Effect of convulsive seizures on synaptosomal protein synthesis from El mouse —Relationship between protein components and seizure-susceptibility

1989 ◽  
Vol 9 ◽  
pp. 63
Author(s):  
Daisuke Furutsuka ◽  
Sakae Yamagami ◽  
Yukio Kawakita
2020 ◽  
Vol 56 (98) ◽  
pp. 15426-15429
Author(s):  
Kai Libicher ◽  
Hannes Mutschler

Recombinant in vitro translation systems can regenerate essential protein components that maintain protein synthesis during serial dilution.


1996 ◽  
Vol 731 (1-2) ◽  
pp. 190-198 ◽  
Author(s):  
Itsugi Nagatomo ◽  
Yasuaki Akasaki ◽  
Fumihiro Nagase ◽  
Mitsuo Nomaguchi ◽  
Morikuni Takigawa

Biomolecules ◽  
2020 ◽  
Vol 10 (5) ◽  
pp. 783 ◽  
Author(s):  
Sandeep Ojha ◽  
Sulochan Malla ◽  
Shawn M. Lyons

Ribosomes are perhaps the most critical macromolecular machine as they are tasked with carrying out protein synthesis in cells. They are incredibly complex structures composed of protein components and heavily chemically modified RNAs. The task of assembling mature ribosomes from their component parts consumes a massive amount of energy and requires greater than 200 assembly factors. Among the most critical of these are small nucleolar ribonucleoproteins (snoRNPs). These are small RNAs complexed with diverse sets of proteins. As suggested by their name, they localize to the nucleolus, the site of ribosome biogenesis. There, they facilitate multiple roles in ribosomes biogenesis, such as pseudouridylation and 2′-O-methylation of ribosomal (r)RNA, guiding pre-rRNA processing, and acting as molecular chaperones. Here, we reviewed their activity in promoting the assembly of ribosomes in eukaryotes with regards to chemical modification and pre-rRNA processing.


1992 ◽  
Vol 46 (2) ◽  
pp. 529-530 ◽  
Author(s):  
Koji Mui ◽  
Aki Nakanishi ◽  
Sakae Yamagami ◽  
Tetsuro Kioka ◽  
Hiroshi Onishi ◽  
...  

1993 ◽  
Vol 47 (2) ◽  
pp. 380-381 ◽  
Author(s):  
Koji Mui ◽  
Yoko Kuroda ◽  
Aki Nakanishi ◽  
Hiroshi Onishi ◽  
Sakae Yamagami

Parasitology ◽  
1972 ◽  
Vol 65 (1) ◽  
pp. 55-69 ◽  
Author(s):  
J. R. Kusel

Saponin treatment of cercariae and schistosomula alters the surface membrane so that it may be sheared from the organism and isolated as fragments by centrifugation. Saponin-calcium chloride treatment or freezing and thawing of adult worms removes the surface membrane, which can be washed from the bodies and collected by centrifugation. The small quantities of material available necessitated the development of a sensitive technique for detecting the proteins in the membranes. The surface membranes were radioiodinated after butan-1-ol extraction and electrophoresed in polyacrylamide gel. Adult surfaces prepared by the saponin-calcium chloride and by the freezing and thawing technique had identical protein components, detected as gel-cut profiles or in autoradiographs. The quantity of a rapidly migrating PAS-positive amido black negative component was greater in the surfaces prepared by saponincalcium chloride than in the frozen and thawed surfaces. This component contains lipid, some of which may be glycolipid. It was largely absent from the surface membranes of cercariae and schistosomula. Cercarial surface membranes contained a major protein component which was absent from the surface membranes of schistosomula. Otherwise the surface membranes of the cercariae were identical to those of the schistosomula in their protein components. The rate of incorporation of freshly synthesized protein per unit area of surface membrane of schistosomula was very low in the first 5 days in culture, after which there was a very rapid increase to a maximum rate on the 15th day. After this time, the rate of protein synthesis decreased to a low level at 26 days. In these studies the activity per unit area was measured and this would not be expected to vary greatly during growth. The biological significance of the observed variation in protein incorporation into the membrane is unclear.


1998 ◽  
Vol 789 (2) ◽  
pp. 213-220 ◽  
Author(s):  
Itsugi Nagatomo ◽  
Yasuaki Akasaki ◽  
Masahiro Uchida ◽  
Satoshi Kuchiiwa ◽  
Shiro Nakagawa ◽  
...  

Biomolecules ◽  
2020 ◽  
Vol 10 (7) ◽  
pp. 969 ◽  
Author(s):  
Eric Cockman ◽  
Paul Anderson ◽  
Pavel Ivanov

The cellular response to changes in the surrounding environment and to stress requires the coregulation of gene networks aiming to conserve energy and resources. This is often achieved by downregulating protein synthesis. The 5’ Terminal OligoPyrimidine (5’ TOP) motif-containing mRNAs, which encode proteins that are essential for protein synthesis, are the primary targets of translational control under stress. The TOP motif is a cis-regulatory RNA element that begins directly after the m7G cap structure and contains the hallmark invariant 5’-cytidine followed by an uninterrupted tract of 4–15 pyrimidines. Regulation of translation via the TOP motif coordinates global protein synthesis with simultaneous co-expression of the protein components required for ribosome biogenesis. In this review, we discuss architecture of TOP mRNA-containing ribonucleoprotein complexes, the principles of their assembly, and the modes of regulation of TOP mRNA translation.


Biologia ◽  
2006 ◽  
Vol 61 (4) ◽  
Author(s):  
Andrej Kormuťák ◽  
Terézia Salaj ◽  
Božena Vooková

AbstractComposition and accumulation patterns of storage proteins in female gametophyte and embryos of the white fir (Abies concolor) were investigated during embryogenesis and germination of mature seeds using SDS-PAGE and immunological approach. Altogether 9 major and minor protein components with molecular masses of 14, 16, 22, 24, 27, 30, 35, 38, and 43 kDa were detected in female gametophytes and 9 protein bands in the embryos with the molecular sizes of 14, 16, 22, 24, 25, 27, 34, 38, and 43 kDa. The species seems to deviate in this respect from other representatives of Pinaceae. A conspicuous increase of storage protein synthesis was observed at the stage of fully cellularized female gametophytes and at the cotyledonary stage of embryo development. There exists a high degree of similarity between storage protein profiles of white fir zygotic and somatic embryos. Successive stages of somatic embryogenesis exhibited a high degree of similarity of storage proteins except for cotyledonary stage when a noticeable increase in storage protein synthesis was registered. Conversely, during germination of somatic embryos, an overwhelming majority of storage proteins was depleted.


2015 ◽  
Vol 04 (02) ◽  
pp. 067-071 ◽  
Author(s):  
Yoshiya Murashima ◽  
Mitsutoshi Tsukimoto ◽  
Asami Baba ◽  
Chiharu Miyatake ◽  
Tetsuya Okazaki ◽  
...  

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