Results 201 to 210 of about 27,012 (233)

New oxaanalogues of spermine

Russian Journal of Bioorganic Chemistry, 2005
A new isosteric charge-deficient spermine analogue, 1,12-diamino-4,9-diaza-5-oxadodecan, and O-(7-amino-4-azaheptyl)oxime of 3-aminopropanal, a stable analogue of the Schiff base intermediate in the enzymatic oxidation of spermine, were synthesized. The possible use of these compounds for the inhibition of spermine oxidase is discussed.
A R, Khomutov, A R, Simonian, J, Vespalainen, T A, Keinanen, L, Alhonen, J, Janne   +5 more
openaire   +2 more sources

Interaction of spermine and DNA

Biopolymers, 1967
AbstractThe effect of spermine upon the denaturation temperature (Tm) of DNA's of various base compositions has been found to depend upon both the base composition of the DNA and the pH of the solution. Measurement of the hydrogen ion titration curve of spermine as a function of temperature reveals that the net charge of the spermine molecule is ...
S, Hirschman, M, Leng, G, Felsenfield
openaire   +2 more sources

Spermine accumulation under salt stress

Journal of Plant Physiology, 2004
Polyamines have long been recognized to be linked to stress situations, and it is generally accepted that they have protective characteristics. However, little is known about their physiological relevance in plants subjected to long-term salt stress.
Santiago, Maiale, Diego H, Sánchez, Alejandra, Guirado, Alfonso, Vidal, Oscar A, Ruiz   +4 more
openaire   +2 more sources

Spermine Metabolism and Anticancer Therapy

Current Cancer Drug Targets, 2009
The natural polyamines (PA), putrescine (PUT), spermidine (SPD) and spermine (SPM) are ubiquitous constituents of eukaryotic cells. The increase of PA in malignant and proliferating cells attracted the interest of scientists during last decades, addressing PA depletion as a new strategy to inhibit cell growth. Selective enzyme inhibitors were developed
Amendola, R., Cervelli, M., Fratini, E., Polticelli, F., Sallustio, D., Mariottini, P.   +5 more
openaire   +2 more sources

Spermine oxidase: ten years after

Amino Acids, 2011
Spermine oxidase (SMO) was discovered much more recently than other enzymes involved in polyamine metabolism; this review summarizes 10 years of researches on this enzyme. Spermine oxidase (SMO) is a FAD-dependent enzyme that specifically oxidizes spermine (Spm) and plays a dominant role in the highly regulated mammalian polyamines catabolism.
CERVELLI, MANUELA, Amendola R, POLTICELLI, Fabio, MARIOTTINI, Paolo   +3 more
openaire   +3 more sources

Spermine-dialdehyde

Reactions Weekly, 2023
openaire   +1 more source

Spermine

Scientific American, 1889
openaire   +1 more source

Spermine

Cold Spring Harbor Protocols, 2006
openaire   +1 more source

SPERMINE

1967
TADEUSZ KORZYBSKI, ZUZANNA KOWSZYK-GINDIFER, WŁODZIMIERZ KURYŁOWICZ   +2 more
openaire   +1 more source

Spermine as antisecretory agent

Digestive Diseases and Sciences, 1987
T K, Ray, J, Nandi
openaire   +2 more sources