Results 11 to 20 of about 144,340 (386)

Ribonucleoprotein Immunoprecipitation (RIP) Analysis [PDF]

open access: yesBio-Protocol, 2020
RNAs and RNA-binding proteins (RBPs) can interact dynamically in ribonucleoprotein (RNP) complexes that play important roles in controlling gene expression programs.
Jennifer Martindale   +2 more
doaj   +4 more sources

The Ribonucleoprotein Csr Network [PDF]

open access: yesInternational Journal of Molecular Sciences, 2013
Ribonucleoprotein complexes are essential regulatory components in bacteria. In this review, we focus on the carbon storage regulator (Csr) network, which is well conserved in the bacterial world. This regulatory network is composed of the CsrA master regulator, its targets and regulators.
Seyll, Ethel, Van Melderen, Laurence
openaire   +4 more sources

Ribonucleoprotein bodies are phased in [PDF]

open access: yesBiochemical Society Transactions, 2016
Intracellular compartments are necessary for the regulation of many biochemical processes that ensure cell survival, growth and proliferation. Compartmentalisation is commonly achieved in organelles with defined lipid membranes, such as mitochondria, endoplasmic reticulum or the Golgi apparatus. While these organelles are responsible for many localised
Sfakianos, Aristeidis   +2 more
openaire   +2 more sources

Ribonucleoprotein complexes as autoantigens [PDF]

open access: yesCurrent Opinion in Immunology, 1995
Many intracellular proteins and nucleic acids, that are involved in important biosynthetic pathways, are targeted by autoantibodies occurring spontaneously in the sera of patients with systemic autoimmune diseases. Frequently, the autoantigens are assembled into multicomponent complexes containing both nucleic acid(s) and proteins.
Venrooij, W.J. van, Pruijn, G.J.M.
openaire   +4 more sources

Dilute phase oligomerization can oppose phase separation and modulate material properties of a ribonucleoprotein condensate

open access: yesbioRxiv, 2021
Ribonucleoprotein bodies are exemplars of membraneless biomolecular condensates that can form via spontaneous or driven phase transitions. The fungal protein Whi3 forms ribonucleoprotein condensates with different RNA molecules, and these condensates are
Ian Seim   +6 more
semanticscholar   +1 more source

From Capsids to Complexes: Expanding the Role of TRIM5α in the Restriction of Divergent RNA Viruses and Elements

open access: yesViruses, 2021
An evolutionary arms race has been ongoing between retroviruses and their primate hosts for millions of years. Within the last century, a zoonotic transmission introduced the Human Immunodeficiency Virus (HIV-1), a retrovirus, to the human population ...
Kevin M. Rose   +6 more
doaj   +1 more source

Structure of spliceosomal ribonucleoproteins [PDF]

open access: yesF1000 Biology Reports, 2010
Splicing of the precursors of eukaryotic mRNA and some non-coding RNAs is catalyzed by the 'spliceosome', which comprises five RNA-protein complexes (small nuclear ribonucleoproteins, or snRNPs) that assemble in an ordered manner onto precursor-mRNAs. Much progress has been made in determining the gross morphology of spliceosomal assembly intermediates.
Kiyoshi Nagai   +2 more
openaire   +3 more sources

Approaches to Identify and Characterise the Post-Transcriptional Roles of lncRNAs in Cancer

open access: yesNon-Coding RNA, 2021
It is becoming increasingly evident that the non-coding genome and transcriptome exert great influence over their coding counterparts through complex molecular interactions.
Jean-Michel Carter   +4 more
doaj   +1 more source

Membrane surfaces regulate assembly of a ribonucleoprotein condensate

open access: yesbioRxiv, 2021
Biomolecular condensates organize biochemistry in time and space, yet little is known about how cells control either the position or scale of these assemblies. In cells, condensates often appear as dispersed, relatively small assemblies that do not grow (
W. T. Snead   +4 more
semanticscholar   +1 more source

Ribonucleoprotein multimers and their functions [PDF]

open access: yesCritical Reviews in Biochemistry and Molecular Biology, 2010
Ribonucleoproteins (RNPs) play key roles in many cellular processes and often function as RNP enzymes. Similar to proteins, some of these RNPs exist and function as multimers, either homomeric or heteromeric. While in some cases the mechanistic function of multimerization is well understood, the functional consequences of multimerization of other RNPs ...
Franziska Bleichert, Susan J. Baserga
openaire   +2 more sources

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