about
DVC1 (C1orf124) is a DNA damage-targeting p97 adaptor that promotes ubiquitin-dependent responses to replication blocksUbxd1 is a novel co-factor of the human p97 ATPaseThe tissue-specific Rep8/UBXD6 tethers p97 to the endoplasmic reticulum membrane for degradation of misfolded proteinsMolecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradationProtein quality control in the nucleusFission yeast 26S proteasome mutants are multi-drug resistant due to stabilization of the Pap1 transcription factorA chaperone-assisted degradation pathway targets kinetochore proteins to ensure genome stabilityProteins containing the UBA domain are able to bind to multi-ubiquitin chainsRegulation of NF-kappaB activity and inducible nitric oxide synthase by regulatory particle non-ATPase subunit 13 (Rpn13).Individual cell motility studied by time-lapse video recording: influence of experimental conditions.Ubiquitin domain proteins in disease.Proteasome nuclear import mediated by Arc3 can influence efficient DNA damage repair and mitosis in Schizosaccharomyces pombe.The proteasome cap RPT5/Rpt5p subunit prevents aggregation of unfolded ricin A chain.HUWE1 and TRIP12 collaborate in degradation of ubiquitin-fusion proteins and misframed ubiquitin.Adrm1, a putative cell adhesion regulating protein, is a novel proteasome-associated factor.New ATPase regulators--p97 goes to the PUB.Transferring substrates to the 26S proteasome.Single site suppressors of a fission yeast temperature-sensitive mutant in cdc48 identified by whole genome sequencing.UBA domain containing proteins in fission yeast.Human ASPL/TUG interacts with p97 and complements the proteasome mislocalization of a yeast ubx4 mutant, but not the ER-associated degradation defect.Proteasomes: a complex story.Integral UBL domain proteins: a family of proteasome interacting proteins.DSS1/Sem1, a Multifunctional and Intrinsically Disordered Protein.A Two-step Protein Quality Control Pathway for a Misfolded DJ-1 Variant in Fission YeastHigh-Throughput siRNA Screening Applied to the Ubiquitin-Proteasome System.Ubiquitin-binding proteins: similar, but different.Predicting the impact of Lynch syndrome-causing missense mutations from structural calculationsRedox control of the ubiquitin-proteasome system: from molecular mechanisms to functional significance.The Ku70/80 ring in Non-Homologous End-Joining: easy to slip on, hard to remove.Bioinformatics analysis identifies several intrinsically disordered human E3 ubiquitin-protein ligases.Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S proteasomeCell-cycle-dependent regulation of cell motility and determination of the role of Rac1.Effects of taurine depletion on cell migration and NCAM expression in cultures of dissociated mouse cerebellum and N2A cells.UBL/BAG-domain co-chaperones cause cellular stress upon overexpression through constitutive activation of Hsf1.Dss1 is a 26S proteasome ubiquitin receptor.Interaction of the anaphase-promoting complex/cyclosome and proteasome protein complexes with multiubiquitin chain-binding proteins.The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and nonproteolytic ubiquitin-dependent processes.Mass spectrometry analyses of normal and polyglutamine expanded ataxin-3 reveal novel interaction partners involved in mitochondrial function.Characterisation of the nascent polypeptide-associated complex in fission yeast.Blocking protein quality control to counter hereditary cancers.
P50
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Rasmus Hartmann-Petersen
@ast
Rasmus Hartmann-Petersen
@en
Rasmus Hartmann-Petersen
@es
Rasmus Hartmann-Petersen
@nl
Rasmus Hartmann-Petersen
@sl
type
label
Rasmus Hartmann-Petersen
@ast
Rasmus Hartmann-Petersen
@en
Rasmus Hartmann-Petersen
@es
Rasmus Hartmann-Petersen
@nl
Rasmus Hartmann-Petersen
@sl
prefLabel
Rasmus Hartmann-Petersen
@ast
Rasmus Hartmann-Petersen
@en
Rasmus Hartmann-Petersen
@es
Rasmus Hartmann-Petersen
@nl
Rasmus Hartmann-Petersen
@sl
P1053
K-4434-2014
P106
P21
P31
P3829
P496
0000-0002-4155-7791