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April 1, 1992Genes & DevelopmentOpen Access

A splicing factor that is inactivated during in vivo heat shock is functionally equivalent to the U4/U6.U5 triple snRNP-specific proteins.

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Population

Extracts prepared from heat-shocked mammalian cells

Design

Preclinical

Authors

UUU UtansBrigham and Women's HospitalSBSven‐Erik BehrensLuther UniversityRLReinhard LührmannMax Planck Institute for Multidisciplinary Sciences

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Overview

Hypothesis-generating for stress-regulated splicing; leaves open validation in human disease models.

Structured PICO

P
Population
Extracts prepared from heat-shocked mammalian cells
I
Intervention
Characterization and partial purification of a protein factor inactivated during in vivo heat shock
O
Outcome
Function of the protein factor in spliceosome formation (assembling U4/U6 and U5 snRNPs into a triple snRNP particle)

Identifies a specific splicing factor inactivated during heat shock that is essential for assembling the [U4/U6.U5] triple snRNP complex in mammalian cells.

Cite This Study

Utans et al. (1992) studied this question.

synapsesocial.com/papers/6a11fe5af460874a04d205afhttps://doi.org/10.1101/gad.6.4.631
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Inactivation of splicing factors in HeLa cells subjected to heat shock1990 · 38 citations
  2. 220S small nuclear ribonucleoprotein U5 shows a surprisingly complex protein composition.1989 · 148 citations
  3. 3Identification, purification, and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor.1989 · 385 citations
  4. 4Purification and characterization of pre-mRNA splicing factor SF2 from HeLa cells.1990 · 362 citations