Results 251 to 260 of about 24,238 (294)
Some of the next articles are maybe not open access.

The Phlebovirus Ribonucleoprotein: An Overview

In negative strand RNA viruses, ribonucleoproteins, not naked RNA, constitute the template used by the large protein endowed with polymerase activity for replicating and transcribing the viral genome. Here we give an overview of the structures and functions of the ribonucleoprotein from phleboviruses.
Ferron, François, Lescar, Julien
openaire   +3 more sources

Association of viral ribonucleoprotein with polysomes

Experientia, 1969
пРИ 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
openaire   +2 more sources

Ribonucleoprotein complexes in neurologic diseases

Current Opinion in Neurobiology, 2008
Ribonucleoprotein (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
openaire   +2 more sources

A Ribonucleoprotein from Amphibian Gastrulæ

Nature, 1958
DISAGGREGATION of amphibian embryos by agents which chelate calcium is succeeded by re-aggregation if the cells are returned to a medium containing calcium1. It is customary to consider that the removal of calcium from the environment of the cells is responsible for the loss of adhesion displayed in disaggregation.
openaire   +2 more sources

Ribonucleoprotein interaction with mammalian monosomes

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1968
Abstract A subcellular fraction containing RNA and protein was prepared from rabbit reticulocytes. This fraction had a sedimentation behavior which was different from reticulocyte ribosomal subunits, and was capable of stimulating polypeptide synthesis in a mammalian cell-free system.
S A, Armentrout, A S, Weisberger
openaire   +2 more sources

Small nuclear ribonucleoprotein antigens are absent from 10S translation inhibitory ribonucleoprotein but present in cytoplasmic messenger ribonucleoprotein and polysomes

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
openaire   +2 more sources

Ribonucleoprotein localization in mouse oocytes

Methods, 2011
RNA 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
openaire   +2 more sources

Dissociation of macromolecular ribonucleoprotein of yeast

Archives of Biochemistry and Biophysics, 1957
Abstract 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 ...
openaire   +2 more sources

Heterogeneous nuclear ribonucleoprotein complexes

Molecular Biology Reports, 1990
Heterogeneous nuclear r ibonuc leopro te ins (hnRNPs) associate with RNA polymerase II transcripts immediately following the initiation of transcription to form hnRNP complexes. These structures are the functional assemblies within which hnRNAs and pre-mRNAs exist in the nucleus.
openaire   +2 more sources

Isolation of messenger-like ribonucleoproteins

Biochemistry, 1975
Subribosomal 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
openaire   +2 more sources

Home - About - Disclaimer - Privacy