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The NEDD8 cycle controlled by NEDP1 upon DNA damage is a regulatory module of the HSP70 ATPase activity

https://doi.org/10.1101/583864
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Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/hep.22159openalex-snapshot
Loss of the glycine N‐methyltransferase gene leads to steatosis and hepatocellular carcinoma in mice†
inferredcites →https://doi.org/10.1007/978-1-4614-4015-4_9openalex-snapshot
Germ Cell Apoptosis and DNA Damage Responses
inferredcites →https://doi.org/10.1007/s00018-004-4464-6openalex-snapshot
Hsp70 chaperones: Cellular functions and molecular mechanism
inferredcites →https://doi.org/10.1007/s13238-017-0455-xopenalex-snapshot
NEDDylation antagonizes ubiquitination of proliferating cell nuclear antigen and regulates the recruitment of polymerase η in response to oxidative DNA damage
inferredcites →https://doi.org/10.1016/j.cbpa.2012.12.024openalex-snapshot
Ubiquitin — omics reveals novel networks and associations with human disease
inferredcites →https://doi.org/10.1016/j.cell.2010.03.017openalex-snapshot
Crystal Structure of the Caenorhabditis elegans Apoptosome Reveals an Octameric Assembly of CED-4
inferredcites →https://doi.org/10.1016/j.cell.2010.03.029openalex-snapshot
Reconstitution of the RIG-I Pathway Reveals a Signaling Role of Unanchored Polyubiquitin Chains in Innate Immunity
inferredcites →https://doi.org/10.1016/j.cell.2012.11.002openalex-snapshot
An Interdomain Energetic Tug-of-War Creates the Allosterically Active State in Hsp70 Molecular Chaperones
inferredcites →https://doi.org/10.1016/j.molcel.2007.08.022openalex-snapshot
Structural Basis of J Cochaperone Binding and Regulation of Hsp70
inferredcites →https://doi.org/10.1016/j.molcel.2009.09.023openalex-snapshot
A Small Molecule Inhibitor of Inducible Heat Shock Protein 70
inferredcites →https://doi.org/10.1016/j.molcel.2010.11.011openalex-snapshot
Systematic In Vivo RNAi Analysis Identifies IAPs as NEDD8-E3 Ligases
inferredcites →https://doi.org/10.1016/j.molcel.2012.09.023openalex-snapshot
Structure and Dynamics of the ATP-Bound Open Conformation of Hsp70 Chaperones
inferredcites →https://doi.org/10.1016/j.molcel.2013.01.006openalex-snapshot
RNF111-Dependent Neddylation Activates DNA Damage-Induced Ubiquitination
inferredcites →https://doi.org/10.1016/j.molcel.2013.01.017openalex-snapshot
Regulation of DNA Damage Responses by Ubiquitin and SUMO
inferredcites →https://doi.org/10.1016/j.molcel.2013.01.028openalex-snapshot
The Colossus of Ubiquitylation: Decrypting a Cellular Code
inferredcites →https://doi.org/10.1016/j.molcel.2013.08.016openalex-snapshot
Proteasomes Activate Aggresome Disassembly and Clearance by Producing Unanchored Ubiquitin Chains
inferredcites →https://doi.org/10.1016/j.molcel.2015.02.020openalex-snapshot
Quantifying Ubiquitin Signaling
inferredcites →https://doi.org/10.1016/j.tcb.2014.01.005openalex-snapshot
Crosstalk between ubiquitin and other post-translational modifications on chromatin during double-strand break repair
inferredcites →https://doi.org/10.1016/s0962-8924(00)01874-2openalex-snapshot
Stress management – heat shock protein-70 and the regulation of apoptosis
inferredcites →https://doi.org/10.1038/35019501openalex-snapshot
Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome
inferredcites →https://doi.org/10.1038/35019510openalex-snapshot
Negative regulation of the Apaf-1 apoptosome by Hsp70
inferredcites →https://doi.org/10.1038/embor.2008.10openalex-snapshot
Ribosomal proteins are targets for the NEDD8 pathway
inferredcites →https://doi.org/10.1038/embor.2009.178openalex-snapshot
Regulation of nucleolar signalling to p53 through NEDDylation of L11
inferredcites →https://doi.org/10.1038/nbt.1654openalex-snapshot
Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling
inferredcites →https://doi.org/10.1038/nm.3739openalex-snapshot
Ubiquitination in disease pathogenesis and treatment
inferredcites →https://doi.org/10.1038/nmeth.1679openalex-snapshot
Stable-isotope labeling with amino acids in nematodes
inferredcites →https://doi.org/10.1038/nprot.2009.128openalex-snapshot
Detection of protein SUMOylation in vivo
inferredcites →https://doi.org/10.1038/nrm1836openalex-snapshot
Developmental apoptosis in C. elegans: a complex CEDnario
inferredcites →https://doi.org/10.1038/nrm3919openalex-snapshot
Protein neddylation: beyond cullin–RING ligases
inferredcites →https://doi.org/10.1038/onc.2009.314openalex-snapshot
Chemotherapy induces NEDP1-mediated destabilization of MDM2
inferredcites →https://doi.org/10.1038/onc.2009.494openalex-snapshot
NUB1 promotes cytoplasmic localization of p53 through cooperation of the NEDD8 and ubiquitin pathways
inferredcites →https://doi.org/10.1038/onc.2011.482openalex-snapshot
Recruitment of RPL11 at promoter sites of p53-regulated genes upon nucleolar stress through NEDD8 and in an Mdm2-dependent manner
inferredcites →https://doi.org/10.1038/onc.2012.428openalex-snapshot
NEDDylation controls the target specificity of E2F1 and apoptosis induction
inferredcites →https://doi.org/10.1038/sj.emboj.7600628openalex-snapshot
Structural basis of NEDD8 ubiquitin discrimination by the deNEDDylating enzyme NEDP1
inferredcites →https://doi.org/10.1038/sj.onc.1204656openalex-snapshot
Different effects of p14ARF on the levels of ubiquitinated p53 and Mdm2 in vivo
inferredcites →https://doi.org/10.1042/bj20111671openalex-snapshot
Changes in the ratio of free NEDD8 to ubiquitin triggers NEDDylation by ubiquitin enzymes
inferredcites →https://doi.org/10.1051/medsci/20031967725openalex-snapshot
C. elegans : des neurones et des gènes
inferredcites →https://doi.org/10.1073/pnas.1111220108openalex-snapshot
Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface
inferredcites →https://doi.org/10.1073/pnas.88.13.5719openalex-snapshot
Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding.
inferredcites →https://doi.org/10.1074/jbc.274.32.22686openalex-snapshot
Caspase Activation Involves the Formation of the Aposome, a Large (∼700 kDa) Caspase-activating Complex
inferredcites →https://doi.org/10.1074/jbc.m111.273730openalex-snapshot
Protein Aggregates Are Recruited to Aggresome by Histone Deacetylase 6 via Unanchored Ubiquitin C Termini
inferredcites →https://doi.org/10.1083/jcb.139.5.1281openalex-snapshot
Movement of Bax from the Cytosol to Mitochondria during Apoptosis
inferredcites →https://doi.org/10.1093/genetics/77.1.71openalex-snapshot
THE GENETICS OF CAENORHABDITIS ELEGANS
inferredcites →https://doi.org/10.1101/gad.13.24.3179openalex-snapshot
Caspase-9 and APAF-1 form an active holoenzyme
inferredcites →https://doi.org/10.1105/tpc.114.135996openalex-snapshot
DENEDDYLASE1 Deconjugates NEDD8 from Non-Cullin Protein Substrates in Arabidopsis thaliana
inferredcites →https://doi.org/10.1126/science.1257037openalex-snapshot
Influenza A virus uses the aggresome processing machinery for host cell entry
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Mechanisms of the Hsp70 chaperone systemThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer…
inferredcites →https://doi.org/10.1242/jcs.073643openalex-snapshot
Regulation of the Apaf-1–caspase-9 apoptosome
inferredcites →https://doi.org/10.1242/jcs.138891openalex-snapshot
RNF168-mediated H2A neddylation antagonizes its ubiquitination and regulates DNA damage repair
inferredcites →https://doi.org/10.1371/journal.pgen.1001025openalex-snapshot
The Caenorhabditis elegans Homolog of Gen1/Yen1 Resolvases Links DNA Damage Signaling to DNA Double-Strand Break Repair
inferredcites →https://doi.org/10.15252/embj.2018100024openalex-snapshot
Unanchored tri‐NEDD8 inhibits PARP‐1 to protect from oxidative stress‐induced cell death
inferredcites →https://doi.org/10.1530/erc-14-0315openalex-snapshot
Regulation of cancer-related pathways by protein NEDDylation and strategies for the use of NEDD8 inhibitors in the clinic
inferredcites →https://doi.org/10.18632/oncotarget.3191openalex-snapshot
Stabilization of LKB1 and Akt by neddylation regulates energy metabolism in liver cancer
inferredcites →https://doi.org/10.21037/tgh.2018.06.05openalex-snapshot
Neddylation, a novel paradigm in liver cancer
inferredcites →https://doi.org/10.4161/cc.11.6.19559openalex-snapshot
The ubiquitin E1 enzyme Ube1 mediates NEDD8 activation under diverse stress conditions
inferredcites →https://doi.org/10.7554/elife.24325openalex-snapshot
SENP8 limits aberrant neddylation of NEDD8 pathway components to promote cullin-RING ubiquitin ligase function
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