Evidence map›Paper›PMID 30670591›Full record

ArticleThe Journal of biological chemistry2019

A cytosolic chaperone complex controls folding and degradation of type III CD38.

Yang Wu, Jingzi Zhang, Lei Fang, Hon Cheung Lee, Yong Juan Zhao

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
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

11 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Resolving the topological enigma in CaThe Journal of biological chemistry · 2019
    Review
  11. Article
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

5 authors.

Yang WuFrom the State Key Laboratory of Chemical Oncogenomics, Key Laboratory of Chemical Genomics, Peking University Shenzhen Graduate School, Shenzhen, China, 518055 and.
Jingzi ZhangJiangsu Key Laboratory of Molecular Medicine, Medical School of Nanjing University, Nanjing, Jiangsu Province, China, 210093.
Lei FangJiangsu Key Laboratory of Molecular Medicine, Medical School of Nanjing University, Nanjing, Jiangsu Province, China, 210093 njfanglei@nju.edu.cn.
Hon Cheung LeeFrom the State Key Laboratory of Chemical Oncogenomics, Key Laboratory of Chemical Genomics, Peking University Shenzhen Graduate School, Shenzhen, China, 518055 and leehoncheung@gmail.com.
Yong Juan ZhaoFrom the State Key Laboratory of Chemical Oncogenomics, Key Laboratory of Chemical Genomics, Peking University Shenzhen Graduate School, Shenzhen, China, 518055 and zhaoyongjuan@pku.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cluster of differentiation 38 (CD38) is the best-studied enzyme catalyzing the synthesis of the Ca

Indexed as

Protein FoldingADP-ribosyl Cyclase 1CytosolHEK293 CellsHumansMembrane GlycoproteinsADP-ribosyl Cyclase 1CD38 protein, humanMembrane GlycoproteinsCD38chaperonecyclic ADP ribose (cADPR)cytosolic soluble CD38heat shock protein 90 (Hsp90)heat shock protein (HSP)hsp70Hsp70-interacting protein (Hip)lysosomal degradationprotein degradationprotein foldingtype III CD38

Identifiers

PMID30670591
PMCPMC6422091

What OpenQuestion holds

Textmetadata
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.