Evidence map›Paper›PMID 29234076›Full record

ArticleScientific reports2017

Molecular mechanism of K65 acetylation-induced attenuation of Ubc9 and the NDSM interaction.

Mandar T Naik, Mooseok Kang, Chun-Chen Ho, Pei-Hsin Liao, Yung-Lin Hsieh, Nandita M Naik, Szu-Huan Wang, Iksoo Chang, Hsiu-Ming Shih, Tai-Huang Huang

Erratum issuedOpen access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 86% 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

0 citing papers in PubMed, 2 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 4 institutions in 3 countries.

Mandar T NaikInstitute of Biomedical Sciences, Academia Sinica, Taipei, 11529, Taiwan.
Mooseok KangDepartment of Physics, Pusan National University, Busan, 46241, Korea.
Chun-Chen HoInstitute of Biomedical Sciences, Academia Sinica, Taipei, 11529, Taiwan.
Pei-Hsin LiaoInstitute of Biomedical Sciences, Academia Sinica, Taipei, 11529, Taiwan.
Yung-Lin HsiehInstitute of Biomedical Sciences, Academia Sinica, Taipei, 11529, Taiwan.
Nandita M NaikInstitute of Biomedical Sciences, Academia Sinica, Taipei, 11529, Taiwan.
Szu-Huan WangInstitute of Biomedical Sciences, Academia Sinica, Taipei, 11529, Taiwan.
Iksoo ChangCenter for Proteome Biophysics, Department of Brain and Cognitive Sciences, DGIST, Daegu, 42988, Korea. iksoochang@dgist.ac.kr.
Hsiu-Ming ShihInstitute of Biomedical Sciences, Academia Sinica, Taipei, 11529, Taiwan. hmshih@ibms.sinica.edu.tw.
Tai-Huang HuangInstitute of Biomedical Sciences, Academia Sinica, Taipei, 11529, Taiwan. taihuanghuang@gmail.com.
Institute of Biomedical Sciences, Academia Sinica · TWDaegu Gyeongbuk Institute of Science and Technology · KRNational Health Research Institutes · TWPusan National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The negatively charged amino acid-dependent sumoylation motif (NDSM) carries an additional stretch of acidic residues downstream of the consensus Ψ-K-x-E/D sumoylation motif. We have previously shown that acetylation of the SUMO E2 conjugase enzyme, Ubc9, at K65 downregulates its binding to the NDSM and renders a selective decrease in sumoylation of substrates with the NDSM motif. Here, we provide detailed structural, thermodynamic, and kinetics results of the interactions between Ubc9 and its K65 acetylated variant (Ac-Ubc9

Indexed as

Protein Interaction Domains and MotifsProtein Processing, Post-TranslationalAcetylationCalpainets-Domain Protein Elk-1HumansKineticsMolecular Dynamics SimulationPeptide FragmentsProtein BindingSialoglycoproteinsThermodynamicsUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9bone sialoprotein (35-62), humanCalpainCAPN2 protein, humanELK1 protein, humanets-Domain Protein Elk-1Peptide FragmentsSialoglycoproteinsUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9

Identifiers

PMID29234076
PMCPMC5727262
OpenAlexW2771546925

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.