about
An aberrant phase transition of stress granules triggered by misfolded protein and prevented by chaperone function.Granulostasis: Protein Quality Control of RNP Granules.Assembly of the U5 snRNP component PRPF8 is controlled by the HSP90/R2TP chaperones.Promiscuous interactions and protein disaggregases determine the material state of stress-inducible RNP granules.A Surveillance Function of the HSPB8-BAG3-HSP70 Chaperone Complex Ensures Stress Granule Integrity and Dynamism.Retinitis pigmentosa mutations of SNRNP200 enhance cryptic splice-site recognition.SART3-Dependent Accumulation of Incomplete Spliceosomal snRNPs in Cajal Bodies
P50
Q33795104-833AB547-9767-43AB-B62D-A7D331D00047Q34555053-2E1F67E9-0F85-40EA-B357-25825ADF1D5EQ38780090-7939809B-BF78-44E4-87AD-05B00D8228BEQ42208957-8A5744E0-74FF-4D78-950A-D27C317ECBD7Q51545556-D9154F05-A9A7-4E5D-A9FF-F1AFD3EC48B9Q55057536-0B76192B-A58A-475B-9664-65DCD18454E0Q86557491-8C0F5B0D-FEB1-44AA-8DFB-A14305886D90
P50
description
onderzoeker
@nl
researcher ORCID ID = 0000-0002-3220-1443
@en
name
Daniel Mateju
@ast
Daniel Mateju
@en
Daniel Mateju
@es
Daniel Mateju
@nl
type
label
Daniel Mateju
@ast
Daniel Mateju
@en
Daniel Mateju
@es
Daniel Mateju
@nl
prefLabel
Daniel Mateju
@ast
Daniel Mateju
@en
Daniel Mateju
@es
Daniel Mateju
@nl
P106
P166
P21
P31
P496
0000-0002-3220-1443