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PARP12-catalyzed mono-ADP-ribosylation of Golgin-97 controls the transport of E-cadherin
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/1873-3468.13567openalex-snapshot
Form and function of the Golgi apparatus: scaffolds, cytoskeleton and signalling
inferredcites →https://doi.org/10.1007/978-1-4939-8588-3_3openalex-snapshot
In Vitro Techniques for ADP-Ribosylated Substrate Identification
inferredcites →https://doi.org/10.1007/s00018-009-0190-4openalex-snapshot
Visualization of subcellular NAD pools and intra-organellar protein localization by poly-ADP-ribose formation
inferredcites →https://doi.org/10.1007/s12032-017-0980-8openalex-snapshot
Epithelial-to-mesenchymal transition in tumor progression
inferredcites →https://doi.org/10.1016/j.bcp.2019.03.028openalex-snapshot
Mitotic functions of poly(ADP-ribose) polymerases
inferredcites →https://doi.org/10.1016/j.bcp.2019.05.019openalex-snapshot
PARPs and PAR as novel pharmacological targets for the treatment of stress granule-associated disorders
inferredcites →https://doi.org/10.1016/j.canlet.2003.07.007openalex-snapshot
Loss of E-cadherin expression correlates with poor differentiation and invasion into adjacent organs in gastric adenocarcinomas
inferredcites →https://doi.org/10.1016/j.cell.2011.02.013openalex-snapshot
Hallmarks of Cancer: The Next Generation
inferredcites →https://doi.org/10.1016/j.celrep.2018.07.083openalex-snapshot
Systems-wide Analysis of Serine ADP-Ribosylation Reveals Widespread Occurrence and Site-Specific Overlap with Phosphorylation
inferredcites →https://doi.org/10.1016/j.molcel.2009.11.020openalex-snapshot
Eukaryotic Stress Granules: The Ins and Outs of Translation
inferredcites →https://doi.org/10.1016/j.molcel.2011.04.015openalex-snapshot
Poly(ADP-Ribose) Regulates Stress Responses and MicroRNA Activity in the Cytoplasm
inferredcites →https://doi.org/10.1016/j.molcel.2017.01.003openalex-snapshot
Serine ADP-Ribosylation Depends on HPF1
inferredcites →https://doi.org/10.1016/j.tibs.2009.12.003openalex-snapshot
Toward a unified nomenclature for mammalian ADP-ribosyltransferases
inferredcites →https://doi.org/10.1016/s0021-9258(17)40578-3openalex-snapshot
Mechanism of action of choleragen. Evidence for ADP-ribosyltransferase activity with arginine as an acceptor.
inferredcites →https://doi.org/10.1016/s0092-8674(00)80225-1openalex-snapshot
The Vesicle Docking Protein p115 Binds GM130, a cis-Golgi Matrix Protein, in a Mitotically Regulated Manner
inferredcites →https://doi.org/10.1016/s0092-8674(00)81737-7openalex-snapshot
Cdc2 Kinase Directly Phosphorylates the cis-Golgi Matrix Protein GM130 and Is Required for Golgi Fragmentation in Mitosis
inferredcites →https://doi.org/10.1016/s0169-5002(01)00471-8openalex-snapshot
The E-cadherin cell–cell adhesion complex and lung cancer invasion, metastasis, and prognosis
inferredcites →https://doi.org/10.1016/s1054-3589(08)60277-xopenalex-snapshot
Mono-ADP-ribosylation: A Reversible Posttranslational Modification of Proteins
inferredcites →https://doi.org/10.1023/a:1006924514074openalex-snapshot
Characterization of NAD:arginine ADP-ribosyltransferases
inferredcites →https://doi.org/10.1038/cr.2012.52openalex-snapshot
The Axin/TNKS complex interacts with KIF3A and is required for insulin-stimulated GLUT4 translocation
inferredcites →https://doi.org/10.1038/nbt0303-255openalex-snapshot
Proteomic analysis of post-translational modifications
inferredcites →https://doi.org/10.1038/ncb1322openalex-snapshot
Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function
inferredcites →https://doi.org/10.1038/ncb2445openalex-snapshot
A 14-3-3γ dimer-based scaffold bridges CtBP1-S/BARS to PI(4)KIIIβ to regulate post-Golgi carrier formation
inferredcites →https://doi.org/10.1038/ncb2593openalex-snapshot
PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1α-mediated unfolded protein response
inferredcites →https://doi.org/10.1038/ncb3627openalex-snapshot
TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at the trans-Golgi
inferredcites →https://doi.org/10.1038/nchembio.2568openalex-snapshot
Insights into the biogenesis, function, and regulation of ADP-ribosylation
inferredcites →https://doi.org/10.1038/ncomms12148openalex-snapshot
Golgi membrane fission requires the CtBP1-S/BARS-induced activation of lysophosphatidic acid acyltransferase δ
inferredcites →https://doi.org/10.1038/ncomms5426openalex-snapshot
Family-wide analysis of poly(ADP-ribose) polymerase activity
inferredcites →https://doi.org/10.1038/nmeth.1928openalex-snapshot
Synchronization of secretory protein traffic in populations of cells
inferredcites →https://doi.org/10.1038/s41467-017-02253-1openalex-snapshot
Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase
inferredcites →https://doi.org/10.1038/s41598-017-14156-8openalex-snapshot
PARP1-produced poly-ADP-ribose causes the PARP12 translocation to stress granules and impairment of Golgi complex functions
inferredcites →https://doi.org/10.1042/bj20020660openalex-snapshot
Endogenous mono-ADP-ribosylation of the free Gβγ prevents stimulation of phosphoinositide 3-kinase-γ and phospholipase C-β2 and is activated by G-protein-coupled receptors
inferredcites →https://doi.org/10.1042/bj20050885openalex-snapshot
NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis
inferredcites →https://doi.org/10.1042/bj20060793openalex-snapshot
Insulin-stimulated exocytosis of GLUT4 is enhanced by IRAP and its partner tankyrase
inferredcites →https://doi.org/10.1042/bj3230173openalex-snapshot
Cell-surface ADP-ribosylation of fibroblast growth factor-2 by an arginine-specific ADP-ribosyltransferase
inferredcites →https://doi.org/10.1042/bst0300963openalex-snapshot
Stress granules: sites of mRNA triage that regulate mRNA stability and translatability
inferredcites →https://doi.org/10.1042/bst20180416openalex-snapshot
ADP-ribosylation and intracellular traffic: an emerging role for PARP enzymes
inferredcites →https://doi.org/10.1073/pnas.0800137105openalex-snapshot
A trans -Golgi network golgin is required for the regulated secretion of TNF in activated macrophages in vivo
inferredcites →https://doi.org/10.1073/pnas.0900066106openalex-snapshot
Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome
inferredcites →https://doi.org/10.1074/jbc.275.13.9418openalex-snapshot
Endogenous ADP-ribosylation of the G Protein β Subunit Prevents the Inhibition of Type 1 Adenylyl Cyclase
inferredcites →https://doi.org/10.1074/jbc.m007635200openalex-snapshot
Tankyrase Is a Golgi-associated Mitogen-activated Protein Kinase Substrate That Interacts with IRAP in GLUT4 Vesicles
inferredcites →https://doi.org/10.1074/jbc.m110.112466openalex-snapshot
Mono-ADP-ribosylation of the G Protein βγ Dimer Is Modulated by Hormones and Inhibited by Arf6
inferredcites →https://doi.org/10.1074/jbc.m114.589515openalex-snapshot
PARP12, an Interferon-stimulated Gene Involved in the Control of Protein Translation and Inflammation
inferredcites →https://doi.org/10.1074/jbc.ra117.001058openalex-snapshot
Tankyrase modulates insulin sensitivity in skeletal muscle cells by regulating the stability of GLUT4 vesicle proteins
inferredcites →https://doi.org/10.1083/jcb.201402114openalex-snapshot
Poly(ADP-ribose): An organizer of cellular architecture
inferredcites →https://doi.org/10.1083/jcb.201707172openalex-snapshot
Segregation in the Golgi complex precedes export of endolysosomal proteins in distinct transport carriers
inferredcites →https://doi.org/10.1084/jem.129.1.1openalex-snapshot
STUDIES ON THE MODE OF ACTION OF DIPHTHERIA TOXIN
inferredcites →https://doi.org/10.1091/mbc.e03-01-0033openalex-snapshot
Mechanism of Constitutive Export from the Golgi: Bulk Flow via the Formation, Protrusion, and En Bloc Cleavage of largetrans-Golgi Network Tubular Domains
inferredcites →https://doi.org/10.1091/mbc.e09-06-0477openalex-snapshot
Interaction between Poly(ADP-ribose) and NuMA Contributes to Mitotic Spindle Pole Assembly
inferredcites →https://doi.org/10.1091/mbc.e10-04-0313openalex-snapshot
FIP1/RCP Binding to Golgin-97 Regulates Retrograde Transport from Recycling Endosomes to thetrans-Golgi Network
inferredcites →https://doi.org/10.1093/bioinformatics/bty159openalex-snapshot
ADPredict: ADP-ribosylation site prediction based on physicochemical and structural descriptors
inferredcites →https://doi.org/10.1093/emboj/cdg209openalex-snapshot
Functional aspects of protein mono‐ADP‐ribosylation
inferredcites →https://doi.org/10.1101/841965openalex-snapshot
Determining the content of vesicles captured by golgin tethers using LOPIT-DC
inferredcites →https://doi.org/10.1101/cshperspect.a029140openalex-snapshot
Adherens Junctions on the Move—Membrane Trafficking of E-Cadherin
inferredcites →https://doi.org/10.1101/gad.183509.111openalex-snapshot
On PAR with PARP: cellular stress signaling through poly(ADP-ribose) and PARP-1
inferredcites →https://doi.org/10.1101/gad.291518.116openalex-snapshot
PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes
inferredcites →https://doi.org/10.1111/j.1600-0854.2005.00349.xopenalex-snapshot
E‐Cadherin Transport from the trans‐Golgi Network in Tubulovesicular Carriers is Selectively Regulated by Golgin‐97
inferredcites →https://doi.org/10.1111/j.1742-4658.2005.04876.xopenalex-snapshot
Physiological relevance of the endogenous mono(ADP‐ribosyl)ation of cellular proteins
inferredcites →https://doi.org/10.1111/tra.12448openalex-snapshot
Cadherin tales: Regulation of cadherin function by endocytic membrane trafficking
inferredcites →https://doi.org/10.1126/science.1256898openalex-snapshot
The specificity of vesicle traffic to the Golgi is encoded in the golgin coiled-coil proteins
inferredcites →https://doi.org/10.1126/scisignal.aas9332openalex-snapshot
PARP12 suppresses Zika virus infection through PARP-dependent degradation of NS1 and NS3 viral proteins
inferredcites →https://doi.org/10.1128/jvi.00733-12openalex-snapshot
New PARP Gene with an Anti-Alphavirus Function
inferredcites →https://doi.org/10.1128/jvi.03443-13openalex-snapshot
Interferon-Stimulated Poly(ADP-Ribose) Polymerases Are Potent Inhibitors of Cellular Translation and Virus Replication
inferredcites →https://doi.org/10.1128/mcb.25.1.389-402.2005openalex-snapshot
Lysosomal Targeting of E-Cadherin: a Unique Mechanism for the Down-Regulation of Cell-Cell Adhesion during Epithelial to Mesenchymal Transitions
inferredcites →https://doi.org/10.1186/1471-2164-6-139openalex-snapshot
In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)
inferredcites →https://doi.org/10.1186/s12915-016-0345-3openalex-snapshot
The golgin coiled-coil proteins capture different types of transport carriers via distinct N-terminal motifs
inferredcites →https://doi.org/10.1371/journal.pone.0037352openalex-snapshot
PARP16/ARTD15 Is a Novel Endoplasmic-Reticulum-Associated Mono-ADP-Ribosyltransferase That Interacts with, and Modifies Karyopherin-ß1
inferredcites →https://doi.org/10.2147/cmar.s225606openalex-snapshot
Genetic And Epigenetic Regulation Of E-Cadherin Signaling In Human Hepatocellular Carcinoma
inferredcites →https://doi.org/10.2174/0929867043455611openalex-snapshot
Ecto-ADP-Ribosyltransferases (ARTs): Emerging Actors in Cell Communication and Signaling
inferredcites →https://doi.org/10.2741/2909openalex-snapshot
The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases
inferredcites →https://doi.org/10.3389/fcell.2015.00086openalex-snapshot
The Golgin Family of Coiled-Coil Tethering Proteins
inferredcites →https://doi.org/10.3389/fcell.2016.00018openalex-snapshot
Transport Vesicle Tethering at the Trans Golgi Network: Coiled Coil Proteins in Action
inferredcites →https://doi.org/10.3389/fcell.2019.00094openalex-snapshot
The Physiological Functions of the Golgin Vesicle Tethering Proteins
inferredcites →https://doi.org/10.3390/cells9041040openalex-snapshot
E-Cadherin in Pancreatic Ductal Adenocarcinoma: A Multifaceted Actor during EMT
inferredcites →https://doi.org/10.7554/elife.02009openalex-snapshot
Transport of soluble proteins through the Golgi occurs by diffusion via continuities across cisternae
inferredcites →https://doi.org/10.7554/elife.02009.025openalex-snapshot
Author response: Transport of soluble proteins through the Golgi occurs by diffusion via continuities across cisternae
inferredcites →https://doi.org/10.7554/elife.28533openalex-snapshot
Serine ADP-ribosylation reversal by the hydrolase ARH3
inferredcites →https://doi.org/10.7554/elife.28533.016openalex-snapshot
Author response: Serine ADP-ribosylation reversal by the hydrolase ARH3
inferredcites →https://doi.org/10.7554/elife.34334openalex-snapshot
Serine is the major residue for ADP-ribosylation upon DNA damage
inferredcites →https://doi.org/10.7554/elife.34334.011openalex-snapshot
Author response: Serine is the major residue for ADP-ribosylation upon DNA damage
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1007/978-1-0716-2891-1_9openalex-snapshot
Immunoprecipitation Using Mono-ADP-Ribosylation-Specific Antibodies
inferred← citeshttps://doi.org/10.1042/bst20201212openalex-snapshot
Host ADP-ribosylation and the SARS-CoV-2 macrodomain
inferred← citeshttps://doi.org/10.1093/protein/gzac006openalex-snapshot
Protein engineering approach to enhance activity assays of mono-ADP-ribosyltransferases through proximity
inferred← citeshttps://doi.org/10.2147/cmar.s303064openalex-snapshot
Analysis of Mono-ADP-Ribosylation Levels in Human Colorectal Cancer
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