Results 251 to 260 of about 25,962 (290)
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Dissociation of macromolecular ribonucleoprotein of yeast
Archives of Biochemistry and Biophysics, 1957Abstract In 0.01 M KH 2 PO 4 K 2 HPO 4 (1:4) the omission of MgSO 4 causes the dissociation of the 80 S particles into two components which have sedimentation coefficients of 60 S and 40 S , respectively. Recombination of the 60 S and 40 S particles to form the 80 S particles takes place when 0.001 M MgSO 4 or 0.001 M CaCl 2 is ...
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Archives of Biochemistry and Biophysics, 1986
A cytoplasmic 10S ribonucleoprotein particle (iRNP), which is isolated from chick embryonic muscle, is a potent inhibitor of mRNA translation in vitro and contains a 4S translation inhibitory RNA species (iRNA). The iRNP particle shows similarity in size to the small nuclear ribonucleoprotein (snRNP) particles.
A M, Boak +4 more
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A cytoplasmic 10S ribonucleoprotein particle (iRNP), which is isolated from chick embryonic muscle, is a potent inhibitor of mRNA translation in vitro and contains a 4S translation inhibitory RNA species (iRNA). The iRNP particle shows similarity in size to the small nuclear ribonucleoprotein (snRNP) particles.
A M, Boak +4 more
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Influenza virus messenger ribonucleoprotein
Virology, 1975Abstract Evidence is presented which indicates that influenza virus messenger RNA exists on polysomes, not as free RNA but in the form of a ribonucleoprotein (RNP). The data make it appear extremely unlikely that the presence of RNP on polysomes is an artifact of the extraction procedure.
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Ribonucleoprotein localization in mouse oocytes
Methods, 2011RNA molecules rarely function alone in cells. For most RNAs, their function requires formation of various ribonucleoprotein (RNP) complexes. For example, mRNP composition can determine mRNA localization, translational repression, level of translation or mRNA stability. RNPs are usually studied by biochemical methods. However, biochemical approaches are
Matyas, Flemr, Petr, Svoboda
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Isolation of messenger-like ribonucleoproteins
Biochemistry, 1975Subribosomal and polyribosomal messenger ribonucleoproteins (mRNPs) were isolated from Ehrlich ascites tumor cells by a method involving sedimentation of polyribosomal and subribosomal particles, dissociation with EDTA, and rate-zonal sedimentation.
A, Barrieux +3 more
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The SMN complex, an assemblyosome of ribonucleoproteins
Current Opinion in Cell Biology, 2002Spinal muscular atrophy is a common, often lethal, neurodegenerative disease that results from low levels of, or loss-of-function mutations in, the SMN (survival of motor neurons) protein. SMN oligomerizes and forms a stable complex with five additional proteins: Gemins 2-6. SMN also interacts with several additional proteins referred to as "substrates"
Paushkin, Sergey +3 more
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Association of viral ribonucleoprotein with polysomes
Experientia, 1969пРИ жАРАжЕНИИ клЕтОк АсцИтНОИ кАРцИНОМы ЁРлИхА ВИРУсОМ сЕНДАИ ВИРУсНыИ РИБОНУкл ЕОпРОтЕИД (РНп) ОБНАРУжИВАлсь В цИтОплАжМЕ пО кРАИНЕИ МЕРЕ В тЕЧЕНИЕ 6 ЧАсОВ пОслЕ жАРАжЕНИь. ЧАстИЧНО ДЕпРОтЕИНИжИРОВАН НыИ РНп ОБлАДАлспОсОБН ОстьУ АссОцИИРОВАт ьсь с РИБОсОМАМИ, ОБРАжУь кОМплЕксы с РАжНОИ плАВУЧЕИ плОтНОстьУ (δ=1,41, 1,45, 1,49 И 1,55 g/cm3).
A G, Bukrinskaya, V M, Zhdanov
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Ribonucleoprotein complexes in neurologic diseases
Current Opinion in Neurobiology, 2008Ribonucleoprotein (RNP) complexes regulate the tissue-specific RNA processing and transport that increases the coding capacity of our genome and the ability to respond quickly and precisely to the diverse set of signals. This review focuses on three proteins that are part of RNP complexes in most cells of our body: TAR DNA-binding protein (TDP-43), the
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Ribonucleoprotein of Clostridium perfringens (BP6K)
Archives of Biochemistry and Biophysics, 1953Abstract A procedure has been presented for the isolation and purification of the ribonucleoprotein from lyophilized Clostridium perfringens (BP6K) cells. Separation of the ribonucleoprotein from the desoxyribonucleoprotein was effected by extracting the lyophilized cells with 0.14 M NaCl. The amino acid composition of the purified nucleoprotein was
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Cytodifferentiation induced by ribonucleoproteins
Experientia, 1961S, RANZI, G, GAVAROSI, P, CITTERIO
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