Evidence map›Paper›PMID 40148320›Full record

ArticleNature communications2025

Molecular basis for the regulation of human phosphorylase kinase by phosphorylation and Ca

Ruifang Ma, Bowen Du, Chen Shi, Lei Wang, Fuxing Zeng, Jie Han, Huiyi Guan, Yong Wang, Kaige Yan

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    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

9 authors.

Ruifang Ma *Shenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology, Shenzhen, 518055, China.ORCID http://orcid.org/0000-0002-3663-2240
Bowen Du *Shenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology, Shenzhen, 518055, China.ORCID http://orcid.org/0009-0007-5714-7280
Chen Shi *College of Life Sciences, Zhejiang University, Hangzhou, 310058, China.ORCID http://orcid.org/0009-0008-5239-6234
Lei WangShenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology, Shenzhen, 518055, China.ORCID http://orcid.org/0000-0001-8044-7184
Fuxing ZengDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, 518055, China.ORCID http://orcid.org/0000-0003-0790-0151
Jie HanShenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology, Shenzhen, 518055, China.ORCID http://orcid.org/0009-0008-6564-6845
Huiyi GuanShenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology, Shenzhen, 518055, China.
Yong WangCollege of Life Sciences, Zhejiang University, Hangzhou, 310058, China. yongwang_isb@zju.edu.cn.ORCID http://orcid.org/0000-0001-9156-0377
Kaige YanShenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology, Shenzhen, 518055, China. yankg@sustech.edu.cn.ORCID http://orcid.org/0000-0003-4176-5109

Funding

China Postdoctoral Science Foundation 2022M721477Guangdong Innovative and Entrepreneurial Research Team Program 2021QN02Y429Guangdong Innovative and Entrepreneurial Research Team Program 2021ZT09Y104National Natural Science Foundation of China (National Science Foundation of China) 32271251National Natural Science Foundation of China (National Science Foundation of China) 32371300Shenzhen Science and Technology Innovation Commission 20231120160100001Shenzhen Science and Technology Innovation Commission JCYJ20220530115214033Shenzhen Science and Technology Innovation Commission KQTD20210811090115021
6 · The paper itself

Abstract

Phosphorylase kinase (PhK) regulates the degradation of glycogen by integrating diverse signals, providing energy to the organism. Dysfunctional mutations may directly lead to Glycogen Storage Disease type IX (GSD IX), whereas the abnormal expression of PhK is also associated with tumors. Here, we use cryo-electron microscopy (cryo-EM) to resolve its near-atomic structures in the inactive and active states. These structures reveal the interactions and relative locations of the four subunits (αβγδ) within the PhK complex. Phosphorylated α and β subunits induce PhK to present a more compact state, while Ca

Indexed as

CalciumPhosphorylase KinaseCryoelectron MicroscopyGlycogen PhosphorylaseGlycogen Storage DiseaseHumansModels, MolecularPhosphorylationProtein BindingProtein SubunitsCalciumGlycogen PhosphorylasePhosphorylase KinaseProtein Subunits

Identifiers

PMID40148320
PMCPMC11950179

What Socratic 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 Socratic graph.