Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Hypo- and Hyper-Assembly Diseases of RNA-Protein Complexes.

Trends in molecular medicine - 1 Jul 2016

Shukla Siddharth, Parker Roy

Abstract excerpt

A key aspect of cellular function is the proper assembly and utilization of ribonucleoproteins (RNPs). Recent studies have shown that hyper- or hypo-assembly of various RNPs can lead to human diseases. Defects in the formation of RNPs lead to 'RNP hypo-assembly diseases', which can be caused by RNA degradation outcompeting RNP assembly. By contrast, excess RNP assembly, either in higher order RNP granules, or due...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Dwarfism
Share to Dyskeratosis Congenita
Share to Fetal Growth Retardation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hirschsprung Disease

Share to Muscular Atrophy, Spinal

Share to Primary Immunodeficiency Diseases

Share to Ribonucleoproteins

Share to Scoliosis

Source

Open in PubMed Open full text

Identifiers

PMID: 27263464
DOI: 10.1016/j.molmed.2016.05.005
PMCID: PMC4925306

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Hypo- and Hyper-Assembly Diseases of RNA-Protein Complexes.PMID 27263464Read ↗

Defective Ribonucleoproteins, Mistakes in RNA Processing, and Diseases.Semantic proximity Read ↗

Signal Recognition Particle in Human DiseasesSemantic proximity Read ↗

Pathological phase transitions in ALS-FTD impair dynamic RNA-protein granules.Semantic proximity Read ↗

Stress granules, RNA-binding proteins and polyglutamine diseases: too much aggregation?Semantic proximity Read ↗

Short Tandem Repeat Expansions and RNA-Mediated Pathogenesis in Myotonic DystrophySemantic proximity Read ↗

Different alterations in mRNP composition trigger an increase in harmful R-loopsSemantic proximity Read ↗

RNA-Binding Proteins and the Complex Pathophysiology of ALSSemantic proximity Read ↗

Disorders of protein biogenesis and stability.Semantic proximity Read ↗

Dysregulation of RNA-Binding Proteins in Amyotrophic Lateral SclerosisSemantic proximity Read ↗

SMN control of RNP assembly: From post-transcriptional gene regulation to motor neuron diseaseSemantic proximity Read ↗

Connecting the “dots”: RNP granule network in health and diseaseSemantic proximity Read ↗

Riluzole partially restores RNA polymerase III complex assembly in cells expressing the leukodystrophy-causative variant POLR3B R103HSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.