Results 141 to 150 of about 3,470 (173)

Methionine restriction in cancer: a dietary insight for therapy. [PDF]

Front Nutr
Tian X, Zhu G, Zhang Y, Liu N.
europepmc   +1 more source

Homocysteine Attack on Vascular Endothelium-Old and New Features. [PDF]

Int J Mol Sci
Hurjui LL, Tarniceriu CC, Serban DN, Lozneanu L, Bordeianu G, Nedelcu AH, Panzariu AC, Jipu R, Hurjui RM, Tanase DM, Serban IL.   +10 more
europepmc   +1 more source

Genomic and phenotypic insights into quorum sensing-mediated spoilage of Morganella psychrotolerans isolated from tuna. [PDF]

NPJ Sci Food
Wang D, Wang Y, Yu G, Ma Z, Wei Y, Li C, Wang Y, Chen S, Shen C, Zhao Y.   +9 more
europepmc   +1 more source

Anticancer Activity of Enantiomeric Neplanocins A: Exploring the Role of Chirality in Tumor Suppression. [PDF]

Int J Mol Sci
Pawlowska R, Banaszkiewicz H, Chworos A, Żurawiński R.   +3 more
europepmc   +1 more source

Methionine cycle inhibition disrupts antioxidant metabolism and reduces glioblastoma cell survival. [PDF]

J Biol Chem
Rowland EC, D'Antuono M, Jermakowicz AM, Ayad NG.   +3 more
europepmc   +1 more source

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Adenosylhomocysteinase from Yellow Lupin Seeds

European Journal of Biochemistry, 1977
Adenosylhomocysteinase from yellow lupin seeds (Lupinus luteus) has been purified to homogeneity.Active enzyme, Mr= 110 000, consists of two probably identical subunits with Mr= 55 000 as judged by gel filtration and dodecyl sulphate/polyacrylamide gel electrophoresis in the presence of 2‐mercaptoethanol.
A, Guranowski, J, Pawelkiewicz
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Adenosylhomocysteinase:Adenosine complex

Biochemical and Biophysical Research Communications, 1978
Adenosylhomocysteinase from yellow lupin seeds forms a specific complex with adenosine. The complex can be isolated either by nonequilibrium or equilibrium gel filtration. It is also adsorbed on nitrocellulose disks. Dissociation constant of the complex determined by nitrocellulose filter assay is 5 × 10−8M.
H, Jakubowski, A, Guranowski
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Molecular characterisation of adenosylhomocysteinase from Trichomonas vaginalis

Molecular and Biochemical Parasitology, 1996
The enzyme S-adenosylhomocysteine hydrolase (SAHH) has been identified as a potential target for chemotherapy in protozoan parasites including Trichomonas vaginalis. To investigate this area of trichomonad metabolism in more detail, we have isolated and characterised a gene which encodes this activity from the WAA38 strain of this parasite.
A S, Bagnara, V E, Tucker, L, Minotto, E R, Howes, G A, Ko, M R, Edwards, I W, Dawes   +6 more
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Trichomonas vaginalis:Expression and Characterisation of RecombinantS-Adenosylhomocysteinase

Experimental Parasitology, 1998
The gene encoding S-adenosylhomocysteinase activity (S-adenosylhomocysteine hydrolase, SAHH; EC 3.3.1.1) in Trichomonas vaginalis has been expressed in Escherichia coli to facilitate the characterisation of the enzyme. Expression of this gene using the pQE-30 (6xHis N-terminal tag) expression system (QIAGEN) has enabled the one-step purification of 6 ...
L, Minotto, G A, Ko, M R, Edwards, A S, Bagnara   +3 more
openaire   +2 more sources