Evidence map›Paper›PMID 36077334›Full record

ReviewInternational journal of molecular sciences2022

NEDD4 E3 Ligases: Functions and Mechanisms in Bone and Tooth.

Ke Xu, Yanhao Chu, Qin Liu, Wenguo Fan, Hongwen He, Fang Huang

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Regulation of Ubiquitin Family Signaling in Disease.International journal of molecular sciences · 2023
    Article
  13. Review
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

6 authors at 2 institutions in 1 country.

Ke XuHospital of Stomatology, Guanghua School of Stomatology, Sun Yat-sen University, Guangzhou 510008, China.
Yanhao ChuHospital of Stomatology, Guanghua School of Stomatology, Sun Yat-sen University, Guangzhou 510008, China.
Qin LiuHospital of Stomatology, Guanghua School of Stomatology, Sun Yat-sen University, Guangzhou 510008, China.
Wenguo FanHospital of Stomatology, Guanghua School of Stomatology, Sun Yat-sen University, Guangzhou 510008, China.
Hongwen HeGuangdong Provincial Key Laboratory of Stomatology, Guangzhou 510008, China.
Fang HuangHospital of Stomatology, Guanghua School of Stomatology, Sun Yat-sen University, Guangzhou 510008, China.
Stomatology Hospital · CNSun Yat-sen University · CN

Funding

National Natural Science Foundation of China 81870737Natural Science Foundation of Guangdong Province 2021A1515011779
6 · The paper itself

Abstract

Protein ubiquitination is a precisely controlled enzymatic cascade reaction belonging to the post-translational modification of proteins. In this process, E3 ligases catalyze the binding of ubiquitin (Ub) to protein substrates and define specificity. The neuronally expressed developmentally down-regulated 4 (NEDD4) subfamily, belonging to the homology to E6APC terminus (HECT) class of E3 ligases, has recently emerged as an essential determinant of multiple cellular processes in different tissues, including bone and tooth. Here, we place special emphasis on the regulatory role of the NEDD4 subfamily in the molecular and cell biology of osteogenesis. We elucidate in detail the specific roles, downstream substrates, and upstream regulatory mechanisms of the NEDD4 subfamily. Further, we provide an overview of the involvement of E3 ligases and deubiquitinases in the development, repair, and regeneration of another mineralized tissue-tooth.

Indexed as

UbiquitinUbiquitin-Protein LigasesEndosomal Sorting Complexes Required for TransportNedd4 Ubiquitin Protein LigasesProtein Structure, TertiaryUbiquitinationEndosomal Sorting Complexes Required for TransportNedd4 Ubiquitin Protein LigasesUbiquitinUbiquitin-Protein LigasesNEDD4 subfamilyosteogenesisSmurf1toothubiquitination

Identifiers

PMID36077334
PMCPMC9455957
OpenAlexW4294253191

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.