is not homologous with another NADH oxidase present in the same microorganism. Biochemical characterization of the enzyme and cloning of the encoding gene.
Arcari P, Masullo L, Masullo M, Catanzano F, Bocchini V. Arcari P, et al. Among authors: masullo l, masullo m. J Biol Chem. 2000 Jan 14;275(2):895-900. doi: 10.1074/jbc.275.2.895. J Biol Chem. 2000. PMID: 10625624 Free article.
A NAD(P)H oxidase has been isolated from the archaeon Sulfolobus solfataricus. The enzyme is a homodimer with M(r) 38,000 per subunit (SsNOX38) containing 1 FAD molecule/subunit. ...The primary structure of SsNOX38 did not show any homology with the N-terminal amino acid s …
A NAD(P)H oxidase has been isolated from the archaeon Sulfolobus solfataricus. The enzyme is a homodimer with M(r) 38,000 per subunit …
Valine 114 replacements in archaeal elongation factor 1 alpha enhanced its ability to interact with aminoacyl-tRNA and kirromycin.
Masullo M, Cantiello P, De Paola B, Fiengo A, Vitagliano L, Zagari A, Arcari P. Masullo M, et al. Biochemistry. 2002 Dec 10;41(49):14482-8. doi: 10.1021/bi026428n. Biochemistry. 2002. PMID: 12463746
This sequence is well-conserved among most of eukaryal and eubacterial counterparts, and in the three-dimensional structure of SsEF-1alpha, V114 is located in a hydrophobic pocket near the first GDP-binding consensus sequence G(13)XXXXGK[T,S] [Vitagliano, L., Masullo, M …
This sequence is well-conserved among most of eukaryal and eubacterial counterparts, and in the three-dimensional structure of SsEF-1alpha, …
249 results