Evidence map›Paper›PMID 34969853›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

PKD-dependent PARP12-catalyzed mono-ADP-ribosylation of Golgin-97 is required for E-cadherin transport from Golgi to plasma membrane.

Giovanna Grimaldi, Angela Filograna, Laura Schembri, Matteo Lo Monte, Rosaria Di Martino, Marinella Pirozzi, Daniela Spano, Andrea R Beccari, Seetharaman Parashuraman, Alberto Luini and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 29 citations in OpenAlex.

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  15. microPublication biology · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 1 country.

Giovanna GrimaldiInstitute for Endocrinology and Experimental Oncology "G. Salvatore," National Research Council, 80131 Naples, Italy; g.grimaldi@ieos.cnr.it a.luini@ieos.cnr.it c.valente@ieos.cnr.it daniela.corda@cnr.it.ORCID 0000-0003-0134-7869
Angela FilogranaInstitute for Endocrinology and Experimental Oncology "G. Salvatore," National Research Council, 80131 Naples, Italy.ORCID 0000-0002-0175-0415
Laura SchembriInstitute of Biochemistry and Cell Biology, National Research Council, 80131 Naples, Italy.
Matteo Lo MonteInstitute for Endocrinology and Experimental Oncology "G. Salvatore," National Research Council, 80131 Naples, Italy.
Rosaria Di MartinoInstitute for Endocrinology and Experimental Oncology "G. Salvatore," National Research Council, 80131 Naples, Italy.
Marinella PirozziInstitute for Endocrinology and Experimental Oncology "G. Salvatore," National Research Council, 80131 Naples, Italy.
Daniela SpanoInstitute of Biochemistry and Cell Biology, National Research Council, 80131 Naples, Italy.ORCID 0000-0003-3567-6492
Andrea R BeccariDrug Discovery Platform, Dompé Farmaceutici SpA Research Center, 67100 L'Aquila, Italy.ORCID 0000-0001-6830-2695
Seetharaman ParashuramanInstitute for Endocrinology and Experimental Oncology "G. Salvatore," National Research Council, 80131 Naples, Italy.
Alberto LuiniInstitute for Endocrinology and Experimental Oncology "G. Salvatore," National Research Council, 80131 Naples, Italy; g.grimaldi@ieos.cnr.it a.luini@ieos.cnr.it c.valente@ieos.cnr.it daniela.corda@cnr.it.
Carmen ValenteInstitute for Endocrinology and Experimental Oncology "G. Salvatore," National Research Council, 80131 Naples, Italy; g.grimaldi@ieos.cnr.it a.luini@ieos.cnr.it c.valente@ieos.cnr.it daniela.corda@cnr.it.ORCID 0000-0002-6244-9108
Daniela CordaDepartment of Biomedical Sciences, National Research Council, 00185 Rome, Italy g.grimaldi@ieos.cnr.it a.luini@ieos.cnr.it c.valente@ieos.cnr.it daniela.corda@cnr.it.ORCID 0000-0002-3614-751X
Institute for Experimental Endocrinology and Oncology · ITNational Research Council · ITDompé (Italy) · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adenosine diphosphate (ADP)-ribosylation is a posttranslational modification involved in key regulatory events catalyzed by ADP-ribosyltransferases (ARTs). Substrate identification and localization of the mono-ADP-ribosyltransferase PARP12 at the

Indexed as

ADP-RibosylationAntigens, CDAutoantigensCadherinsCatalysisCell MembraneGolgi ApparatusGolgi Matrix ProteinsHeLa CellsHumansPoly(ADP-ribose) PolymerasesProtein Kinase CProtein Transporttrans-Golgi NetworkTumor Necrosis Factor-alphaAntigens, CDAutoantigensCadherinsCDH1 protein, humanGolgi complex autoantigen, 97-kDaGolgi Matrix ProteinsPoly(ADP-ribose) PolymerasesProtein Kinase Cprotein kinase DTumor Necrosis Factor-alphaE-cadherinGolgin-97 ADP-ribosylationintracellular membrane transportPARP12PKD

Identifiers

PMID34969853
PMCPMC8740581
OpenAlexW4206378575

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.